Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
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H2KZ60 | RIG6_CAEEL | MMMLIRCISIFLLFGFVNALIDEASCPIGWQIASDQCVRIVIAPANLKHSKKYCHHEGGELMDTSVTLLLEDVMDLLKNLHENGLSEPTFHVGGMGQALNRTEDGNYKIITINPSSHFPFICSLNKMARRSLLFQQKLLPVGAPQISLTGQSEIYFHPRHDADYIALPCTVQGNPKPTVAWYKNDVEVLSPSMSNVSYLLSGGNLLVPASSTLAYSSFHCTARNSLGEVRSPPILLKPSFIDPFRPHRLDVYSLATGGAKLDCDAPAHQPKSLTYSWLYGSSTDRILSQNERKFISLDGTLFFSYVTAEDEDSYACSLSVYSTQSGHYGPFFRLISSTPKLVNSTFPPKLDSTQPQIFPEDPKVGDSIYLECFAYASPLPQYKWSRVDGKPIPARSHISNYGRVLKIEKVNYGDAGKYKCVAMNAFGSAAGEVHVKLRAPPSILQGLHDRLVPTESNVSFECLLSNADSYSSVEWFKDAKPIVPLLLPAEKRKRLKIDHNVLHLKFADETDSGVYQCVASNDVGSSSSSALLTVKDSAPVFPPNAMSRKVFAAFGSTVSIPCIFEASPRFHGKWADAGGSKLPQKGRIRDEEGVISIEKVLHEDAGLFFCTAHNKLGKAHAQVQLIVVNKPSIKTNFLDEETVNMSCEVELTCENSAECPEALFEWKINDRPAKEYPSLKSKVHEKKSGHKGRHLKQKVDLEVPKSLAGSRQIGRFACSSLYGGSSEFVTKPQLPSPIALTVEQMDEDGKKKKMFRLRWRLPPQHRDTRDHSPKVEGYLVELRTRKNRKWRAAERQLVGNMEKDSITVENLLPNTEYQFRVRSVESAAIGEPSIPSDWVKTAPGAPSETIDNLKWRSLDSQTLLVEWQPIEIGQESSGDNLRYRVSWSEATVGKNATDDMKLSNQDDDFENHLDSDQPQAILKLNTTEGCRMVVLAVRPVNDQGNGSVGTDTIAFLNSHGELKKVSLHNVKPINASHVNISWTWDNTSDCDTKHAVQITCINLSGSEISATVASDRIFWMLGGLEAETAYDCDLKAIDNHGSFGPASKKFRIHTKQHPPSETPLIGKLMMKQMKDTYTTILEWSSIELQKPNRTENGCGYKIFIYISETATEAIELDMPLQRLSDRRNPSARLDGLKLMYMYTIKVAGYNPGGIGPISEPRSIRLGSPGTMDYTTGSSDVPIPSLLLLLLLLLWRL | null | null | axon guidance [GO:0007411]; brain development [GO:0007420]; dendrite self-avoidance [GO:0070593]; determination of left/right asymmetry in nervous system [GO:0035545]; dorsal/ventral axon guidance [GO:0033563]; embryo development ending in birth or egg hatching [GO:0009792]; epithelial tube morphogenesis [GO:0060562]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; motor neuron axon guidance [GO:0008045]; negative regulation of defecation rhythm [GO:2000747]; negative regulation of locomotion involved in locomotory behavior [GO:0090327]; negative regulation of multicellular organism growth [GO:0040015]; positive regulation of axon extension involved in axon guidance [GO:0048842]; positive regulation of distal tip cell migration [GO:1903356]; regulation of tube size [GO:0035150] | axon [GO:0030424]; cytoplasm [GO:0005737]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; synapse [GO:0045202] | cell-cell adhesion mediator activity [GO:0098632] | PF00041;PF07679;PF13927; | 2.60.40.10; | Immunoglobulin superfamily, Contactin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Perikaryon {ECO:0000269|PubMed:23123963, ECO:0000269|PubMed:28901288}. Cell projection, axon {ECO:0000269|PubMed:23123963, ECO:0000269|PubMed:28901288}. Synapse {ECO:0000269|PubMed:23123963}. Cytoplasm {ECO:0000269|PubMed:28901288}. | null | null | null | null | null | FUNCTION: Probable cell adhesion protein involved in patterning of the nervous system, playing a role in ALM and PLM touch receptor axon growth and VNC axon navigation (PubMed:23123963). By associating with the transmembrane protein sax-7, mediates axonal interactions to establish synaptic connections between the AVG interneuron and the two PHC sensory neurons (PubMed:28901288). Also required for non-neuronal cell migration in the excretory canal, regulating excretory canal elongation and excretory cell morphogenesis (PubMed:23123963). Plays a role in regulating male mating behavior (PubMed:28901288). {ECO:0000269|PubMed:23123963, ECO:0000269|PubMed:28901288}. | Caenorhabditis elegans |
H2KZB2 | ANKL2_CAEEL | MGRKSAILAVILAIIYFRSNFSKMSNTPVQETEGPVYVAYSMEDMLKSPRDLYKSVKEVAKFVNSAEGKSMSARFKKFGTPREAMDFLAYGDAPTTPKTVPPVAPTEPNSPFSGVNRIQMNEFKKYVEKGDMENFLRLVDSNPRFLVNTGGDVASIVMEGFRYNALHIAAKAGQTEIIAKILELIQNIDFLIRLYGTGADDVTLRKINILDSYLNTPDKGNSDTPLHFASKFGKIGVVRVLTENSATDRTLLNKSGKSALDCAGERYTGEDKDMVQRDIHLAIEGFYVFLHRNPTTGSTQLTVSQKPPATYSTSPTTATVTVSAQAGPFFTEREARDFAKSWQTAGKELKRTDFDKGWERVGRVLAEQSEAMWRETWHFLGSMELLDLGSEQGLGVLEAFLREKRRGNLRNSEISEISTKKSIFRRGIHARKLDFGILDGEKSAEISENLTPDGSDSADDEDDDDIFYDTFSEIPAAAEKSINDPDDTLGSLTDRFAAISIFSPLPPPPPPQWSNSPNFDYSEGEDSFATPPTTPPPTFVADDEPCKIDNDLFEVLAQISSELISKFPLTQDYVQKLGKLTAHDRSTWRPIDSPARCDSRRKI | null | null | cell division [GO:0051301]; mitotic nuclear membrane reassembly [GO:0007084]; negative regulation of phosphorylation [GO:0042326]; positive regulation of protein dephosphorylation [GO:0035307] | endoplasmic reticulum [GO:0005783]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965] | protein phosphatase 2A binding [GO:0051721] | null | 1.25.40.20; | ANKLE2 family | null | SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:22770216}; Single-pass membrane protein {ECO:0000269|PubMed:22770216}. | null | null | null | null | null | FUNCTION: Involved in mitotic nuclear envelope reassembly by promoting dephosphorylation of baf-1 during mitotic exit. Coordinates the control of baf-1 dephosphorylation by inhibiting VRK1 kinase and promoting dephosphorylation of baf-1 by protein phosphatase 2A (PP2A), thereby facilitating nuclear envelope assembly. It is unclear whether it acts as a real PP2A regulatory subunit or whether it is involved in recruitment of the PP2A complex. {ECO:0000269|PubMed:22770216}. | Caenorhabditis elegans |
H2KZH5 | TOE2_CAEEL | MSSSRHFSIPYDEDVVHSVILENTPSPPPKPPRGILRKEAPMKPQRSALKIEPARDDDKENNSQPQARSQFKAKDTMEQMQSYFKRSISVLRKSEEHFTGAEAADILTAYIETHRNEFPRDNIGRSNAVKLLEIWLESNTIQSVESHQKKFVDSERTFYRLGGDSESLYIVNTPIASRNHDDSASVSRSESSRRSNSIKRLFSPFVRRNRSNSRGRDKDKDNLKDGSSTNLKSTWSLFSSSSEKNEKKLKKAEQQLIKEEEAEVYELSLFHLLSLIDVEFLEDVALPVQDSKNNASFLSSILGKVGLGASEERLDPHQEDHMDLLIETHPLIRDASQWFQMARCCAPLLYFEAKPVASNHKTSHNEQLYLWCRAALDAVKNRLEKMTQNGSSPLFPSEFAPLLTKIAQQLINDMDSGEKLSTAVMYIFLMVPHPIRKTIDQLVQWLQLTMRTDAVEDLRSPYYLGKKDPRRYKENVNVIIGELSSFIFPRGCMTNVQQDIFIETLVELRQKGKLGQRPAQLESSLRAKSVNGQIKWQRKERKHNSLEGDLTPVRYTVRRESIRSKTSKSKDGLNETDSALVTMINSVIDNKELSLTEKKKQLMNFKKFYPKLYNDFFPGMI | null | null | phosphorylation [GO:0016310]; positive regulation of apoptotic process [GO:0043065]; regulation of asymmetric cell division [GO:0009786] | centrosome [GO:0005813]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; midbody [GO:0030496]; nucleus [GO:0005634] | kinase activity [GO:0016301] | null | 1.10.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24961802}. Nucleus {ECO:0000269|PubMed:24961802}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:24961802}. Midbody {ECO:0000269|PubMed:24961802}. Chromosome {ECO:0000269|PubMed:24961802}. Note=Before first cell division of the Q neuroblast lineage, localized diffusely in cytoplasm and concentrated in the nucleus (PubMed:24961802). Around metaphase, localized to the centrosomes and subsequently inherited by both daughter cells (PubMed:24961802). Before anaphase, localized near the region of the membrane that eventually forms the furrow and as anaphase continues, concentrated within the furrow and remains there, eventually localizing to the midbody (PubMed:24961802). During telophase, localized to chromatin (PubMed:24961802). {ECO:0000269|PubMed:24961802}. | null | null | null | null | null | FUNCTION: Involved in promoting a consistent pattern of asymmetric cell division and fate assignment, perhaps by regulating apoptosis of specific cells, including in the Q neuroblast lineage (PubMed:24961802). Downstream target of MAP kinase mpk-1 (PubMed:24961802). {ECO:0000269|PubMed:24961802, ECO:0000303|PubMed:24961802}. | Caenorhabditis elegans |
H2KZM6 | PTPR_CAEEL | MRINRWIWWATVILLYLRTGLAADFFRSSEENDRKSSDDLDNFNSTKIEPDKPKTAKELGVKSCESNQDCVHDGVCHRGNDGHGICMCPRSCPAITPKQCGYNYRTPSTCLLMDADYRSKYDVKEPTCYSRKCVCPPQFDDVHVTANQKPLRLNSTLLPTKCDKRDLAVVARAHPSTSVSKGIDVTLFCCINVDPEGFIDVASVFFIQNGTIMREATSHPFAPRNGLARRVHEKYSCWELEIKNAQTSDSGSYMCRVTASASDLDVTDTMQFEVKAPRQIKNLTVNPSERDAIVTWESEGGEDMAIDLRLVRRTDTRGQVVFSKDNLTSPVSIKDLRAATPYTLFVSGNNGQVPFEFTEHFTTKQKRPFPPKEEDVRVLNSGSALSCEVEWKSPAEPNGRITKYFVSVRGAMRKSDGSLTPDDLPAAVEVDKRCANWDGDENTSKHNGINPIDFANEFYSCKFGPLKPNRNYTVTVWAENSAGRSLPAVFHKNCVTNYAQPDMVETPQPLLSNNHSTFSLTFPQPPDDINGPISCYYIAIVPLPANVSLDILPKSEEIVMHSFSKVFTNNLLPSSAEEKRFFAYIAESYVQLPEETTIGDGVRVSDLKACNVQYLSRYSSEDLALRRGLKYTGFLIVRVDKEEELNRKDVRNGADPNIFRNLIDKSVSPTSRTRTASPMSRHLRQLHLSGPAYGYSAYFKPILLDTESSSSGFGIFMKIILPFLLFLAFATGVTMFFVNRKGHMLSTWCPLFTKMTSKDVVERTLLKQTFGAIPVDDLPTEYVVRHRDTDFLFAQEYESLPHFQLDTVASNRKENAIKNRYNDIRAFDDTRVKLKKINGDDYSDYINANFIKSWKEKKLFIAAQAPVDATIGDFWRMVWEQESYLIVMVANLTEKNRQQCAKYWPDEQITRYGDIIVEPASFSFHSDYAIRAFDIAHIGECGPDVIPNGNGVEYANVPIVKGQFANNSRRILQYHFTNWNDYKAPECSTGLLRFMYRLRELPQFNNSPVVIHCSAGVGRTGTFISIDSMLDQCLAEDKANIFEFVCNLRRQRNLMVQSLEQYVFIYKALAEWHMYGDTDEDVRDFEDHYQRLCASNRDRAVSFNQQSSTNGSISPRVAIVSSRESMTTSNGETGLEEEFKKLERNLTTPLSSNFAAKDENLLKNRYEAAVPFDKYRVILPPTIGHADSSYINASHIKGYFFDYIAAQDPVSEGTAFDFWRMIADQNVTTVVMLSDETDWSDVEKYWPIDGSGTECHFGSERNSVNVTCVSEEHHQDFIIRNLSYSMKDNESMPANQEVVQYSYTGWPSDSIVPKSANSLMNLIEMVLQRQSSLMGSQAPIVVHCRNGSSESGIFICISLLWLRQKAEQRIDVFQTVKGLQSHRPMMFTRFEQYSFCYRALADYISKTYR | 3.1.3.48 | null | chemosensory behavior [GO:0007635]; dephosphorylation [GO:0016311]; negative regulation of fibroblast growth factor receptor signaling pathway [GO:0040037]; nervous system development [GO:0007399]; netrin-activated signaling pathway [GO:0038007]; positive regulation of synapse assembly [GO:0051965]; sensory perception of chemical stimulus [GO:0007606]; synaptic signaling [GO:0099536] | plasma membrane [GO:0005886]; postsynapse [GO:0098794] | protein tyrosine phosphatase activity [GO:0004725]; transmembrane receptor protein tyrosine phosphatase activity [GO:0005001] | PF00102; | 2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 2A subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9585503}; Single-pass membrane protein {ECO:0000255}. Synapse {ECO:0000269|PubMed:29742100}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000269|PubMed:9585503}; | null | null | null | null | FUNCTION: Possesses an intrinsic protein tyrosine phosphatase (PTPase) activity (PubMed:9585503). Regulates egl-15 activity which is required for hypodermis-mediated fluid homeostasis and protein degradation in muscle (PubMed:9585503). During the formation of neuromuscular junctions at the larval stage, negatively regulates membrane protrusion from body wall muscles (PubMed:16495308). Plays a role in nicotinic acetylcholine receptor (nAChR)-mediated sensitivity to nicotine (PubMed:15990870). Regulates synaptic levels of nAchR subunit lev-1 in the nerve cord (PubMed:15990870). Promotes the outgrowth of the quaternary dendritic branches of the PVD sensory neurons (PubMed:26968353). In parallel to the sax-7/mnr-1 pathway, also controls the extension of the PVD primary branches (PubMed:26968353). Acts in the netrin/DCC pathway to mediate the formation of synapses between the AVA interneurons and the PHB sensory neurons (PubMed:29742100). Also required for the formation of synapses between the AVA interneurons and the VA10 motor neurons (PubMed:29742100). {ECO:0000269|PubMed:14517244, ECO:0000269|PubMed:15990870, ECO:0000269|PubMed:16495308, ECO:0000269|PubMed:26968353, ECO:0000269|PubMed:29742100, ECO:0000269|PubMed:9585503}. | Caenorhabditis elegans |
H2KZM9 | TTL11_CAEEL | MGCKISTEFCSDNPVGSISTSKVHPTDLSTPSYAIKPVEFYEEPLKDDQLFYKVALAKKEYREKEKDKKEQLSSNRRVSLQVEPNKLPIPLTRSSSLSSIMENRPPSGISNSSFIRSRNTASRRFTIDTSRAKSNQYVVSLCSKKIGIIEYPDGRSDKQPCDVYWHNVVLSDMNKIVTSPQSRVNKFPGMTELAKKISLTHSISSMQKLFPDEYAFYPNSWFLPAHLADFHAFYRKAQALGKTEMWFIVKPDEGAQGTGIYLINSPNQIRNVDQRQLVQEYVADPLLMNDKLKFDFRVYGVIKSINPLSIYVAREGMARFCTEKYEKPDSSNFKNLYAHLTNYSLNKANEAYVHSNTLQDQTRGSKRLLSTVFHQLESRGVKTKRLWHDIKLILVKTTLAMLPEIMLHYEHHFYDSTGPQCFQIMGFDVMIREDGTPILLEVNAAPSLTADHIVPHPGRTLLEGGQRVRSIVDEVIKIPLVRDTLLLVLGLMEEEYQNNSLKGETKSLDDMQTIKQRRKPHLSEIFPTRYGAHSGHLLFLDKAMYIYMQFVQLRSNVNITNAGLKQFVRKCNLIDIIPVVHVDAKVSEINYYFTGEKRTNGNGLPFHAFLMFLFFIAEKKFVLENDLLSKVQRLLSFCDMSLRRYGVRSARLRRAEVDSTIGNVEIYMLPSRMARNRSGTNGRKQNFTDDNNNPNSFAHLPKINERL | 6.-.-.- | null | microtubule cytoskeleton organization [GO:0000226]; protein polyglutamylation [GO:0018095]; response to hermaphrodite contact [GO:0034606] | axon [GO:0030424]; cilium [GO:0005929]; dendrite [GO:0030425]; perikaryon [GO:0043204] | ATP binding [GO:0005524]; tubulin binding [GO:0015631]; tubulin-glutamic acid ligase activity [GO:0070740] | PF03133; | 3.30.470.20; | Tubulin--tyrosine ligase family | null | SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:20519502, ECO:0000269|PubMed:29129530}. Perikaryon {ECO:0000269|PubMed:29129530}. Cell projection, dendrite {ECO:0000269|PubMed:29129530}. Cell projection, cilium {ECO:0000269|PubMed:20519502}. Extracellular vesicle {ECO:0000269|PubMed:29129530}. | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-glutamyl-L-glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:29129530}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60145; Evidence={ECO:0000269|PubMed:29129530}; | null | null | null | null | FUNCTION: Polyglutamylase which preferentially modifies tubulin (PubMed:27635036, PubMed:29129530). Involved in the side-chain initiation step of the polyglutamylation reaction (PubMed:27635036, PubMed:29129530). By controlling tubulin glutamylation, regulates ciliary specialization and motor-based transport. Promotes the formation of A and B tubule singlets by splaying microtubule doublets in cilia (PubMed:29129530). Together with ttll-4 and 5, required for male mating (PubMed:27635036). {ECO:0000269|PubMed:27635036, ECO:0000269|PubMed:29129530}.; FUNCTION: [Isoform a]: Specifically promotes tubulin glutamylation in a subset of ciliated neurons including amphid, phasmid, CEP and RnA neurons. {ECO:0000269|PubMed:29129530}.; FUNCTION: [Isoform b]: Specifically promotes tubulin glutamylation in male ciliated CEM, HOB and RnB neurons that release bioactive extracellular vesicles (PubMed:29129530). Regulates the localization of TRP channel pdk-2 in male CEM, HOB and RnB neurons (PubMed:29129530). Regulates the environmental release of bioactive extracellular vesicles in cilia (PubMed:29129530). {ECO:0000269|PubMed:29129530}. | Caenorhabditis elegans |
H2KZU7 | SVH2_CAEEL | MVLGSSQSSAKELTTQSSIFRFLVLLLCFTSATGGQINGKLLNGNGVFVSRDELQNKNVLGVITGFDLLVVATHSRFQVFENNEERRTVGHVSLDMHPRTKFLELKLFSKSEIFYCDESSCGLCTYSGVTSSCSTFMLNGDEPKIQEILSSSAVKIENLGQIMLAISFKNEEDPDNPRTMILRYNAQDTGTVIPTAYHADSSFIHNNHALTGFEREGFVYFVMTASQIFEPEVFLHDQSNNKVTVTKVIRFCATDQTADLASKISILVGCDQEFRNISSRGETAVYDHANDLINIVMFNHTSMNHLMCRFKMANIEKRFKTIWSTCQETSFSGSTAKTTRCKYPQIFDQMKVKKGCLTYSRLDDESSPTLCVRYGRGDALDNCQLHTAKSNSYRYGWLEDYNVLQGELMMRIPYPFFGIAESLITDGKSYFAAVSGEFDMSDVLRFSASESADIRPHWRTNISVVGKFSITKTKENQLLYTTVEGLQSLDISCKGLYPNCQTLRQGGWEDPLECSWCADDNAQRTITSSEVSSCKNNLKHECPPSMRWIHKYNNNSGFTAVVDGFRALKNPKLNACGTNCVVTVVDSSSIQCDTNPDEVIGDSCKQVFLSGMIGDKNYSFPFDYQQADRGTQTDVKNSQVDDKKGSSPGWKIAIAIISVMTIILIVAIIVYYMRNRFPRIKTHVRPPIGQRIENEYDMGHMAGRQAQLAINGDNYVKVFRSMRPDLKVDFKNLRVDKLDPIGQGHYGVVYKAMYSPSKSLEEKVVCKYLKEGKISEFYEEARTMSEFDHPNILKLIGVALDDSSHLPIIITEYMAKGDLKSFIENVENTIKMRDLFEFAFDIAKGMNYMHSKKFIHRDLACRNCLLDEHLRVKIADFGLCRKVDIETELYVQMHERDLPVRWFPPEISEQGFGITSDIWSFGVVIWELFTRGSTPYSNMASWILILPWLKESETNRLRKPPYCPEKLYTDVMLACWKANPAERPQFSDLVTIIPNVVKYMEGYDRSQLQAGYERVSSRFLSLSRHDPAFPIYQNEMPNTPLLANCQNDTNDSKTLAELPSDSPSTSTAIPQSTPYQLLSECSETSV | 2.7.10.1 | null | axon regeneration [GO:0031103]; cell migration [GO:0016477]; peptidyl-tyrosine autophosphorylation [GO:0038083]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of axon regeneration [GO:0048680]; positive regulation of MAPK cascade [GO:0043410]; protein phosphorylation [GO:0006468]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; mitogen-activated protein kinase kinase kinase binding [GO:0031435]; protein tyrosine kinase activity [GO:0004713]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF07714; | 1.10.510.10;2.130.10.10; | Protein kinase superfamily, Tyr protein kinase family | PTM: May be autophosphorylated on Tyr-890 following dimerization. {ECO:0000269|PubMed:22388962}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000305|PubMed:22388962, ECO:0000305|PubMed:27984580}; | null | null | null | null | FUNCTION: Receptor tyrosine kinase which may phosphorylate mlk-1, a component of the mlk-1, mek-1 and kgb-1 pathway (PubMed:22388962). Involved in axon regeneration after injury by promoting the generation of productive and stable growth cones (PubMed:22388962, PubMed:27984580, PubMed:31109965). {ECO:0000269|PubMed:22388962, ECO:0000269|PubMed:27984580, ECO:0000269|PubMed:31109965}. | Caenorhabditis elegans |
H2KZW3 | M3K20_CAEEL | MSTPTSNESTSSSSNNSDQRVLFPDIQRDDIQVGDHIGVGTFGAVFSGNWTLPDGSQRTIALKKVFVLEKEAEILSKIRHKNIIQFYGICKATGNDFFIVTEYAEKGSLYDFIHSEESQSFASSSGGNSFDVVVKWASQIASGIQYLHYDAVDTIIHRDLKSKNVVLDKNLVCKICDFGTSKDLTHSCTAPSWGGTAAWMSPEMILQSEGLTTATDVWSYGVVLWEILSKEVPYKDYSEFRIFTMITQSGITLAIPPSCPAPLKQLMSNCWKMTPKDRANMRQIQGELNRLAGNQKVMDECEKFMGLEDWKTEIEKQEKNVEKMRKDLEKRREQLEIREKALKQRMKVEQAVLDSARHPPEDVHQWSEHHTSHWVETVLGRVANDKKFLDRVNAAVFRNRITGARLLGMTQNDLEHLGVHKVGSRIELMKMIRKLADTQKALHNFPTLEQAKRIEMTLKTEKEAAGQLANDVDIVIIVGMYVRKMNATRRKFKFYADSDWIDDTDIPAKSKSKHASSLIKTVCFSVLDENTKKPINEPACSISSGMTTNPDWITVDTEDDVKIRVIVSVYYADIVTQPRNTEVIKVVTSLEESKILEERHVHLRLRRSSSSASISTPSPVIAPVYHPFGHLNNGFHHTTSSPQLRGFWHRKQTGMNRHGLTETELSSLQEQLRTPSPDKKVVDENVIIHVPKLTRRRRTTTTNSEDTEKSDTNNKTPESQARRVHVHGGKDKWNWKKGKSRPKFT | 2.7.11.25 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9NYL2}; | phosphorylation [GO:0016310]; signal transduction [GO:0007165]; stress-activated MAPK cascade [GO:0051403] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; rRNA binding [GO:0019843] | PF07714;PF07647; | 1.10.150.50;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NYL2}. Nucleus {ECO:0000250|UniProtKB:Q9NYL2}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; Evidence={ECO:0000250|UniProtKB:Q9NYL2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:Q9NYL2}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25; Evidence={ECO:0000250|UniProtKB:Q9NYL2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000250|UniProtKB:Q9NYL2}; | null | null | null | null | FUNCTION: Stress-activated component of a protein kinase signal transduction cascade that promotes programmed cell death in response to ribotoxic stress (PubMed:32289254). Acts as the proximal sensor of ribotoxic stress: directly binds to the ribosome, thereby acting as a sentinel for colliding ribosomes (By similarity). Upon ribosome collisions, activates the stress-activated protein kinase signal transduction cascade, leading to programmed cell death (By similarity). Acts by catalyzing phosphorylation of MAP kinase kinases, leading to activation of the JNK and MAP kinase p38 pathways (PubMed:32289254). {ECO:0000250|UniProtKB:Q9NYL2, ECO:0000269|PubMed:32289254}. | Caenorhabditis elegans |
H2KZZ2 | HLH30_CAEEL | MIRQLNSPGGGGGLGLNNPRAQQPPGAQQQQQPQQAQQQFYDDEPYQANASQFRFGAGKSMEQRRETGNLIPIAQRSMGSTSTPFGSAPTQSYFGGGSSGAALSSPRKMQQTHQMLFGNIQPPRGSPPSDGSDKIHRFGESPTPGGVGGVFGTELDDLIIDELMGMEDDQRMRPGATRPMTIGGEKTMSMARPIPGASSRAGSGHSGSPITIPNAMSNNFRQVVSSSAPTSSIDIEKMIGAVSNGGGNSGGDNDPEDYYRDRRKKDIHNMIERRRRYNINDRIKELGQMLPKNTSEDMKLNKGTILKASCDYIRVLQKDREQAMKTQQQQKSLESTAHKYADRVKELEEMLARQGVQVPPSHLPPIPKVIERPIKQEIDESPPNHTPTGSFVSSSGFLSEVTNNTAAMQITSPNDSRPNNFMNNSAPSDSFFSVGSASPPDYRTSSGTASWKLPGSNAFSDLMMDDLNPMMNGDPLISSAGAHPSPHFHSSQMSPDIHWDASGFSPDPINTQQSNSGHYHMDFS | null | null | cellular response to toxic substance [GO:0097237]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; determination of adult lifespan [GO:0008340]; positive regulation of gene expression [GO:0010628]; positive regulation of macroautophagy [GO:0016239]; positive regulation of plasma membrane repair [GO:1905686]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of xenophagy [GO:1904417]; regulation of autophagy [GO:0010506]; regulation of transcription by RNA polymerase II [GO:0006357] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00010; | 4.10.280.10; | MiT/TFE family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23604316, ECO:0000269|PubMed:24882217, ECO:0000269|PubMed:28198373}. Cytoplasm {ECO:0000269|PubMed:24882217, ECO:0000269|PubMed:28198373, ECO:0000269|PubMed:34323215}. Note=Localization to nucleus enhanced during fasting and on mutant backgrounds involved in modulating longevity: glp-1, let-363 (tor), eat-2, daf-2, clk-1 or rsks-1 (PubMed:23604316, PubMed:23925298). Nuclear localization abolished on mml-1;glp-1 or mxl-2;glp-1 mutant backgrounds (PubMed:27001890). Localization to nucleus enhanced as a result of bacterial pore-forming toxin treatment, or heat shock (PubMed:27875098, PubMed:28198373). {ECO:0000269|PubMed:23604316, ECO:0000269|PubMed:23925298, ECO:0000269|PubMed:27001890, ECO:0000269|PubMed:27875098}.; SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24882217, ECO:0000269|PubMed:27184844}. Note=(Microbial infection) Localization to nucleus enriched rapidly after Staphylococcus aureus infection. {ECO:0000269|PubMed:24882217, ECO:0000269|PubMed:27184844}. | null | null | null | null | null | FUNCTION: Transcription factor which regulates the expression of genes involved in lipid metabolism and autophagy in response to nutrient availability, bacterial pore-forming toxins or heat shock (PubMed:23604316, PubMed:23925298, PubMed:27001890, PubMed:27875098, PubMed:28198373). Binds to the E-box motif 5'-CACGTG-3' (PubMed:19632181). Under fasting conditions, binds to the promoter and activates the expression of lipase genes lipl-2, lipl-3 and lipl-5, and to a lesser extent, lipl-1, thereby regulating lipolysis (PubMed:23604316). Involved in modulating longevity in response to TOR signaling, dietary restriction, germline signaling, heat shock and the insulin-like signaling pathway (PubMed:23925298, PubMed:24882217, PubMed:27001890, PubMed:28198373). Involved in the immune response to infection by the S.aureus bacterium, probably acting downstream of the protein kinase dkf-1, leading to the transcriptional activation of host defense genes (PubMed:24882217, PubMed:27184844). May also play a role in lysosomal biogenesis in response to nutrient availability (PubMed:23604316). {ECO:0000269|PubMed:19632181, ECO:0000269|PubMed:23604316, ECO:0000269|PubMed:23925298, ECO:0000269|PubMed:24882217, ECO:0000269|PubMed:27001890, ECO:0000269|PubMed:27184844, ECO:0000269|PubMed:27875098}. | Caenorhabditis elegans |
H2L002 | GCY7_CAEEL | MKPFYSMSLVLFLVITLLPKPMFPQVATGTTGNVIRVGFIHCRDFQSAPITVGYRTSAAAASIAVDRLKRENLMSGWEFNFTIEFDDCVESEAAGMTVDLIEKHNVDVIIGPTMNQPTLAAFIVSNYFNRPIIAWGLVNAAQLDDFERFPNAGILSAGQRSLGVAIRAVLKRYEWSQFVYAYFTEEDTEKCVTMRNDLQQVVSYFGDIILAYSIQVADISNDGMIEALKKIQSRGRIIVTCMKDGIGLRRKWLLAAEEAGMIGDEYVYVFSDIKSKGYVVPLLGGGERPSWILSTGSDENDTRALKAFKQSIFICDMMGQGSIATNYTIFGQEIIARMKEAPYFCTKDCEGENFTVAATYAGQLHDAVYAYGVALDKMLKAGQIAQYRNATAFMRYFPQSFIGMSGNVTINEKGTRNPTLFLLALDENNNNTRMATIYVENMSATFNALYSDEGVMWASRKNNARPVDVPLCGFTGNLCPKSFVDEYLIWVIVAIVVLFLAITAAACGIYFSIQARRQEIERLNRLWQIPFIHLHQINSKQKGKGEHSVRSLQSGTSTLSSRTTVSFKTESRNFLFFSLQRESDYEPVVAKKHAYRPRLDDDKCTFMRSLRNLDQDNLNRFIGLCLDGPQMLSVWRFCSRGSIADVILKATIQMDNFFIYSLIKDMVHGLVFLHGSMVGYHGMLTSKCCLIDDRWQVKISNYGLQDLRSPEMYEKKDLLWSAPELLRAEDIKGSKEGDVYSLGIICAELITRKGVFNMEDRKEDPEEIIYLLKKGGLKSPRPDLEYDHTIEINPALLHLVRDCFTERPSERPSIETVRSQLRGMNSSRNDNLMDHVFNMLESYASSLEEEVSERTKELVEEKKKSDVLLYRMLPKTVADKLKLGQTVEPETFEQVTIFFSDVVQFTTLASKCTPLQVVNLLNDLYTIFDGIIEKHDVYKVETIGDGYLCVSGLPHRNGNEHVRQIALMSLAFLSSLQFFRVPHLPSERINLRIGMNCGSVVAGVVGLTMPRFCLFGDAVNTASRMESNGKPGKIHVSAEANRMLHLVGGFDTESRGEVIIKGKGVMETFWLTGQGTGAVSGARHVSAKKVSKKMDEIHRQETLKSDEQLSD | 4.6.1.2 | null | cGMP biosynthetic process [GO:0006182]; chemosensory behavior [GO:0007635]; chemotaxis [GO:0006935]; intracellular signal transduction [GO:0035556]; receptor guanylyl cyclase signaling pathway [GO:0007168]; response to magnesium ion [GO:0032026] | cilium [GO:0005929]; plasma membrane [GO:0005886] | adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; guanylate cyclase activity [GO:0004383]; peptide receptor activity [GO:0001653]; protein kinase activity [GO:0004672] | PF01094;PF00211;PF07701;PF07714; | 3.40.50.2300;3.30.70.1230;1.10.510.10; | Adenylyl cyclase class-4/guanylyl cyclase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000250|UniProtKB:Q19187}; | null | null | null | null | FUNCTION: Guanylate cyclase involved in the production of the second messenger cGMP (By similarity). Unlike other guanylate cyclases expressed in ASE neurons, may not play a role in chemotaxis responses toward salt ions in ASEL (ASE left) sensory neurons (PubMed:19523832). {ECO:0000250|UniProtKB:Q19187, ECO:0000269|PubMed:19523832}. | Caenorhabditis elegans |
H2L006 | TSP14_CAEEL | MPHRAPRRFMKTAPGACDWEQCLLMGSGEPTRARAVVSSSHKQRKPRQEISACLKWLVFLLNSIVFLVGVGILALGVYLFIKDFREVKLVDIILNPAILISIFGFSICVVSFFGFMGALRDNIFLLKCFAACVFLSYILVVAVTLVFFTLFYTDTTEGLSANWLLLYAVKNYHTNRNLAEIMDALQENLECCGVSSIAQGYRDWNMSYQFNCTNSNPQPEKCGVPFSCCRKSVISEAAGSSNPLLPAMRSLECWQNALTKRPGDLEHDIYTRGCLQPLRTLFESHAVHVGAFVALLIVPVCISVCLTNILAKQVDHQRYLLEREARRNDRRRKRDHNRRDQLNSLDLLEEGKFNNASANATRPRPPDIPPPLPPIEHVPRKKSRNASSSPTRKPKSAGVENAAARRKRTATTTRTPPAAAGPAPTPQATTTNRTHQWVLQQTDLVPQKSKS | null | null | nematode male tail tip morphogenesis [GO:0045138]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of egg-laying behavior [GO:1901046]; positive regulation of embryonic development [GO:0040019]; positive regulation of vulval development [GO:0040026]; regulation of mesodermal cell fate specification [GO:0042661] | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; early endosome membrane [GO:0031901]; late endosome membrane [GO:0031902]; recycling endosome membrane [GO:0055038] | protease binding [GO:0002020] | PF00335; | 1.10.1450.10; | Tetraspanin (TM4SF) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:31988138}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Endosome membrane {ECO:0000269|PubMed:31988138}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Early endosome membrane {ECO:0000269|PubMed:31988138}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Late endosome membrane {ECO:0000269|PubMed:31988138}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Recycling endosome membrane {ECO:0000269|PubMed:31988138}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Note=Often in close juxtaposition to the retromer but not part of it, suggesting separate microdomains of the same endosome. {ECO:0000303|PubMed:31988138}.; SUBCELLULAR LOCATION: [Isoform a]: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:35089916}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Endosome membrane {ECO:0000269|PubMed:35089916}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Early endosome membrane {ECO:0000269|PubMed:35089916}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Late endosome membrane {ECO:0000269|PubMed:35089916}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Apical cell membrane {ECO:0000269|PubMed:35089916}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Note=Primarily localised to intracellular vesicles. {ECO:0000269|PubMed:35089916}.; SUBCELLULAR LOCATION: [Isoform b]: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:35089916}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Endosome membrane {ECO:0000269|PubMed:35089916}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Recycling endosome membrane {ECO:0000303|PubMed:35089916}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Basolateral cell membrane {ECO:0000269|PubMed:35089916}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Note=Primarily localised to the cell surface. {ECO:0000269|PubMed:35089916}. | null | null | null | null | null | FUNCTION: Functions redundantly with tsp-12 to regulate cell surface levels of the BMP type II receptor daf-4 (but not BMP type I receptor sma-6), probably by regulating endosomal sorting and recycling of receptors, preventing their targeting to degradative lysosomes (PubMed:31988138). Together with tsp-12, regulates cell fate specification in the postembryonic mesodermal M lineage, body size, male development and vulva development, probably by positively modulating BMP-like Sma/Mab signaling (PubMed:25978409, PubMed:28068334, PubMed:31988138). Together with tsp-12 involved in maintaining the structural and functional integrity of the endosomal network (PubMed:31988138). Together with tsp-12, probably acts by modulating the activation of glp-1, Notch-like receptor, to regulate germline maturation (PubMed:20220101). {ECO:0000269|PubMed:20220101, ECO:0000269|PubMed:25978409, ECO:0000269|PubMed:28068334, ECO:0000269|PubMed:31988138}.; FUNCTION: [Isoform a]: Functions redundantly with tsp-12 to regulate cell fate specification in the postembryonic mesodermal M lineage, body size, embryonic and vulva development. {ECO:0000269|PubMed:35089916}.; FUNCTION: [Isoform b]: Functions redundantly with tsp-12 to regulate cell fate specification in the postembryonic mesodermal M lineage. Likely plays a complementary role in mesodermal development with tsp-14 isoform a, but may be more critical. {ECO:0000269|PubMed:35089916}. | Caenorhabditis elegans |
H2L008 | ZTF16_CAEEL | MDELNACTECGFTTTVFSEFQGHIEKHENEHSRSSSGEMSNSQTIEWGDGIQSSTPSPRSTPPSDPTPSPDSDEHLEHHISITEITNTLIKKEPGTKGQKTVHVCPHCNFTTCMSQHMKSHLEAHERHQGQMYQCDICKMQFSQKANMHRHRMRHSGVKPYECRFCKKRFFRKDQMQEHSMTHIKTGFGFDCPVSQCNMQFSQHNALRAHLEETHTISSTNPASCKRCNLMFANSRRLLLHFQTRHDDSESSPKKENTPKRKKLSNGNALPMDPANMSITEQLQRMVKSEFSPPNTDTSDNSTSSEFDKIPPSFPMANPDILLMCLNQMNQFNGFGENIPRPMLNIPNIPLPALHNIPAVAAIVKQDQVQLWSEQTSSSVSVSAPSPSEQSHSPPANESSLSLTEKEKSPTPEKEDEENVECCHCGMMFYDNTMYLLHKSLHSDGDPFKCALCGTQCGEKYMFTTHVIFADHSTQATTSA | null | null | gonad development [GO:0008406]; positive regulation of gene expression [GO:0010628]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00096; | 3.30.160.60; | Ikaros C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22298710}. | null | null | null | null | null | FUNCTION: Positively regulates the expression of ver-1 in the amphid sheath glia of amphid sensory neurons (PubMed:22298710). Together with ehn-3, plays a role in somatic gonad development and is required for proper gonadal primordium assembly and somatic gonad precursor cell morphology (PubMed:20026024). {ECO:0000269|PubMed:20026024, ECO:0000269|PubMed:22298710}. | Caenorhabditis elegans |
H2L045 | TENSH_CAEEL | MAAAALCCASRKSNKYNNEAGYEVYTISEDQLRLKQKMKDRKEGVQVEYITSRLIVLSCTSETSERKFVESLLKASQQIQNAHNKHIRVWNVSQRRHDISSSLDAIPFGWPSETAPSLEKLCTICKNLDQWMLEHPLNIAVIFCKGGLERCAIVVNAFMRFNAISATDDSVDDRFSMQRFSERFLGPDGPPSYKRYLGYFSSLLSGRISVNSDPLYLHNIILTFFEPINVFLKIYERLVPVYQSKTVALNKSSKFEMDGSLKLRGDIFFKCIVAASSPGSSTRCLFTCQLNTCALELHPINSEGYSVVRLHKEELDLIFNDKKIDNRVTVELVVSHTSGPTTIATAAVQSVHSLLPRNNSYETFELAQDDETNRSRLEVEYSEIRKKSTKSSKSANPINNNQEEEMPVGPPVPPKPSTPIMNGERLGEYGVGGHIGNGDVVPERRGILPASLREKINQKKELEGRATPSIEPDLVGRDRYDKASRCFSYVPAKSMQEAFERPRRTSFSRAIEKRENSVENVSQEEVARTEIPQSYQQNDISTPAKWDEQVEDAKQSALLEELARAPSAMQHNYWGNGEVDNVQVVDQAQRAVITPTSTLQRRPKPPARSGSYRTLNDDAYCSDMDELCDPEYYLNYNSNTAPLPPPRRQEQHAGTRSVQLPRKKMNFDAVTDPLDDVLESTKRLGSAYSVGDVRGGQQQQQEQHNASNDFNFSNTLNNTPTDYRQHYRNRNCQSVTTPRNHHFSTPSREQEADAADTWLSGKLKKVRSKRDIDPDIVRRRTQEKMLLEELKDSAANNDENQHNLPNGHARGAGLQNIDPLAEFRREEERLRNTRSPYGEERWRGRMRGKPPTPPPRESSASPVNSLPRGTPAHHMDRQRHNQSVPLPMHHRQFDEDFDVNSLFNFSHDPRQQSTTLERGGRSLSRGARIQDAYYASQQDLSANNRFNSGQERVAAAIYRAETAHRDMYASGTINRAETPGRYFPENSAVLERSSTPSFPVSRATPLPFHPLLYNNGERGGSGHAAGGGGGGHNGYSTMNNRSASPRLFGGSSTLSRRSSVNSVDTSEIIHHHPLFVKDTSKYWYKPTISREQAINMLRDKPPGTFVVRDSNSFPGAFGLALKVSTPPPGVNPGDGSELVRHFLIEPSPKGVKLKGCNNEPVFGSLSALVYQHSITALALPTKLVLPDFDPAATPEHLSATQALLEQGAACNVVYVGSVDVESLTGNECVKRSIATCSQRAINGDSRAVSVHFKVSSQGVTLTDNTRKVFFRRHFNVQSVIFAGMDPIERRFENTRALGFHDGCIAQARLFAFVARIPSSSENACHVFAELEPEQPGSAVVNFINKVMLAQKNRS | 3.1.3.48 | null | positive regulation of axon regeneration [GO:0048680] | axon [GO:0030424]; cell junction [GO:0030054]; focal adhesion [GO:0005925]; M band [GO:0031430]; striated muscle dense body [GO:0055120] | protein tyrosine phosphatase activity [GO:0004725] | PF08416;PF00017; | 2.60.40.1110;2.30.29.30;3.90.190.10;3.30.505.10; | PTEN phosphatase protein family | null | SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:31109965}. Note=Localizes to punctate structures along the axon in motor neurons. {ECO:0000269|PubMed:31109965}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000250|UniProtKB:Q63HR2}; | null | null | null | null | FUNCTION: Probable phosphatase which regulates axon regeneration after injury by linking the svh-2 and integrin signaling pathways. {ECO:0000269|PubMed:31109965}.; FUNCTION: [Isoform e]: Not involved in axon regeneration after injury. {ECO:0000269|PubMed:31109965}. | Caenorhabditis elegans |
H2L056 | UBXN3_CAEEL | MDLTASLEDDQREKLRQYTEFTHQQDYEVAIGTLASLNWNLEQAIEAHLMQEDKNDDEDPEILETIPAAASGRNAGASSSSRFEPEVINIEDDEMPATRGRRRGRAVTPDETTTVDNQVKRLRIDDGSSSSSNGAATHHRGAAIPRQKRGQATEPTPSSSGSSSASFSSRRGTRANPVPPPNQEPAHPESARQNGGILASRHNNHNNQQNNHHHHHQRIPINPRRVDVFNVDSDEDDDSMAIAYEDDDDGVHEVHHSEVVARGSGPPNGRIPMIPDGFSSVSDALRNFVAIFSDRFCSTPQTQAFMPPFYTEPLPAAVKEAFDHPNSEHRRPLLFYINHDRSIAANIFASQVLCSETVSTLIRHQYVLFPWDITSDSNLMLFLEYLQAANMGDVRTIIQRLAMSKIESFPLMAIVVKERNSYRLVDYCRGTDTSDQVMEKLLSGVSEYSDIRMNEQSERREREEREAIRNQQEAEYKASLAADKARMEAKQQEIEEQRLEEERKLREEEEECVRRQTVASTVPEEPPASAPLAEIINVKFRLPEGGQDMRRFRRLESIQTLINYLSSKGYSPDKFKYFNSDFPKKEITRHFDLSHNFADTKWPAREQIFVEEI | null | null | cell differentiation [GO:0030154]; ERAD pathway [GO:0036503]; masculinization of hermaphroditic germ-line [GO:0042006]; positive regulation of mitotic cell cycle, embryonic [GO:0045977]; positive regulation of protein catabolic process [GO:0045732]; regulation of protein localization to chromatin [GO:1905634]; spermatogenesis [GO:0007283] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | K48-linked polyubiquitin modification-dependent protein binding [GO:0036435]; NF-kappaB binding [GO:0051059]; protein-containing complex binding [GO:0044877]; ubiquitin binding [GO:0043130] | PF21021;PF14555;PF00789; | 1.10.8.10;3.40.30.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26842564}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20977550}. Chromosome {ECO:0000269|PubMed:26842564}. Cytoplasm {ECO:0000269|PubMed:26842564}. Note=Colocalizes with cdc-48.1 to the perinuclear region in spermatocytes (PubMed:20977550). Localizes to the nucleus during S phase in a cdc-48 and npl-4-dependent manner (PubMed:26842564). {ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:26842564}. | null | null | null | null | null | FUNCTION: Ubiquitin-binding protein which acts as an adapter for ATPase cdc-48.1 and/or cdc-48.2, conferring substrate specificity (PubMed:20977550, PubMed:26842564, PubMed:28368371). Together with ubxn-1 and ubxn-2, plays a role in hermaphrodite spermatogenesis probably by promoting the degradation of sex determination terminal factor tra-1 (PubMed:20977550). During mitosis, ensures the degradation of DNA licensing factor cdt-1 and the disassembly of the DNA replication CMG helicase complex by promoting the dissociation from chromatin of several of its components including cdc-45 and sld-5 (PubMed:26842564, PubMed:28368371). {ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:26842564, ECO:0000269|PubMed:28368371}. | Caenorhabditis elegans |
H2L099 | GCK1_CAEEL | MTTTSSDELPRQADDDSMKWDRIYIQKLDPEVIFTKQERIGRGSFGEVYKGIDNRTGRVVAIKIIDLEQAEDEIEDIQQEIQVLSQCDSQYVTKYFGSFLKGSKLWIIMEYLGGGSALDLTKSGKLDESHIAVILREILKGLEYLHSERKIHRDIKAANVLVSEHGDVKVADFGVAGQLTETVKKRITFVGSPFWMAPELIKQSSYDYKADIWSLGITAIELANGEPPHSDLHPMRVLFLIPKNPPPVLQGSQWSKPFKEFVEMCLNKDPENRPSASTLLKHQFIKRAKKNSILVDLIERAAEYRLRTGVSSDSDLDEDSDGGGGTSKWDYPTVRGPRVSADDDGTVRQRTDRPRAQVDRRSPSGSPGGTIVRGSPQVAAVAEQLRNSSVGSSGYGSGGNSASSQYATSSLPQSHTASSGGATTITLGSPNGSPTSSLARTQSMVSPSGQRSGSAQSWELERGNRPMSERVSSQVSPSKYNQHRTSSSNGVQGGSGGRREYINGSGSGLNGNSSNQNHSEYSDAVRQRGPGGSGGRLDYRESHVPTSSQENLNHGRMYGYGAPPPSREANNVPMPRVKGALDCSLLPAIEHLSRTRHATAALDQLRHVFRDVEDSCPGICNELIEELMQRIAVPQVSQSDLDAAIRRLTTPPS | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9P289}; | epithelial tube morphogenesis [GO:0060562]; meiotic cell cycle [GO:0051321]; negative regulation of apoptotic process [GO:0043066]; oogenesis [GO:0048477]; phosphorylation [GO:0016310]; positive regulation of endocytic recycling [GO:2001137]; positive regulation of GTPase activity [GO:0043547]; regulation of Golgi organization [GO:1903358]; regulation of oocyte development [GO:0060281] | cytoplasm [GO:0005737]; cytoplasmic side of apical plasma membrane [GO:0098592] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; mitogen-activated protein kinase binding [GO:0051019]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF20929;PF00069; | 1.10.12.70;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25743393}. Apical cell membrane {ECO:0000269|PubMed:25743393}; Peripheral membrane protein {ECO:0000269|PubMed:25743393}. Note=Co-localizes with ccm-3 in the apical membrane of the excretory canals. {ECO:0000269|PubMed:25743393}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9P289}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9P289}; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase which is required for normal oogenesis and suppression of germline cell apoptosis. Inhibits phosphorylation and thus probably activation of mpk-1 during pachytene stage (PubMed:19826475). Involved in excretory canal elongation during postembryonic development, probably acting downstream of ccm-3 (PubMed:25743393). {ECO:0000269|PubMed:19826475, ECO:0000269|PubMed:25743393}. | Caenorhabditis elegans |
H2L0G5 | PTC3_CAEEL | MSFPDEETDLLSEAKHCIRNVIHRTHRKFLENRLIGNFDSEDFSDAWKKKFAHAPTWCDADMSLQQIKRGKAVGNTVALTARAFFQLWLFRIGCFVQRWAWSTIFISLFLYCLCLGGLRHVTIETDLVKLWVSEGGRLNEEMGYLGQVKFERESGHLVHKVKRAVEQTTEPPAPAVKAEVRRGPELPKENGLGGGFQVVIQTPSFDGQNILSKEALQQHTKLMEEISTYEVKMFNETWTLSDICFKPPGPSFNSGPLAGIMSKLLDKIIPCIWITPIDCYWDGAKPLGPNPPLNLGPEVASFVSSLPPGNVTWKNLNPTSVIKEVGTLFDLGPIGNFFERAGIDGAYLDRPCIDPLEEECPKSAPNYFDRCHALTKFNEWNMAKAMSEQVTLERKIIPKDDGKSDIAETILNDIFGKKRRKRQADTTTKKPATKKDEDYYEYEDDADYLAGIANSTIAKKNPEKEAKDLLCLEYGSSLLKWMQENPERLGEFLTKEEMPDYPNYGDVMTGGCKGFGKKIMEWPEDLIIGGIQRDNGKLVSAEALQSVFLVSGAYDVFARIKNDKTDSHPGLDRHHFQPWMAGEIISTWQRNFTKRLYSHELNRERRQFHPLASTSIADMLEEFSQFNYIIIVIGYILMVIYAAFTQGRFQGWWLAVQSNVALAICGVILVTISSICGLGFATHLGINFNAATTQVVPFLSLGLGIDDMFLLLHNYDEIINICNKNEIGVLLKETGMSVMLTSINNILAFISGYVLPIPALRSFCSQTAILLAFNLIFLMFIFPAMIGIDLRRQRKGKRDLAYCSRGNPQMATSQSVPSNVSNMSSRAELAGYEKQADEYKRHEPWYTVGGFLNKIYIPALKNNVVKACVLIGTTTAVVFGLYGMYTSTLGLELADVLPEHTPPAAFLRAREQYFSFYPMFAVLRGDKLDIPNQQQLIEEYRAQLGSSKFMIKAEGKLQPYWMSMLRVWLQSLDMALEKDLAAGKFDLTNGNPIKVNGEKPSPESMIAARLVCSFGTNYNCDGRLGKMKMVENEVINPEGFYNYLTGWFNVDNMMYYVSQASFYPTPPGWEYNEKLAKVVPAAEPLLYSQMPFYQNDLIDTPAIVKMIEEIRATCEEYSERGLSNHPSGIAFTFWEQYLTLRWNLFQAICIIALAVFCVISILMFNPWAATLIMCIVVITTIELGGFMGLMGIKMNPISAVTLICAVGIGVEFTAHVELAFLTALGTIDQRLESCLQHMFVPVYHGAISTFLGVVMLVFSEFDFVVTYFFYTMTLLVALGVFNGLCVLPVILTLVGPKPELTPTDGSSVLPPPPPLRQQYAEKSGGVEGGMRKRKEKRPAEVEMSARDSPSTSSASHSSDDESSPAHK | null | null | molting cycle, collagen and cuticulin-based cuticle [GO:0018996]; negative regulation of smoothened signaling pathway [GO:0045879] | adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; cytoplasmic vesicle [GO:0031410]; plasma membrane [GO:0005886] | hedgehog family protein binding [GO:0097108]; hedgehog receptor activity [GO:0008158]; smoothened binding [GO:0005119] | PF02460; | 1.20.1640.10; | Patched family | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:21215260}; Multi-pass membrane protein {ECO:0000255}. Cell junction, adherens junction {ECO:0000269|PubMed:21215260}. Note=Co-localizes with ajm-1, an adherens junction marker in hypodermal cells and vulval toroids. {ECO:0000269|PubMed:21215260}. | null | null | null | null | null | FUNCTION: Regulates osmosis during embryonic development. Required for larval development and in particular is involved in larval molting. {ECO:0000269|PubMed:21215260}. | Caenorhabditis elegans |
H2L0N8 | ARL13_CAEEL | MTEKSWFETIFCCCCHRTPIIRREIKLGCFGIGSAGKTTFLKVLKGEDPRDLLRTNGFSTVKMEYDETFHLTIYDVGGDKGIRGIWSNYYAEVHGIIYVIDYSTDETFTESIEALHSLTSNPHVQKKPIFLLLNNQNNREFDDVEISNETKIQAGQHKIVLFSHFNKYNGYLDNIKSATLTVMARAKKDRNEYQEQFVRFIDSISEHYVELSEGVKTAELALRIRQEEAKEQRRLMQMKVEHDALKADVAGLELRNQPPVQPPIPPDPPSDPKSASVHIEESPPMSLASSTIPSDIIQSTPETGTPRDPVNFCRISQTSTKPVSPESNSVKEEPTIILKDNYFLPPKAPGRQYSRIQRIQNVLNNRVVPK | null | null | cilium assembly [GO:0060271]; intraciliary transport [GO:0042073]; non-motile cilium assembly [GO:1905515]; receptor localization to non-motile cilium [GO:0097500]; sensory perception of chemical stimulus [GO:0007606] | ciliary inversin compartment [GO:0097543]; ciliary membrane [GO:0060170]; cilium [GO:0005929]; leading edge of dendritic growth cone [GO:0061917]; microvillus membrane [GO:0031528]; motile cilium [GO:0031514]; non-motile cilium [GO:0097730] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00025; | 3.40.50.300; | Small GTPase superfamily, Arf family | PTM: Sumoylation regulates the targeting of membrane sensory receptors to the cilium. {ECO:0000269|PubMed:23128241}. | SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:20231383, ECO:0000269|PubMed:20530210, ECO:0000269|PubMed:24339792, ECO:0000269|PubMed:31259686}; Lipid-anchor {ECO:0000269|PubMed:20231383, ECO:0000269|PubMed:20530210, ECO:0000269|PubMed:24339792}. Note=Associates to the cilium membrane via palmitoylation. Localizes to proximal ciliary membranes, to an inversin-like subciliary membrane compartment, excluding the transition zone. | null | null | null | null | null | FUNCTION: Cilium-specific protein required to control the microtubule-based, ciliary axoneme structure. Required for normal sensory cilium function. May act by maintaining the association between IFT subcomplexes A and B. {ECO:0000269|PubMed:20231383, ECO:0000269|PubMed:20530210}. | Caenorhabditis elegans |
H2L0Q3 | GABR1_CAEEL | MFVRSSWLLLWGTIVWASAEPVTLHIGGTFPMESGSGGWAGGEACLPAVEMALKDVNSRLDILPGYVLNMTNHNSQCQPGLAMQQLYDFLYKPPTKLMLLTGCSPVTTVIAEAAPVWKLVVLSYGGSSPALSNRNRFPTLFRTHPSANMQNPTRIHIMEKFKWKRFTILMSVEEVFVTTAKDLEAIARKKGIKVDRQSFYGDPTDAMKTLQRQDARIIVGLFYVTEARKVLCQAYHHGLYGRRYVWFFIGWYADTWYIPPPEEHLNCTAEQMTEAAEYHFTTESVMLSRDNIPAISEMTGMQFQQRLTQYFQKDTANVGGFPEAPLAYDAVWALALAFNCTRNNLPSHIRLENFTYDNKVIADTLFQCVKNTSFRGVSGKVMFSDSGDRIARTQIEQMQGGKYKIMGYYDTTSGDLEWYNKEQWLNGKGPPPDSTVIKKHAMTVSNEFYYPTILFAVLGIAACVFIYLFTQKHHERLIIFQSQPECNNILLIGCSLCLFSLFLIGLPSDDISISESLFPLLCHARVTILLFGFTFAYGSMFAKVWIVHRMGATENQQLASRQKDEEENTPWEGIRTLISTMVGRQALMRKSSGQAYGALLEKRNTVLNQPISSSKFYVIVAALTAVDVFVCFVWVLIDPLHLTEQKFPLFTPADSEEDEMIMPVLQQCQSNQQEVWIGIIMGFKCLLLVFGTFLSYETRNLKLRFINDSRFVGLAIYNVAVMTLVTAPVVTLLIHGKVDANFAFISLTVLICTYISVGLIYGPKIRHIIKVPPSADEIQLNGNVGPGVMSKVDQKRYDMLKKENETLQIQIEEKERKIHECKERLEELTKNSETEDMNAQLLCENDKQIADENLTYSTATTLTTTIPLIDLQNGNHPGQIYENDNDDDGSSTSSDEILL | null | null | G protein-coupled receptor signaling pathway [GO:0007186]; gamma-aminobutyric acid signaling pathway [GO:0007214]; negative regulation of synaptic transmission, cholinergic [GO:0032223]; regulation of locomotion [GO:0040012]; response to xenobiotic stimulus [GO:0009410] | G protein-coupled GABA receptor complex [GO:1902712]; G protein-coupled receptor heterodimeric complex [GO:0038039] | G protein-coupled GABA receptor activity [GO:0004965] | PF00003;PF01094; | 3.40.50.2300; | G-protein coupled receptor 3 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UBS5}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Component of a heterodimeric G-protein coupled receptor for GABA, formed by gbb-1 and gbb-2 (By similarity). Within the heterodimeric GABA receptor, only gbb-1 seems to bind agonists, while gbb-2 mediates coupling to G proteins (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (By similarity). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (By similarity). Calcium is required for high affinity binding to GABA (By similarity). Plays a critical role in the fine-tuning of inhibitory synaptic transmission (By similarity). Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials (By similarity). Along with gbb-2, may couple to the G(o)-alpha G-protein goa-1 to negatively regulate cholinergic receptor activity in the presence of high levels of acetylcholine in ventral cord motor neurons (PubMed:18614679). As acetylcholine depolarizes body wall muscles, modulation of acetylcholine levels most likely results in the control of locomotory behavior (PubMed:18614679). Acts in neurons to regulate lifespan, and this may be through G-protein-egl-8/PLC-beta signaling to the transcription factor daf-16/FOXO (PubMed:26537867). {ECO:0000250|UniProtKB:Q9UBS5, ECO:0000250|UniProtKB:Q9Z0U4, ECO:0000269|PubMed:18614679, ECO:0000269|PubMed:26537867}. | Caenorhabditis elegans |
H2LBU8 | YAP1_ORYLA | MDPSQHNPPVGHQIVHVRGDSETDLEALFNAVMNPKGAVVPQSVPMRMRKLPDSFFKPPEPKSHSRQASTDAGSGGVLTPHHVRAHSSPASLQLGAVSGGSLSGMASAGASPQHLRQSSYEIPDDVPLPPGWEMAKTSSGQRYFLNHIDQTTTWQDPRKALLQLNQATPPSTVPVQQQNLLSPASGPLPEGWEQAITPEGEIYYINHKNKTTSWLDPRLETRYALNQQRITQSAPVKQGGPLPPNPHGGVMGGNNQMRLQQMEKERIRLKQQELLRQSQRPQIDLQPSTANQDAEHCDELALRNQLPTSMDQDGSSNPVSSPMAQDARTMTANSNDPFLNSVSSGTYHSRDESTDSGLSMSSYSVPRTPDDFLNSVDEMDTGDPLAPSMATQPSRFPDYLDTIPGTDVDLGTLEGESMAVEGEELMPSLQEALSSDILNDMESVLAATKIDKESFLTWL | null | null | hippo signaling [GO:0035329]; positive regulation of transcription by RNA polymerase II [GO:0045944] | cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714] | PF00397; | 2.20.70.10;6.20.430.10; | YAP1 family | PTM: Phosphorylated by lats1 and lats2; leading to cytoplasmic translocation and inactivation. {ECO:0000305|PubMed:25778702}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P46937}. Nucleus {ECO:0000250|UniProtKB:P46937}. Cell junction {ECO:0000250|UniProtKB:P46938}. Note=Both phosphorylation and cell density can regulate its subcellular localization. Phosphorylation sequesters it in the cytoplasm by inhibiting its translocation into the nucleus. At low density, predominantly nuclear and is translocated to the cytoplasm at high density. {ECO:0000250|UniProtKB:P46937}. | null | null | null | null | null | FUNCTION: Transcriptional regulator which can act both as a coactivator and a corepressor and is the critical downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis (By similarity). Plays a key role in tissue tension and 3D tissue shape by regulating cortical actomyosin network formation (PubMed:25778702). {ECO:0000250|UniProtKB:P46937, ECO:0000269|PubMed:25778702}. | Oryzias latipes (Japanese rice fish) (Japanese killifish) |
H2LNR5 | ABCB7_ORYLA | MAPMLVSLNCGIRVQRRTLTLLIRQTSSYHIWDKSCINNGTNYQRRRTYALNSLHPQRTASWSTNRTENRRQILEAAKHLQVTDKRTCWHGNAGGRLNADPKNVLKEVHSAKILSAMLSYVWPKDRPDLRARVAVSLGLLAGAKLTNVMVPFMFKYAVDELNQMSGHMLNLNDAPSTVATMTTAVLIGYGVSRAGSALFNELRNTVFGKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLGPTVFEMFLVSAILYYKCGGEFAAVALGTLSAYTIFTILVTQWRTRFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGYLKLYESSSLKTTSTLAMLNFGQSAIFSVGLTAIMLLASKGIAAGNMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLNVDTKIKEKDLAPPLAVTPQDATIRFEDVYFEYMEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYISGQNIRDVSLESLRKALGVVPQDAVLFHNNIFYNLQYGNINATPEEVYQVARLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSITEENIMTSMKEMVKDRTSVFIAHRLSTIVDADEILVLSQGKVAERGTHQALLDTPGSLYAELWNAQNSKILNSRKSSSAPAAERLSQKEEERKKLQEEILNSVKGCGNCSC | null | null | cellular detoxification [GO:1990748]; detoxification of zinc ion [GO:0010312]; intracellular iron ion homeostasis [GO:0006879]; iron-sulfur cluster assembly [GO:0016226]; iron-sulfur cluster export from the mitochondrion [GO:0140466]; negative regulation of reactive oxygen species biosynthetic process [GO:1903427]; positive regulation of heme biosynthetic process [GO:0070455]; transmembrane transport [GO:0055085] | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | ABC-type iron-sulfur cluster transporter activity [GO:0140481]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626] | PF00664;PF00005; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily, ABCB family, Heavy Metal importer (TC 3.A.1.210) subfamily | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P40416}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P40416}. Mitochondrion {ECO:0000269|PubMed:19046159}. | CATALYTIC ACTIVITY: Reaction=(glutathione)4[2Fe(III)-2S] cluster(in) + ATP + H2O = (glutathione)4[2Fe(III)-2S] cluster(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:67028, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167627, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O75027}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67029; Evidence={ECO:0000250|UniProtKB:O75027}; | null | null | null | null | FUNCTION: Exports glutathione-coordinated iron-sulfur clusters such as [2Fe-2S]-(GS)4 cluster from the mitochondria to the cytosol in an ATP-dependent manner allowing the assembly of the cytosolic iron-sulfur (Fe/S) cluster-containing proteins and participates in iron homeostasis (By similarity). May play a role in iron and lipid metabolism (PubMed:19046159). {ECO:0000250|UniProtKB:O75027, ECO:0000269|PubMed:19046159}. | Oryzias latipes (Japanese rice fish) (Japanese killifish) |
H2LRU7 | PKD2_ORYLA | MSATRVRPQSQAGTDKPPRTLDSSEGIEMENIQHQDPGLGGVAGSPSPPSRQAWSRDNPVFEPEEEIMQADWPQASPGRRSAFTASGGSSCSSGHGGYTRAGSSTQIPRGGLYPTQTLNGQQQDRHEHPGCMKRIFQNIRILWGTELMEDGDSNRERYLWNVLRELLTYIAFLITICILTYGMISTNMYYYTKAMSQLFLDAPLSSENPKTFRSLSTMEDFWKYTQGPFLGGMYWEVWYNNQSLPGNQSFIYYENILLGVPRLRQVRVHNETCSIHEDLRDEVQGCYGVYTPSNEDNSPFGPQNGTAWVHTTESKMNASTHWGQVSKYGGGGYYQDLSRTREESGLQLQFLKDHLWLDRGTRAIFLDFSVYNGNVNLVCIARLLVEFPATGGVLTSWQFQTLRLIKYVSSWDYFVGVCEVAFCLFVLYYVVEEVLEIHIHRLHYFKNLWNCLDVLIVTLSVVAIIMSITRAAMGGDLLKGLENYTSHTSFDSLANLQVQFNNMAAVIVFFCWVKLFKFINFNKTMSQLSTTMSRCAKDLVGFAIMFFIIFLAYAQLAYLVFGTQVNDFSTFQGSVFTQFRIILGDFDFFEIKEANPVLGPIYFITFVLFIFFILMNMFLAIINDTYSEVKADMAQHRSEMEMTDFIKKGCTKALVKLRLKKTTVDDISDSLRQAGGKLNYDELLQDLKEKGHTEAEIQAIFAKYDQDGDLELTEHDHQQMRDDLEKEREDLDLERNSLTRPSSGRSFPRTQDDSEEDDDEDSGHSSRRRGSSSGGVSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLEGMERAKLKRRDVLVRLLDGVMEDERLGRDADTHREQMERLVKEELERWETDDVASQVSHPQPATPIGPRPRPPSSLSTDGLDTSANGGTHV | null | null | calcium ion transmembrane transport [GO:0070588]; cell-cell signaling by wnt [GO:0198738]; cellular response to calcium ion [GO:0071277]; detection of mechanical stimulus [GO:0050982]; detection of nodal flow [GO:0003127]; inorganic cation transmembrane transport [GO:0098662]; potassium ion transmembrane transport [GO:0071805]; protein heterotetramerization [GO:0051290]; protein tetramerization [GO:0051262]; release of sequestered calcium ion into cytosol [GO:0051209]; Wnt signaling pathway [GO:0016055] | basolateral plasma membrane [GO:0016323]; cation channel complex [GO:0034703]; ciliary membrane [GO:0060170]; cilium [GO:0005929]; cytoplasmic vesicle membrane [GO:0030659]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; plasma membrane [GO:0005886] | calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; monoatomic cation channel activity [GO:0005261]; muscle alpha-actinin binding [GO:0051371]; outward rectifier potassium channel activity [GO:0015271]; potassium channel activity [GO:0005267]; signaling receptor binding [GO:0005102]; voltage-gated calcium channel activity [GO:0005245]; voltage-gated sodium channel activity [GO:0005248] | PF18109;PF08016;PF20519; | 1.10.287.70;1.20.5.340;1.10.238.10;1.20.120.350; | Polycystin family | PTM: Phosphorylated. Phosphorylation is important for protein function; a mutant human construct that lacks the N-terminal phosphorylation sites cannot complement a zebrafish pkd2-deficient mutant. {ECO:0000250|UniProtKB:Q13563}.; PTM: N-glycosylated. The four subunits in a tetramer probably differ in the extent of glycosylation; simultaneous glycosylation of all experimentally validated sites would probably create steric hindrance. {ECO:0000250|UniProtKB:Q13563}. | SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:21307098}; Multi-pass membrane protein {ECO:0000269|PubMed:21307098}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q13563}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13563}. Cell membrane {ECO:0000250|UniProtKB:Q13563}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13563}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q13563}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q13563}. | null | null | null | null | null | FUNCTION: Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B. Can also form a functional, homotetrameric ion channel (By similarity). Functions as non-selective, voltage-gated cation channel. Required for normal oscillation of Ca(2+) levels within cilia; these oscillations of the intraciliary Ca(2+) levels can trigger cytoplasmic Ca(2+) signaling cascades (By similarity). May contribute to the release of Ca(2+) stores from the endoplasmic reticulum (By similarity). Plays a role in fluid-flow mechanosensation: forms a complex with pkd1l1 in cilia to facilitate flow detection in left/right patterning (PubMed:21307098). Required for normal specification of the body left-right axis during embryogenesis (PubMed:21307098). {ECO:0000250|UniProtKB:O35245, ECO:0000250|UniProtKB:Q13563, ECO:0000250|UniProtKB:Q6IVV8, ECO:0000269|PubMed:21307098}. | Oryzias latipes (Japanese rice fish) (Japanese killifish) |
H2MCM1 | CAHM1_ORYLA | MDKFRMMFQFLQSNQESFMNGICGIMALASAQMYSSFEFSCPCMPEYNYTYGIGLLIIPPIWFFLLGFVLNNNVSVLAEEWKRPTGRRTKDPSVLRYMLCSITQRSLIAPAVWVSVTLMDGKSFLCAFSINLDIEKFGNASLVIGMTETEKLKFLARIPCKDLFEDNEVRVAATRYIKCISQACGWMFLLMMTFTAFLIRAIRPCFTQAAFLKTKYWSHYIDIERKMFDETCKEHAKSFAKVCIHQYFENISGEMQNFHRHQSKDTSDAEEEEKQRSDEDKLLGIKAQEDMNKVLWNWHTCKPALALRKDHLDTESNGKLNGTMNGAVNGFAQGHTHDVAKKEWAVYYSKV | null | null | null | membrane [GO:0016020] | monoatomic cation channel activity [GO:0005261] | PF14798; | null | CALHM family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:D3Z291}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:D3Z291}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8IU99}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8IU99}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q8IU99}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP(in) = ATP(out); Xref=Rhea:RHEA:75687, ChEBI:CHEBI:30616; Evidence={ECO:0000269|PubMed:32832629}; CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:D3Z291, ECO:0000250|UniProtKB:Q8IU99}; CATALYTIC ACTIVITY: Reaction=Mg(2+)(in) = Mg(2+)(out); Xref=Rhea:RHEA:29827, ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8IU99}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:D3Z291, ECO:0000250|UniProtKB:Q8IU99}; CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:D3Z291, ECO:0000250|UniProtKB:Q8IU99}; CATALYTIC ACTIVITY: Reaction=Li(+)(in) = Li(+)(out); Xref=Rhea:RHEA:78551, ChEBI:CHEBI:49713; Evidence={ECO:0000250|UniProtKB:Q8IU99}; CATALYTIC ACTIVITY: Reaction=Rb(+)(in) = Rb(+)(out); Xref=Rhea:RHEA:78547, ChEBI:CHEBI:49847; Evidence={ECO:0000250|UniProtKB:Q8IU99}; CATALYTIC ACTIVITY: Reaction=Cs(+)(in) = Cs(+)(out); Xref=Rhea:RHEA:78555, ChEBI:CHEBI:49547; Evidence={ECO:0000250|UniProtKB:Q8IU99}; CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:D3Z291, ECO:0000250|UniProtKB:Q8IU99}; | null | null | null | null | FUNCTION: Pore-forming subunit of a voltage-gated ion channel. Has poor ion selectivity and forms a wide pore that mediates permeation of small ions including Ca(2+), Na(+), K(+) and Cl(-), as well as larger ions such as ATP(4-). {ECO:0000250|UniProtKB:D3Z291, ECO:0000250|UniProtKB:Q8IU99, ECO:0000269|PubMed:32832629}. | Oryzias latipes (Japanese rice fish) (Japanese killifish) |
H2N0D4 | AMY_ORYLA | MKLFVLIALFGLGFAQHNPNTRDGRTAIVHLFEWRWADIAAECERFLGPKGFAGVQISPPNEHILVSSPWRPWWQRYQPISYNLCSRSGGENELRDMITRCNNVGVNVYVDAVINHMCGAGGGEGTHSSCGSWFNANNKDFPSVPYSNLDFNDGKCKTGSGNIENYGDPYQVRDCRLVGLLDLALEKDYVRGKVADFMNKLIDMGVAGFRVDACKHMWPGDLDNVYRRLNNLNTKWFPGGSRPFIFQEVIDLGGEPITTGEYVGLGRVTEFKYGARLGELFRKWNGQKLSYTKNWGEGWGFMADGNAVVFTDNHDNQRGHGAGGASILTFWDPRLYKMAVGYMLAHPYGFTRVMSSYSWDRNFVNGKDENDWIGPPSNGDGSTKPVPINPDQTCGDGWVCEHRWRQIMNMVQFRNVVNGQPHANWWDNGNNQVAFGRGNRGFIVFNNDDWALDVTLNTGLPGGTYCDVISGNKDGGSCTGKQITVGGDGRAHFYINNSEEDPFIAIHADSKL | 3.2.1.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:22613096}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:22613096}; COFACTOR: Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:22613096}; Note=Binds 1 Cl(-) ion per subunit. {ECO:0000269|PubMed:22613096}; | carbohydrate metabolic process [GO:0005975] | extracellular space [GO:0005615] | alpha-amylase activity [GO:0004556]; metal ion binding [GO:0046872] | PF00128;PF02806; | 3.20.20.80;2.60.40.1180; | Glycosyl hydrolase 13 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:22613096}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.18 mg/ml for potato amylopectin {ECO:0000269|PubMed:22613096}; Vmax=2560 umol/min/mg enzyme {ECO:0000269|PubMed:22613096}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.1. {ECO:0000269|PubMed:22613096}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:22613096}; | FUNCTION: Catalyzes the hydrolysis of alpha-1,4 glycosidic linkages in starch, glycogen and similar oligosaccharides. {ECO:0000269|PubMed:22613096}. | Oryzias latipes (Japanese rice fish) (Japanese killifish) |
H2QII6 | RBP2_PANTR | MRRSKADVERYIASVQGSTPSPRQKSIKGFYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDGRAKYWVERAAKLFPGSPAVYKLKEQLLDCEGEDGWNKLFDLIQSELYVRPDDVHVNIRLVEVYRSTKRLKDAVAHCHEAERNIALRSSLEWNSCVVQTLKEYLESLQCLESDKSDWRATNTDLLLAYANLMLLTLSTRDVQESRELLESFDSALQSVKSLGGNDELSATFLEMKGHFYMHAGSLLLKMGQHSSNVQWRALSELAALCYLIAFQVPRPKIKLIKGEAGQNLLEMMACDRLSQSGHMLLNLSRGKQDFLREIVETFANKSGQSALYDALFSSQSPKDTSFLGSDDIGNIDVREPELEDLARYDVGAIRAHDGSLQHLTWLGLQWNSLPALPGIRKWLKQLFHHLPQETSRLETNAPESICILDLEVFLLGVVYTSHLQLKEKCNSHHSSYQPLCLPLPVCKQLCTERQKSWWDAVCTLIHRKAVPGNAAKLRLLVQHEINTLRAQEKHGLQPALLVHWAKCLQKTGSGLNSFYDQREYIGRSVHYWKKVLPLLKIIKKKNSIPEPIDPLFKHFHSVDIQASEIVEYEEDAHITFAILDVVNGNIEDAMTAFESIQSVVSYWNLALIFHRKAEDIENDALSPEEQEECKNYLRKTRDYLIKIIDDSDSNLSVVKKLPVPLESVKEMLKSVMQELEAYSEGGPLYTNGSLRNADSEIKHSTPSHTRYSLSPSKSYKYSPKTPPRWAEDQNSLLKMICQQVEAIKKEMQELKLNSSNSASPHRWPTENYGPDSVPDGYQGSQTFHGAPLTVATTGPSVYYSQSPAYNSQYLLRPAANVTPTKGPVYGMNRLPPQQHIYAYPQQMHTPPVQSSSACMFSQEMYGPPALRFESPATGILSPRGDDYFNYNVQQTSTNPPLPEPGYFTKPPIAAHASRSAESKTIEFGKTNFVQPMPGEGLRPSLPTQAHTTQPTPFKFNSNFKSNDGDFTFSSPQVVTQPPPAAYSNSESLLGLLTSDKPLQGDGYSGAKPIPGGQTIGPRNTFNFGSKNVSGISFTENMGSSQQKNSGFRRSDDMFTFHGPGKSVFGTPTLETANKNHETDGGSAHGDDDDDGPHFEPVVPLPDKIEVKTGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQSILKAPGTNVATASNQAVRIVKEPTSHDNKDICKSDAGNLNFEFQFAKKEGSWWHCNSCSLKNASTAKKCVSCQNLNPSNKELVGPPLAETVFTPKTSPENVQDRFALVTPKKEGHWDCSICLVRNEPTVSRCIACQNTKSANKSGSSFVHQASFKFGQGDLPKPINSDFRSVFSTKEGQWDCSACLVQNEGSSTKCAACQNPRKQSLPATSIPTPASFKFGTSETSKTLKSGFEDMFAKKEGQWDCSSCLVRNEANATRCVACQNPDKPSPSTSVPAPASFKFGTSETSKAPKSGFEGMFTKKEGQWDCSVCLVRNEASATKCVACQNPGKQNQTTSAVSTPASSETSRAPKSGFEGMFTKKEGQWDCSVCLVRNEASATKCIACQSPGKQNQTTSAVSTPASSETSKAPKSGFEGMFTKKEGQWDCSVCLVRNEASATKCIACQCPSKQNQTTAISTPASSEISKAPKSGFEGMFIRKGQWDCSVCCVQNESSSLKCVACDASKPTHKPIAEAPSAFTLGSEMKLHDSPGSQVGTGFKSNFSEKASKFGNTEQGFKFGHVDQENSPSFMFQGSSNTEFKSTKEGFSIPVSADGFKFGISEPGNQEKKSEKPLENDTGFQAQDISGQKNGSGVIFGQTSSTFTFADLAKSTSGEGFQFGKKDPNFKGFSGAGEKLFSSQYGKMANKANTSGDFEKDDDAYKTEDSDDIHFEPVVQMPEKVELVTGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRLLLDIPLQTPHKLVDTGRAAKLIQRAEEMKSGLKDFKTFLTNDQTKVTEEENKGSGTGAAGASDTTIKPNPENTGPTLEWDNYDLREDALDDSVSSSSVHASPLASSPVRKNLFRFGESTTGFNFSFKSALSPSKSPGKLNQSGTSVGTDEESDVTQEEERDGQYFEPVVPLPDLVEVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWLWTAYDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTAQEKDSLITPHVSRSSTPRESPCGKIAVAVLEETTRERTDVTQGDDVADAASEVEVSSTSETTTKAVVSPPKFVFGSESVKSIFSSEKSKPFAFGNTSATGSLFGFSFNAPLKSNNSETSSVAQSGSESKVEPNKCELSKNSDIEQSSDSKVKNLSASFPTEESSINYTFKTPEKAKEKKKPEDSPSDDDVLIVYELTPTAEQKALATKLKLPPTFFCYKNRPDYVSEEEEDDEDFETAVKKLNGKLYLEGSEKCRPLEENTADNEKECIIVWEKKPTVEEKAKADTLKLPPTFFCGVCSDTDEDNGNGEDFQSELQKVQEAQKSQTEEITSTTDSVYTGGTEVMVPSFCKSEEPDSITKSISSPSVSSETMDKPVDLSTRKEIDTDSTSQGESKIVSFGFGSSTGLSFADLASSNSGDFAFGSKDKNFQWANTGAAVFGTQSVGTQSAGKVGEDEDGSDEEVVHNEDIHFEPIVSLPEVEVKSGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQNLMKLQKGHVSLAAELSKETNPVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGEKGFGFKNSIFHRVIPDFVCQGGDITKHDGTGGQSIYGDKFEDENFDVKHTGPGLLSMANQGQNTNNSQFFITLKKAELLDFKHVVFGFVKDGMDTVKKIESFGSPKGSVCRRITITECGQI | 2.3.2.- | null | mRNA transport [GO:0051028]; NLS-bearing protein import into nucleus [GO:0006607]; protein folding [GO:0006457]; protein sumoylation [GO:0016925] | annulate lamellae [GO:0005642]; cytoplasm [GO:0005737]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643] | GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; RNA binding [GO:0003723]; transferase activity [GO:0016740] | PF12185;PF00160;PF00638;PF00641; | 2.40.100.10;2.30.29.30;1.25.40.10;4.10.1060.10; | RanBP2 E3 ligase family | PTM: Polyubiquitinated by PRKN, which leads to proteasomal degradation. {ECO:0000250|UniProtKB:P49792}.; PTM: The inner channel of the NPC has a different redox environment from the cytoplasm and allows the formation of interchain disulfide bonds between some nucleoporins, the significant increase of these linkages upon oxidative stress reduces the permeability of the NPC. {ECO:0000250|UniProtKB:Q9ERU9}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22959972}. Nucleus membrane {ECO:0000269|PubMed:22959972}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:22959972}. Nucleus envelope {ECO:0000250|UniProtKB:P49792}. Note=Detected in diffuse and discrete intranuclear foci. Cytoplasmic filaments. {ECO:0000250|UniProtKB:P49792}. | null | null | PATHWAY: Protein modification; protein sumoylation. | null | null | FUNCTION: E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1. Inhibits EIF4E-dependent mRNA export. Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB. Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (By similarity). Binds single-stranded RNA (in vitro) (PubMed:22959972). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity. {ECO:0000250|UniProtKB:P49792, ECO:0000269|PubMed:22959972}. | Pan troglodytes (Chimpanzee) |
H2QL32 | PDE9A_PANTR | MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCCQEGQRIPPEREELIQSVLAQVAEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDVPTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLFCVHDNYRNNPFHNFRHCFCVAQMMYSMVWLCSLQENFSQMDILILMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNIFSNIPPDGFKQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIMLQPLWESRDRYEELKRIDDAMKELQKKTDSLTSGATEKSRERSRDVKNSEGDCA | 3.1.4.35 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O76083}; Note=Binds 1 Zn(2+) ion per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Tightly binds zinc. {ECO:0000250|UniProtKB:O76083}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O76083}; Note=Binds 1 Mg(2+) ions per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Binds magnesium less tightly than zinc. {ECO:0000250|UniProtKB:O76083}; | cAMP-mediated signaling [GO:0019933]; cGMP catabolic process [GO:0046069]; cGMP metabolic process [GO:0046068]; positive regulation of cardiac muscle hypertrophy [GO:0010613] | endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471]; ruffle membrane [GO:0032587]; sarcolemma [GO:0042383] | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; metal ion binding [GO:0046872] | PF00233; | 1.10.1300.10; | Cyclic nucleotide phosphodiesterase family, PDE9 subfamily | null | SUBCELLULAR LOCATION: Cell projection, ruffle membrane {ECO:0000250|UniProtKB:O76083}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O76083}. Golgi apparatus {ECO:0000250|UniProtKB:O76083}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O76083}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:O76083}. | CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746, ChEBI:CHEBI:58115; EC=3.1.4.35; Evidence={ECO:0000250|UniProtKB:O76083}; | null | PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from 3',5'-cyclic GMP: step 1/1. | null | null | FUNCTION: Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP. Specifically regulates natriuretic-peptide-dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart. Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein. In brain, involved in cognitive function, such as learning and long-term memory. {ECO:0000250|UniProtKB:O76083, ECO:0000250|UniProtKB:Q8QZV1}. | Pan troglodytes (Chimpanzee) |
H3BCW1 | ADPRS_LATCH | MSAVGRLAAVSLAQVRGALCGALLGDCMGAEFEGSDAVELPDVLEFVRLLEKEKKAGTLFYTDDTAMTRAVIQSLIAKPDFDEVDMAKRFAEEYKKEPTRGYGAGVVQVFKKLLSPKYSDVFQPAREQFDGKGSYGNGGAMRVASIALAYPNIQDVIKFARRSAQLTHASPLGYNGAILQALAVHFALQGELKRDTFLEQLIGEMERIEGGEMSASDAGEHDRPNEVKLPFCSRLKKIKEFLASSNVPKADIVDELGHGIAALESVPTAIYSFLHCMESDPDIPDLYNNLQRTIIYSISLGGDTDTIATMAGAIAGAYYGMDQVTPSWKRSCEAIVETEESAVKLYELYCKQLKTP | 3.2.1.143; 3.2.2.-; 3.5.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:30472116}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305|PubMed:30472116}; Note=Binds 2 magnesium ions per subunit. {ECO:0000269|PubMed:30472116}; | DNA repair [GO:0006281]; negative regulation of necroptotic process [GO:0060546]; peptidyl-serine ADP-deribosylation [GO:0140290] | chromosome [GO:0005694]; mitochondrial matrix [GO:0005759]; nucleus [GO:0005634] | magnesium ion binding [GO:0000287]; poly(ADP-ribose) glycohydrolase activity [GO:0004649] | PF03747; | 1.10.4080.10; | ADP-ribosylglycohydrolase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NX46}. Cytoplasm {ECO:0000250|UniProtKB:Q9NX46}. Chromosome {ECO:0000250|UniProtKB:Q9NX46}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q9NX46}. Note=Recruited to DNA lesion regions following DNA damage; ADP-D-ribose-recognition is required for recruitment to DNA damage sites. {ECO:0000250|UniProtKB:Q9NX46}. | CATALYTIC ACTIVITY: Reaction=[(1''->2')-ADP-alpha-D-ribose](n) + H2O = [(1''->2')-ADP-alpha-D-ribose](n-1) + ADP-D-ribose; Xref=Rhea:RHEA:52216, Rhea:RHEA-COMP:16922, Rhea:RHEA-COMP:16923, ChEBI:CHEBI:15377, ChEBI:CHEBI:57967, ChEBI:CHEBI:142512; EC=3.2.1.143; Evidence={ECO:0000269|PubMed:30472116}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52217; Evidence={ECO:0000269|PubMed:30472116}; CATALYTIC ACTIVITY: Reaction=1''-O-acetyl-ADP-alpha-D-ribose + H2O = acetate + ADP-D-ribose + H(+); Xref=Rhea:RHEA:58112, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57967, ChEBI:CHEBI:142511; Evidence={ECO:0000250|UniProtKB:Q9NX46}; CATALYTIC ACTIVITY: Reaction=H2O + O-(ADP-D-ribosyl)-L-seryl-[protein] = ADP-D-ribose + L-seryl-[protein]; Xref=Rhea:RHEA:58256, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15091, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:57967, ChEBI:CHEBI:142556; Evidence={ECO:0000269|PubMed:30472116}; CATALYTIC ACTIVITY: Reaction=alpha-NAD(+) + H2O = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:68792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57967, ChEBI:CHEBI:77017; Evidence={ECO:0000250|UniProtKB:Q9NX46}; | null | null | null | null | FUNCTION: ADP-ribosylhydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine and threonine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose (PubMed:30472116). Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response (PubMed:30472116). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (By similarity). Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds (By similarity). Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos (PubMed:30472116). Also hydrolyzes free poly(ADP-ribose) in mitochondria (By similarity). Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins (By similarity). Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers (By similarity). {ECO:0000250|UniProtKB:Q9NX46, ECO:0000269|PubMed:30472116}. | Latimeria chalumnae (Coelacanth) |
H3BV60 | TGR3L_HUMAN | MLGTVLLLALLPGITTLPSGPPAPPFPAAPGPWLRRPLFSLKLSDTEDVFPRRAGPLEVPADSRVFVQAALARPSPRWGLALHRCSVTPSSRPAPGPALALLREGCPADTSVAFPPPPPPSPGAARPARFSFRLRPVFNASVQFLHCQLSRCRRLRGVRRAPAPLTPPPPPPPSRCLPQDEACADTGSGSAEGLAADGPHLHTLTQPIVVTVPRPPPRPPKSVPGRAVRPEPPAPAPAALEPAPVVALVLAAFVLGAALAAGLGLVCAHSAPHAPGPPARASPSGPQPRRSQ | null | null | cell migration [GO:0016477]; epithelial to mesenchymal transition [GO:0001837]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; transforming growth factor beta receptor signaling pathway [GO:0007179] | cell surface [GO:0009986]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | glycosaminoglycan binding [GO:0005539]; transforming growth factor beta binding [GO:0050431]; transforming growth factor beta receptor activity [GO:0005024]; type II transforming growth factor beta receptor binding [GO:0005114] | PF00100; | 2.60.40.4100; | null | PTM: Glycosylated. {ECO:0000269|PubMed:34910520}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:33396509, ECO:0000269|PubMed:34910520}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Expressed in gonadotrope cells, acts as an inhibin B coreceptor and regulates follicle-stimulating hormone (FSH) levels and female fertility. {ECO:0000269|PubMed:34910520}. | Homo sapiens (Human) |
H3JQW0 | OTEMO_PSEPU | MSNRAKSPALDAVVIGAGVTGIYQAFLINQAGMKVLGIEAGEDVGGTWYWNRYPGCRLDTESYAYGYFALKGIIPEWEWSENFASQPEMLRYVNRAADAMDVRKHYRFNTRVTAARYVENDRLWEVTLDNEEVVTCRFLISATGPLSASRMPDIKGIDSFKGESFHSSRWPTDAEGAPKGVDFTGKRVGVIGTGATGVQIIPIAAETAKELYVFQRTPNWCTPLGNSPMSKEKMDSLRNRYPTILEYVKSTDTAFPYHRDPRKGTDVSESERDAFFEELYRQPGYGIWLSGFRDLLLNKESNKFLADFVAKKIRQRVKDPVVAEKLIPKDHPFGAKRVPMETNYYETYNRDNVHLVDIREAPIQEVTPEGIKTADAAYDLDVIIYATGFDAVTGSLDRIDIRGKDNVRLIDAWAEGPSTYLGLQARGFPNFFTLVGPHNGSTFCNVGVCGGLQAEWVLRMISYMKDNGFTYSEPTQAAENRWTEEVYADFSRTLLAEANAWWVKTTTKPDGSVVRRTLVHVSGGPEYRKRCEQVAYNNYNGFELA | 1.14.13.160 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:22267661, ECO:0000269|PubMed:6848481}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:22267661, ECO:0000269|PubMed:6848481}; | (+)-camphor catabolic process [GO:0019383] | null | FAD binding [GO:0071949]; identical protein binding [GO:0042802]; monooxygenase activity [GO:0004497]; NADP binding [GO:0050661]; protein homodimerization activity [GO:0042803] | PF07992; | 3.50.50.60; | FAD-binding monooxygenase family | null | null | CATALYTIC ACTIVITY: Reaction=[(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetyl-CoA + H(+) + NADPH + O2 = [(2R)-3,3,4-trimethyl-6-oxo-3,6-dihydro-1H-pyran-2-yl]acetyl-CoA + H2O + NADP(+); Xref=Rhea:RHEA:33015, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64784, ChEBI:CHEBI:64785; EC=1.14.13.160; Evidence={ECO:0000269|PubMed:22286514, ECO:0000269|PubMed:6848481}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.018 mM for OT-CoA (at pH 9 and at 25 degrees Celsius) {ECO:0000269|PubMed:22267661, ECO:0000269|PubMed:22286514, ECO:0000269|PubMed:6848481}; KM=0.032 mM for 2-n-hexyl cyclopentanone (at pH 9 and at 25 degrees Celsius) {ECO:0000269|PubMed:22267661, ECO:0000269|PubMed:22286514, ECO:0000269|PubMed:6848481}; KM=0.16 mM for 2-oxocyclohexyl ethyl acetate (at pH 9 and at 25 degrees Celsius) {ECO:0000269|PubMed:22267661, ECO:0000269|PubMed:22286514, ECO:0000269|PubMed:6848481}; KM=0.31 mM for 2-oxocyclopentyl ethyl acetate (at pH 9 and at 25 degrees Celsius) {ECO:0000269|PubMed:22267661, ECO:0000269|PubMed:22286514, ECO:0000269|PubMed:6848481}; KM=0.6 mM for 4-methyl cyclohexanone (at pH 9 and at 25 degrees Celsius) {ECO:0000269|PubMed:22267661, ECO:0000269|PubMed:22286514, ECO:0000269|PubMed:6848481}; KM=1.4 mM for 2-methyl cyclohexanone (at pH 9 and at 25 degrees Celsius) {ECO:0000269|PubMed:22267661, ECO:0000269|PubMed:22286514, ECO:0000269|PubMed:6848481}; | PATHWAY: Terpene metabolism; (R)-camphor degradation. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9. {ECO:0000269|PubMed:22267661, ECO:0000269|PubMed:22286514, ECO:0000269|PubMed:6848481}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 20 degrees Celsius. {ECO:0000269|PubMed:22267661, ECO:0000269|PubMed:22286514, ECO:0000269|PubMed:6848481}; | FUNCTION: Involved in the degradation of (+)-camphor. Catalyzes the lactonization of 2-oxo-delta(3)-4,5, 5-trimethylcyclopentenylacetyl-CoA (OT-CoA), a key intermediate in the metabolism of camphor. 2-Oxocyclopentyl ethyl acetate is also a good substrate, as is 2-oxocyclohexyl ethyl acetate and methyl-substituted cyclohexanones, but free acid is a poor substrate. {ECO:0000269|PubMed:22267661, ECO:0000269|PubMed:22286514, ECO:0000269|PubMed:6848481}. | Pseudomonas putida (Arthrobacter siderocapsulatus) |
H3K2Y6 | MED12_ARATH | MQRYHAANCTSAVNNSAIGGASARDSGRADSSSIGNYSLNSRRPPPLTPYKLKCEKDGLNSRLGPPDFHPPTSNSPEENLTKEYVQFGYKETVDGLKESEEIILSQVHTFSKPVVHKCKEAVRKCLRAINESRALKRKAGQVYGVPLSGSLLCKPGFPEQRSCGEETKKRWIESLSQQHKRLRSLADNIPGYRRKTLFEVLIRNNVPLLRATWFIKVTYLNQVRPSPAAISSGTPDKTQASRCEQWTKDVIEYLQYLLDELLSRNSSFPAQQTRDRSPQMLYTGSMQKNSPASTSLYGEETSLHFKWWYMVRLLQWHHAEGLLFPNLIVDWVLKLLQEKEIFEILQLLLPIVYGVLESIVLSQTYVQSLVAIAVRFIQEPAPGGSDLVDNSRRAYTLSALIEMVRYLVLAAPDTFVASDFFPLPPSVAACGPNDVSYTSKAYENLEKLRSNSAEISAQFQGRGVLSRFEFLSFDYTISTIQRSADDLAKIASAGYPQHNVAKAVQALDKALSDGDIRAAYSYLFEDLCNGAVDEAWITDVSPCLRSSLRWIGAISTSFVCSVFFLIEWATCDFRDFRAGVPKDIKFSGRKDCSQVYLVIQLLKQKILGGEFTARKGKNCRNNFLGVSKPSGSMDAFESPGPLHDIIVCWIDQHEVHKGGAKRLQLLVFELIRSGIFNPIAYVRQLIVSGMIDVIQPAVDPERRMRHHRILKQLPGCFVHETLEEAQLFGGDKLSEAVRTYSNERRLLLRELLVEKGKYWNNLVLSDQKSKKISTSLSSVIFPRACNAKSNSKGPRKHTKSSVDIRELKERISALLQFPGMSCGVETPVRDEFQNSVKRSSGSVYSKMDQPEATPGCEDCRRAKRPKMNDEKSSCYQGNSPIASDEEDNWWIKKGSKTVESSLKVDPQIEITKQVPRGRQKMARKTQSLAQLQAARIEGSQGASTSHVCDNKVSCPHHGPGVEGENQKVVDVFRTSTPVDMVSVGNSLKQLQFVDKRSIAVWLTTAVRQLVEEPQKSSVRVGQFNRGAPVEEKNTIRWKLGADELYSILFLLDISLDLVSAVKFLLWLLPKANSTPSFAVQGGRNLVTVPRNVENNMCEIGEAILVSSLRRYENILLSADLVPEAMTALMNRAASLMSSNGKISGSAALVYTRYILKRYGSLPSVVEWHNNFKATSEKKLLSELDHTRSGNGEYGNPLGVPAGVDNPDDYLRKKISIGGARPSRVGLSMRDVLQRHVEEATHYLKKLIGTGTMKASLAEKNDDGYQVAQQIVVGLMDCIRQTGGAAQEGDPSLVSSAVSAIINSVGLSVARITDFSLGNIYQNHPSGVDSSNIARYILRIHITCLCLLKEALGERQSRVFEIALATESSTALTGVFAPVKGSRGQHQLSPESYDSNANNSTIDMSNGTGKMALSRATKITAAVSALVIGSITHGVITLERIVGLLRLKDYLDFVQFVRRTKSSSNGSARSMGASKVESPIEVYVHWFRLLVGNCKTVSEGLVLELVGESSVVAISRMQRMLPLKLVFPPAYSIIAFVLWRPFVSNSNSNSSVHEDTHRLYQSLTMAFHDVIKHLPFRDVCFRDTQGLYELIVADSTDAEFASVFESHGLDMHLKSVAFAPLRARLFLNSLIDCKVPSSGYSHEGVSEAKNRHQGNGTKLVDKLVSVLDCLQPAKFHWQWVELRLLLNEQALAEKLENHDMPLTDAIRSSCPTSEKPDASENEKNFIQILLTRLLVRPDAVPLFSEVVHLFGRSVEDSMLKQAEWFLAGQDVLFGRKTIRQKLIIVGESKGLPTKPQFWKPWGWCNSSSSDHITANKAGKKRKFEITSIEEGEVIEEGSGSRKVLLPRVLDENSPSVGYGITTERAFVQLVLPCIDQSSDESRSTFVNELVRQFSNIEQQLSSVTNRSTTSNKQMGTASSGSEISSNKGSTRKGLRGGSPSLARRSSANTTDTSPPPSPAALRASMSLRLQFLLRLLPVICGEPSFKNTRHALASTIVRLLGSRVVYEDYAVCSPRSELSKAETESTIDPSSMADLSSEVLFDRLLFVLHGLLSNHQPKWLKPRPSSNESSKDFTLFDRDAAESLQNELSRMQLPDTIRWRIQAAMPILLPSLRCSLSCQPHSVPPTALTLVQPSGSTAAAGTNQRNSPAISKSGTAAAQGKLKPTMLAPHQQQEADNTDVVDPWTLLEDGTSSGLSSSNASNSSDMANLRATCWLKGAVRVRRTDLTYVGSVDDDS | null | null | regulation of development, heterochronic [GO:0040034]; regulation of radial pattern formation [GO:0090213]; regulation of transcription by RNA polymerase II [GO:0006357] | mediator complex [GO:0016592]; nucleus [GO:0005634] | transcription coregulator activity [GO:0003712] | PF09497; | null | Mediator complex subunit 12 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22247249}. | null | null | null | null | null | FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Flowering regulator which suppresses FLC expression, promotes FT and TSF expression and up-regulates SOC1 and FUL mainly in an FT-dependent manner under long-day conditions. Involved in diverse developmental aspects through gene regulation and modulation of the auxin response. Acts closely together with MAB13. Involved in the regulation of embryo patterning and cotyledon organogenesis by transiently repressing a transcriptional program that interferes with this process. {ECO:0000269|PubMed:20023166, ECO:0000269|PubMed:22247249}. | Arabidopsis thaliana (Mouse-ear cress) |
H6LBB1 | LCTC_ACEWD | MAGIKIIKENVDRETFEALAEICPFDAFSYENDKLEVTAACKMCKMCLKKGPEGVLILEEDEKVAIDKSLYRGITVYVDHIEGQIHPVTFELIGKARELAAVIGHPVYALLMGTNITEKADELLKYGVDKVFVYDKPELKHFVIEPYANVLEDFIEKVKPSSILVGATNVGRSLAPRVAARYRTGLTADCTILEMKENTDLVQIRPAFGGNIMAQIVTENTRPQFCTVRYKVFTAPERVNEPWGDVEMMDIEKAKLVSAIEVMEVIKKEKGIDLSEAETIVAVGRGVKCEKDLDMIHEFAEKIGATVACTRPGIEAGWFDARLQIGLSGRTVKPKLIIALGISGAVQFAAGMQNSEYIIAINSDPKAPIFNIAHCGMVGDLYEILPELLTMIEGPENNKDTETISIPEAIETPERMVV | 1.1.1.436 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P13804}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P13804}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:H6LGM8}; | fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539] | cytoplasm [GO:0005737] | 4 iron, 4 sulfur cluster binding [GO:0051539]; electron transfer activity [GO:0009055]; flavin adenine dinucleotide binding [GO:0050660]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491] | PF01012;PF00766; | 3.30.70.20;3.40.50.620;3.40.50.1220; | ETF alpha-subunit/FixB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24762045}. | CATALYTIC ACTIVITY: Reaction=lactate + 2 NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = 2 NADH + 2 oxidized [2Fe-2S]-[ferredoxin] + pyruvate; Xref=Rhea:RHEA:46964, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15361, ChEBI:CHEBI:24996, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.436; Evidence={ECO:0000269|PubMed:24762045}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=31 uM for ferredoxin {ECO:0000269|PubMed:24762045}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:24762045}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 20 and 30 degrees Celsius. {ECO:0000269|PubMed:24762045}; | FUNCTION: The lactate dehydrogenase-Etf complex catalyzes the oxidation of lactate to pyruvate. It uses flavin-based electron confurcation to drive endergonic lactate oxidation with NAD(+) as oxidant at the expense of simultaneous exergonic electron flow from reduced ferredoxin to NAD(+). The electron transfer flavoprotein (Etf) mediates the electron transfer between the different donors and acceptors. {ECO:0000269|PubMed:24762045}. | Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1) |
H6U1I8 | GLIP_TANCI | MAVASRKLGALVLVAVLCLSLPTGCLSSQQAAALFIFGDSVFDPGNNNHINTHVNFKANFWPYGQSYFSSPTGRFSDGRIIPDFIAEYASLPIIPAYLEPNNDFTHGANFASAGAGALIASHAGLAVGLQTQLRYFGDLVDHYRQNLGDIKSRQLLSDAVYLFSCGGNDYQSPYYPYTQEQYVDIVIGNMTNVIKGIYEKGGRKFGVVNVPLIGCWPGMRAKQPGNTCNTEVDELTRLHNQAFAKRLEQLEKQLEGFVYAKFDLSTAILNRMKNPSKYGFKEGESACCGSGPFGGNYDCGRIKEFGLCDNATEYFFFDPFHPNELASRQFAEMFWDGDSMVTQPYNLKALFEGKPSTKYLPNDEL | 3.1.1.- | null | isoprenoid biosynthetic process [GO:0008299]; lipid catabolic process [GO:0016042]; response to wounding [GO:0009611] | extracellular space [GO:0005615] | acyltransferase activity [GO:0016746]; hydrolase activity, acting on ester bonds [GO:0016788]; lipase activity [GO:0016298]; serine O-acyltransferase activity [GO:0016412] | PF00657; | 3.40.50.1110; | 'GDSL' lipolytic enzyme family | null | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:22385412}. | CATALYTIC ACTIVITY: Reaction=(1R,3R)-chrysanthemoyl-CoA + (Z,S)-pyrethrolone = CoA + pyrethrin I; Xref=Rhea:RHEA:60744, ChEBI:CHEBI:27815, ChEBI:CHEBI:39111, ChEBI:CHEBI:57287, ChEBI:CHEBI:143950; Evidence={ECO:0000269|PubMed:22385412}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60745; Evidence={ECO:0000269|PubMed:22385412}; CATALYTIC ACTIVITY: Reaction=(1R,3R)-pyrethroyl-CoA + (Z,S)-pyrethrolone = CoA + pyrethrin II; Xref=Rhea:RHEA:60748, ChEBI:CHEBI:27474, ChEBI:CHEBI:39111, ChEBI:CHEBI:57287, ChEBI:CHEBI:143953; Evidence={ECO:0000269|PubMed:22385412}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60749; Evidence={ECO:0000269|PubMed:22385412}; CATALYTIC ACTIVITY: Reaction=(1R,3R)-chrysanthemoyl-CoA + (Z,S)-jasmololone = CoA + jasmolin I; Xref=Rhea:RHEA:60752, ChEBI:CHEBI:39113, ChEBI:CHEBI:57287, ChEBI:CHEBI:143950, ChEBI:CHEBI:143951; Evidence={ECO:0000269|PubMed:22385412}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60753; Evidence={ECO:0000269|PubMed:22385412}; CATALYTIC ACTIVITY: Reaction=(1R,3R)-chrysanthemoyl-CoA + (Z,S)-cinerolone = cinerin I + CoA; Xref=Rhea:RHEA:60756, ChEBI:CHEBI:3706, ChEBI:CHEBI:57287, ChEBI:CHEBI:143950, ChEBI:CHEBI:143952; Evidence={ECO:0000269|PubMed:22385412}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60757; Evidence={ECO:0000269|PubMed:22385412}; CATALYTIC ACTIVITY: Reaction=(1R,3R)-pyrethroyl-CoA + (Z,S)-jasmololone = CoA + jasmolin II; Xref=Rhea:RHEA:60760, ChEBI:CHEBI:39114, ChEBI:CHEBI:57287, ChEBI:CHEBI:143951, ChEBI:CHEBI:143953; Evidence={ECO:0000269|PubMed:22385412}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60761; Evidence={ECO:0000269|PubMed:22385412}; CATALYTIC ACTIVITY: Reaction=(1R,3R)-pyrethroyl-CoA + (Z,S)-cinerolone = cinerin II + CoA; Xref=Rhea:RHEA:60764, ChEBI:CHEBI:3707, ChEBI:CHEBI:57287, ChEBI:CHEBI:143952, ChEBI:CHEBI:143953; Evidence={ECO:0000269|PubMed:22385412}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60765; Evidence={ECO:0000269|PubMed:22385412}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=768 uM for (1R,3R)-chrysanthemoyl CoA (in the presence of (S)-pyrethrolone, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; KM=30.7 uM for (S)-pyrethrolone (in the presence of (1R,3R)-chrysanthemoyl CoA, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; KM=1050 uM for (1R,3R)-pyrethroyl CoA (in the presence of (S)-pyrethrolone, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; KM=31.7 uM for (S)-pyrethrolone (in the presence of (1R,3R)-pyrethroyl CoA, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; Vmax=1.52 nmol/sec/mg enzyme with (1R,3R)-chrysanthemoyl CoA as substrate (in the presence of (S)-pyrethrolone, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; Vmax=0.95 nmol/sec/mg enzyme with (1R,3R)-pyrethroyl CoA as substrate (in the presence of (S)-pyrethrolone, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; Vmax=1.17 nmol/sec/mg enzyme with (S)-pyrethrolone as substrate (in the presence of (1R,3R)-chrysanthemoyl CoA, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; Vmax=0.65 nmol/sec/mg enzyme with (S)-pyrethrolone as substrate (in the presence of (1R,3R)-pyrethroyl CoA, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; Vmax=0.0105 nmol/sec/mg enzyme with pyrethrin I as substrate (in the absence of CoA, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; Vmax=0.0305 nmol/sec/mg enzyme with pyrethrin I as substrate (in the presence of CoA, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; Vmax=0.88 nmol/sec/mg enzyme with p-nitrophenyl butanoate as substrate (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; Vmax=0.309 nmol/sec/mg enzyme with p-nitrophenyl octanoate as substrate (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; | PATHWAY: Isoprenoid biosynthesis. {ECO:0000269|PubMed:22385412}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:22385412}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25 degrees Celsius. {ECO:0000269|PubMed:22385412}; | FUNCTION: Component of the monoterpenoid pyrethrins biosynthesis; pyrethrins are widely used plant-derived pesticide (PubMed:30468448). Acyltransferase that catalyzes the esterification of terpene acids and lipid alcohol substrates into pyrethrins; mediates the transfer of a chrysanthemoyl moiety from the coenzyme A (CoA) thio-ester chrysanthemoyl CoA to pyrethrolone, and, to a lower extent, to jasmololone and cinerolone thus producing pyrethrins (e.g. pyrethrin type I) (PubMed:22385412). Can also use pyrethroyl CoA as substrate (PubMed:22385412). Has also esterase activity, being able to cleave the ester bond of pyrethrin I, p-nitrophenyl butanoate and p-nitrophenyl octanoate to produce pyrethrolone and p-nitrophenol, respectively (PubMed:22385412). {ECO:0000269|PubMed:22385412, ECO:0000303|PubMed:30468448}. | Tanacetum cinerariifolium (Dalmatian daisy) (Chrysanthemum cinerariifolium) |
H6WZF2 | TER_NICAL | MNTEPSPNHYSAISSSDQNLTRRSGNYQPTMWDFEYIQSIHNDYAGDKYMKRFNELKEEMKKMIMAEGSQELEKLELIDNLQRLGVSYHFKHEIMQILSSIKQHSTPADSLYATALKFRLLREHGFHISQEIFDGLSETHTKDTKGMLYLYEASFLATEGESELEQAWTEKHLREYLKNKNIDQNVAKLVHRALELPLHWRMLRLEARWFISFYKKRQDMIPLLLELAILDFNIVQAAHIQDLKYVARWWKETGLAENLPFARDRLVENFFWTIGVNFLPQYGYFRRIETKVNALVTTIDDVYDVFGTLDELQCFTDAIQRWNTDELDNLPDNMKMCYFALDDFINEVACDALIVPYLRNAWTDLCKSYLIEAKWYFSKYIPTMEEYMDNAWISISAPVILVHAYFLIANPVNKEALHYLRNYHDIIRWSALILRLANDLGTSSDELKRGDVPKSIQCYMNEKKVSEEEARQHIRLLISETWKKLNEAHNVAAHPFPKMFVKSAMNLARMAQCMYQHGDGHGGQNSETQNRIMALLFESIPPA | 4.2.3.-; 4.2.3.108; 4.2.3.111; 4.2.3.15 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | circadian rhythm [GO:0007623]; diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; limonene biosynthetic process [GO:0046250]; terpenoid biosynthetic process [GO:0016114] | chloroplast [GO:0009507] | 1,8-cineole synthase activity [GO:0102313]; magnesium ion binding [GO:0000287]; myrcene synthase activity [GO:0050551]; sabinene synthase activity [GO:0080015] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsb subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + H2O = (S)-alpha-terpineol + diphosphate; Xref=Rhea:RHEA:32551, ChEBI:CHEBI:128, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.111; Evidence={ECO:0000269|PubMed:21527560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32552; Evidence={ECO:0000269|PubMed:21527560}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + sabinene; Xref=Rhea:RHEA:68636, ChEBI:CHEBI:33019, ChEBI:CHEBI:50027, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:21527560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68637; Evidence={ECO:0000269|PubMed:21527560}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate; Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.15; Evidence={ECO:0000269|PubMed:21527560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966; Evidence={ECO:0000269|PubMed:21527560}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + limonene; Xref=Rhea:RHEA:68640, ChEBI:CHEBI:15384, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:21527560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68641; Evidence={ECO:0000269|PubMed:21527560}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + H2O = 1,8-cineole + diphosphate; Xref=Rhea:RHEA:32543, ChEBI:CHEBI:15377, ChEBI:CHEBI:27961, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.108; Evidence={ECO:0000269|PubMed:21527560}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32544; Evidence={ECO:0000269|PubMed:21527560}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21527560}. | null | null | FUNCTION: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products of the 'cineole cassette', volatile compounds present in floral scent (PubMed:21527560). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into alpha-terpineol and, as minor products, sabinene, beta-myrcene, limonene and 1,8-cineole (PubMed:21527560). {ECO:0000269|PubMed:21527560}. | Nicotiana alata (Winged tobacco) (Persian tobacco) |
H7FWB6 | IBP_FLAFP | MKILKRIPVLAVLLVGLMTNCSNDSDSSSLSVANSTYETTALNSQKSSTDQPNSGSKSGQTLDLVNLGVAANFAILSKTGITDVYKSAITGDVGASPITGAAILLKCDEVTGTIFSVDAAGPACKITDASRLTTAVGDMQIAYDNAAGRLNPDFLNLGAGTIGGKTLTPGLYKWTSTLNIPTDITISGSSTDVWIFQVAGNLNMSSAVRITLAGGAQAKNIFWQTAGAVTLGSTSHFEGNILSQTGINMKTAASINGRMMAQTAVTLQMNTVTIPQ | null | null | null | extracellular region [GO:0005576] | null | PF11999; | null | Ice-binding protein family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27737617}. | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Active at low temperatures, even below 0 degree Celsius. Thermal denaturation midpoint (Tm) is 56.4 degrees Celsius. {ECO:0000269|PubMed:24699650}; | FUNCTION: Has antifreeze activity for survival in a subzero environment. Binds to the surface of ice crystals and inhibits their growth. Has high thermal hysteresis (TH) activity, which is the ability to lower the freezing point of an aqueous solution below its melting point, and thus the freezing of the cell fluid can be prevented protecting the organism from ice damage (PubMed:22750870, PubMed:24699650, PubMed:27737617). The TH activity of this protein is 2.2 degrees Celsius at 5 uM and 2.5 degrees Celsius at 50 uM (PubMed:24699650). {ECO:0000269|PubMed:22750870, ECO:0000269|PubMed:24699650, ECO:0000269|PubMed:27737617}. | Flavobacterium frigoris (strain PS1) |
H8F0D7 | PRPC_MYCTE | MTGPLAAARSVAATKSMTAPTVDERPDIKKGLAGVVVDTTAISKVVPQTNSLTYRGYPVQDLAARCSFEQVAFLLWRGELPTDAELALFSQRERASRRVDRSMLSLLAKLPDNCHPMDVVRTAISYLGAEDPDEDDAAANRAKAMRMMAVLPTIVAIDMRRRRGLPPIAPHSGLGYAQNFLHMCFGEVPETAVVSAFEQSMILYAEHGFNASTFAARVVTSTQSDIYSAVTGAIGALKGRLHGGANEAVMHDMIEIGDPANAREWLRAKLARKEKIMGFGHRVYRHGDSRVPTMKRALERVGTVRDGQRWLDIYQVLAAEMASATGILPNLDFPTGPAYYLMGFDIASFTPIFVMSRITGWTAHIMEQATANALIRPLSAYCGHEQRVLPGTF | 2.3.3.16; 2.3.3.5 | null | carbohydrate metabolic process [GO:0005975]; propionate metabolic process, methylcitrate cycle [GO:0019679]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829] | 2-methylcitrate synthase activity [GO:0050440]; citrate (Si)-synthase activity [GO:0004108]; citrate synthase activity [GO:0036440] | PF00285; | 1.10.580.10;1.10.230.10; | Citrate synthase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + oxaloacetate + propanoyl-CoA = (2S,3S)-2-methylcitrate + CoA + H(+); Xref=Rhea:RHEA:23780, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:58853; EC=2.3.3.5; Evidence={ECO:0000269|PubMed:16689789}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+); Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.16; Evidence={ECO:0000269|PubMed:16689789}; | null | PATHWAY: Organic acid metabolism; propanoate degradation. {ECO:0000305|PubMed:16689789}.; PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2. {ECO:0000305|PubMed:16689789}. | null | null | FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA. {ECO:0000269|PubMed:16689789}. | Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman) |
H8WR05 | BFAT_VARPD | MTHAAIDQALADAYRRFTDANPASQRQFEAQARYMPGANSRSVLFYAPFPLTIARGEGAALWDADGHRYADFIAEYTAGVYGHSAPEIRDAVIEAMQGGINLTGHNLLEGRLARLICERFPQIEQLRFTNSGTEANLMALTAALHFTGRRKIVVFSGGYHGGVLGFGARPSPTTVPFDFLVLPYNDAQTARAQIERHGPEIAVVLVEPMQGASGCIPGQPDFLQALRESATQVGALLVFDEVMTSRLAPHGLANKLGIRSDLTTLGKYIGGGMSFGAFGGRADVMALFDPRTGPLAHSGTFNNNVMTMAAGYAGLTKLFTPEAAGALAERGEALRARLNALCANEGVAMQFTGIGSLMNAHFVQGDVRSSEDLAAVDGRLRQLLFFHLLNEDIYSSPRGFVVLSLPLTDADIDRYVAAIGSFIGGHGALLPRAN | 2.6.1.- | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:23087034}; Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000269|PubMed:23087034}; | null | null | pyridoxal phosphate binding [GO:0030170]; transaminase activity [GO:0008483] | PF00202; | 3.90.1150.10;3.40.640.10; | Class-III pyridoxal-phosphate-dependent aminotransferase family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-3-amino-3-phenylpropanoate + 2-oxoglutarate = 3-oxo-3-phenylpropanoate + L-glutamate; Xref=Rhea:RHEA:47320, ChEBI:CHEBI:16810, ChEBI:CHEBI:22731, ChEBI:CHEBI:29985, ChEBI:CHEBI:68506; Evidence={ECO:0000269|PubMed:23087034}; CATALYTIC ACTIVITY: Reaction=(S)-3-amino-3-phenylpropanoate + pyruvate = 3-oxo-3-phenylpropanoate + L-alanine; Xref=Rhea:RHEA:47324, ChEBI:CHEBI:15361, ChEBI:CHEBI:22731, ChEBI:CHEBI:57972, ChEBI:CHEBI:68506; Evidence={ECO:0000269|PubMed:23087034}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 mM for (S)-beta-phenylalanine; KM=0.3 mM for 2-oxoglutarate; Note=kcat is around 11 sec(-1) with (S)-beta-phenylalanine and 2-oxoglutarate as substrates.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Has high activity over a broad pH range (4 to 11.2).; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. Displays a 2-fold higher activity at 55 degrees Celsius than at 30 degrees Celsius.; | FUNCTION: Aminotransferase that acts exclusively on beta-amino acids and exhibits a broad substrate range in vitro, accepting meta-, para- and, to a lesser extent, ortho-substituted beta-phenylalanine derivatives as amino donors, and 2-oxoglutarate or pyruvate as amino acceptors. Is highly enantioselective toward (S)-beta-phenylalanine (is not active with (R)-beta-phenylalanine) and derivatives with different substituents on the phenyl ring, allowing the kinetic resolution of various racemic beta-amino acids to yield (R)-beta-amino acids with >95% enantiomeric excess (ee). Highly prefers aromatic beta-amino acids over aliphatic beta-amino acids; cannot use beta-alanine or beta-glutamate as substrate. Is likely involved in the beta-phenylalanine degradation pathway that allows V.paradoxus strain CBF3 to use beta-phenylalanine as a sole nitrogen source. {ECO:0000269|PubMed:23087034}. | Variovorax paradoxus |
H8ZM70 | LAS_ABIBA | QSIPHFSTTLNAGSSARKRRSLYLRWGKGSNKIIACVGEGATSVPYQSAEKNDSLYSSTLVKREFPPGFWKDDLIDSLTSSHKVAASDEKRIETLISEIKNMFRCMGYGETNPSAYDTAWVARIPALDGSDNPHFPETVEWILQNQLKDGSWGEGFYFLAYDRILATLACIITLTLWRTGETQVHKGIEFFRTQAGKMEDEADSHRPSGFEIVFPAMLKEAKILGLDLPYDLPFLKQIIEKREAKLKRIPTDVLYALPTTLLYSLEGLQEIVDWQKIMKLQSKDGSFLSSPASTAAVFMRTGNKKCLDFLNFVLKKFGNHVPCHYPLDLFERLWAVDTVERLGIDRHFKEEIKEALDYVYSHWDERGIGWARENPVPDIDDTAMGLRILRLHGYNVSSDVLKTFRDENGEFFCFLGQTQRGVTDMLNVNRCSHVSFPGETIMEEAKLCTERYLRNALENVDAFDKWAFKKNIRGEVEYALKYPWHKSMPRLEARSYIENYGPDDVWLGKTVYMMPYISNEKYLELAKLDFNKVQSIHQTELQDLRRWWKSSGFTDLNFTRERVTEIYFSPASFIFEPEFSKCREVYTKTSNFTVILDDLYDAHGSLDDLKLFTESVKRWDLSLVDQMPQQMKICFVGFYNTFNEIAKEGRESQGRDVLGYIQNVWKVQLEAYTKEAEWSEAKYVPSFNEYIENASVSIALGTVVLISALFTGEVLTDEVLSKIDRGSRFLQLMGLTGRLVNDTKTYQAERGQGEVASAIQCYMKDHPKISEEEALKHVYTVMENSLEELNREFVNNKIPDIYRRLVFETARIMQLFYMQGDGLTLSHDMEIKEHVKNCLFQPVA | 4.2.3.132; 4.2.3.18; 4.2.3.32; 5.5.1.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q40577}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577}; | gibberellin biosynthetic process [GO:0009686] | chloroplast [GO:0009507] | abietadiene synthase activity [GO:0050554]; copalyl diphosphate synthase activity [GO:0050559]; levopimaradiene synthase activity [GO:0052678]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.50.10.160;1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsd subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (+)-copalyl diphosphate; Xref=Rhea:RHEA:24316, ChEBI:CHEBI:58635, ChEBI:CHEBI:58756; EC=5.5.1.12; Evidence={ECO:0000269|PubMed:22337889}; CATALYTIC ACTIVITY: Reaction=(+)-copalyl diphosphate = abieta-7,13-diene + diphosphate; Xref=Rhea:RHEA:13873, ChEBI:CHEBI:30232, ChEBI:CHEBI:33019, ChEBI:CHEBI:58635; EC=4.2.3.18; Evidence={ECO:0000269|PubMed:22337889}; CATALYTIC ACTIVITY: Reaction=(+)-copalyl diphosphate = diphosphate + neoabietadiene; Xref=Rhea:RHEA:33987, ChEBI:CHEBI:29651, ChEBI:CHEBI:33019, ChEBI:CHEBI:58635; EC=4.2.3.132; Evidence={ECO:0000269|PubMed:22337889}; CATALYTIC ACTIVITY: Reaction=(+)-copalyl diphosphate = abieta-8(14),12-diene + diphosphate; Xref=Rhea:RHEA:25548, ChEBI:CHEBI:29616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58635; EC=4.2.3.32; Evidence={ECO:0000269|PubMed:22337889}; | null | PATHWAY: Terpene metabolism; oleoresin biosynthesis. | null | null | FUNCTION: Involved in defensive oleoresin formation in conifers in response to insect attack or other injury. Involved in diterpene (C20) olefins biosynthesis. Bifunctional enzyme that catalyzes two sequential cyclizations of geranylgeranyl diphosphate (GGPP) to abietadiene. The copalyl diphosphate (CPP) intermediate diffuses freely between the 2 active sites in the enzyme. {ECO:0000269|PubMed:22337889}. | Abies balsamea (Balsam fir) (Pinus balsamea) |
H8ZPX1 | PNAO_PSESP | MANDKGDISKDGVSRRKFLGGAVIGAAAAAGVGSQILSLSATAQGADKERVGPLQSNVDYDAVVIGGGFAGVTAARELSRSGLKTLVLEGRSRLGGRTFTSKLDGEKVELGGTWVHWTQPNVWTEVMHYGLEIEETVGLASPETVIWVTDNQVKRAPAAEAFEIFGAACTEYYKEAHNIYPRPFDPFFAKKALQEMDGLSASEYLNKLSLTREQKDMMDSWLSGNGHNYPETIAYSEIMRWFALSNFNMPTMFDSIARYKIKSGTVSLLEAMVAESDMEVQLSTPVLKVKQDSHRVLITTEEGTIAASAVVMAVPLNTMGDVEYSPRLSDAKSEIASQGHAGKGVKGYIRIKQDVGNVMTYAPARNDVTPFTSVFTDHVGENGTLLIAFSADPKLVDINDSKAVEKALHPLLPGVEVTSSYGYDWNLDPFSKGTWCTYRPGQTTRYLTELQKREGRLFFAGSDMANGWRGFIDGAIESGREVGYQVASYLKGKNSNA | 1.4.2.3 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:22267672}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:F8G0P1}; | alkaloid metabolic process [GO:0009820]; nicotine catabolic process [GO:0019608] | periplasmic space [GO:0042597] | FAD binding [GO:0071949]; oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor [GO:0016641] | PF01593; | 3.90.660.10;3.50.50.60;1.10.405.10; | Flavin monoamine oxidase family | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. {ECO:0000255|PROSITE-ProRule:PRU00648}. | SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome c] + H2O + pseudooxynicotine = 4-oxo-4-(pyridin-3-yl)butanal + 2 Fe(II)-[cytochrome c] + 2 H(+) + methylamine; Xref=Rhea:RHEA:75351, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:59338, ChEBI:CHEBI:66878, ChEBI:CHEBI:66879; EC=1.4.2.3; Evidence={ECO:0000305|PubMed:22267672}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75352; Evidence={ECO:0000305|PubMed:22267672}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.247 mM for pseudooxynicotine {ECO:0000269|PubMed:22267672}; Note=kcat is 151 sec(-1) with pseudooxynicotine as substrate. {ECO:0000269|PubMed:22267672}; | PATHWAY: Alkaloid degradation; nicotine degradation. {ECO:0000269|PubMed:22267672}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:22267672}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:22267672}; | FUNCTION: Involved in nicotine degradation (PubMed:22267672). Catalyzes the deamination of pseudooxynicotine to 3-succinoylsemialdehyde-pyridine (PubMed:22267672). {ECO:0000269|PubMed:22267672}. | Pseudomonas sp |
H9A1V3 | AAE1_CANSA | MGKNYKSLDSVVASDFIALGITSEVAETLHGRLAEIVCNYGAATPQTWINIANHILSPDLPFSLHQMLFYGCYKDFGPAPPAWIPDPEKVKSTNLGALLEKRGKEFLGVKYKDPISSFSHFQEFSVRNPEVYWRTVLMDEMKISFSKDPECILRRDDINNPGGSEWLPGGYLNSAKNCLNVNSNKKLNDTMIVWRDEGNDDLPLNKLTLDQLRKRVWLVGYALEEMGLEKGCAIAIDMPMHVDAVVIYLAIVLAGYVVVSIADSFSAPEISTRLRLSKAKAIFTQDHIIRGKKRIPLYSRVVEAKSPMAIVIPCSGSNIGAELRDGDISWDYFLERAKEFKNCEFTAREQPVDAYTNILFSSGTTGEPKAIPWTQATPLKAAADGWSHLDIRKGDVIVWPTNLGWMMGPWLVYASLLNGASIALYNGSPLVSGFAKFVQDAKVTMLGVVPSIVRSWKSTNCVSGYDWSTIRCFSSSGEASNVDEYLWLMGRANYKPVIEMCGGTEIGGAFSAGSFLQAQSLSSFSSQCMGCTLYILDKNGYPMPKNKPGIGELALGPVMFGASKTLLNGNHHDVYFKGMPTLNGEVLRRHGDIFELTSNGYYHAHGRADDTMNIGGIKISSIEIERVCNEVDDRVFETTAIGVPPLGGGPEQLVIFFVLKDSNDTTIDLNQLRLSFNLGLQKKLNPLFKVTRVVPLSSLPRTATNKIMRRVLRQQFSHFE | 6.2.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22353623}; | cannabinoid biosynthetic process [GO:1901696]; fatty acid metabolic process [GO:0006631]; fatty-acyl-CoA biosynthetic process [GO:0046949]; terpenoid biosynthetic process [GO:0016114] | cytosol [GO:0005829]; membrane [GO:0016020] | ATP binding [GO:0005524]; CoA-ligase activity [GO:0016405] | PF00501; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22353623}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA; Xref=Rhea:RHEA:43740, ChEBI:CHEBI:17120, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:22353623}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741; Evidence={ECO:0000269|PubMed:22353623}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.26 uM for CoA {ECO:0000269|PubMed:22353623}; KM=3.7 uM for hexanoate {ECO:0000269|PubMed:22353623}; KM=1.7 uM for decanoate {ECO:0000269|PubMed:22353623}; Vmax=6.8 pmol/sec/g enzyme with hexanoate as substrate {ECO:0000269|PubMed:22353623}; Vmax=1.8 pmol/sec/g enzyme with decanoate as substrate {ECO:0000269|PubMed:22353623}; Note=kcat is 2 sec(-1) with hexanoate as substrate (PubMed:22353623). kcat is 0.5 sec(-1) with decanoate as substrate (PubMed:22353623). {ECO:0000269|PubMed:22353623}; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000303|PubMed:30468448}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9. {ECO:0000269|PubMed:22353623}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:22353623}; | FUNCTION: Involved in the biosynthesis of cannabinoids-related terpenophenolic natural products, which have pharmacological activity (PubMed:22353623). Acyl-activating enzyme that catalyzes the conversion of hexanoic acid to hexanoyl-CoA, precursor of the cannabinoid pathway (PubMed:22353623). Can also activate other fatty acids including heptanoate, octanoate and nonanoate (PubMed:22353623). {ECO:0000269|PubMed:22353623}. | Cannabis sativa (Hemp) (Marijuana) |
H9BZ66 | ABCG1_PETHY | MTNQLPNKVELAEVVPQNGGVFLTWEDLWVTASSVKDGSKAILKGLTGYAMPGELLAIMGPSGSGKSTLLDTIAGRLGSSTRQSGDILINGRRQTLAYGSSAYVTQDDTLLATLTIKEAVYYSAELQLPNSMSKSEKKEIADVTLKGMGLQDAMETRIGGWSGKGISGGQKRRVSICLEILTRPKLLFLDEPTSGLDSAASYYVMKAIASQCQGRTIIASIHQPSVDVFSLFHSLCLLSSGRTVYFGPASAANEFFALSGFPCPTLQNPSDHFLKTINSDFDQDIEEGSTRRKSTEEVIDILIKSYKASDKYNAVQSQVAEICQQEGEMLDKRSHASFITQSLVLTRRSFINMSRDLGYYWLRLAVYVVIAVGLGSLYYDVGFSAASVQARGSMLMFVASFITFMAIGGFPSFVEDMKVFQREKLNGHYGSGSFVIANTLSAMPYLLLVSLIPGAIAYFMTGLQNGFEHFIYFALVLFTCMMIVESLMMIVASMVPNFLMGLIAGAGIQALMLLSGGFFRLPNDLPKPFWKYPLHYVAFHKYAYEGMFKNEFEGLKIHDVNGEDILRNTWQMNMDYSKWIDLVILLGMLVLYRVLFLLVVKAGEIVKPAIRAFMSHSPNQINSAERPLDVFDS | null | null | green leaf volatile biosynthetic process [GO:0010597]; transmembrane transport [GO:0055085] | plasma membrane [GO:0005886] | ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887] | PF01061;PF19055;PF00005; | 3.40.50.300; | ABC transporter superfamily, ABCG family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22345641}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: ABC transporter controlling the release of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) (PubMed:22345641, PubMed:28663500). This scent, mostly produced in the evening and night by the petals, attracts the pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta) (PubMed:22345641). {ECO:0000269|PubMed:22345641, ECO:0000269|PubMed:28663500}. | Petunia hybrida (Petunia) |
H9J9M0 | CDA1_BOMMO | MARYARVATLAACLLFACALADGHRWRRQADETAKKDESLEQELCKDKDAGEWFRLVAGEGDNCRDVIQCTASGIQAIRCPAGLFFDIEKQTCDWKDAVKNCKLKNKERKIKPLLYTEEPLCQDGFLACGDSTCIERGLFCNGEKDCGDGSDENSCDIDNDPNRAPPCDSSQCVLPDCFCSEDGTVIPGDLPARDVPQMITITFDDAINNNNIELYKEIFNGKRKNPNGCDIKATYFVSHKYTNYSAVQETHRKGHEIAVHSITHNDDERFWSNATVDDWGKEMAGMRVIIEKFSNITDNSVVGVRAPYLRVGGNNQFTMMEEQAFLYDSTITAPLSNPRLCPYTMYFRMPHRCHGNLQSCPTRSHAVWEMVMNELDRREDPSNDEYLPGCAMVDSCSNILTGDQFYNFLNHNFDRHYEQNRAPLGLYFHAAWLKNNPEFLEAFLYWIDEILQSHNDVYFVTMTQVIQWVQNPRTVTEAKNFEPWREKCSVEGNPACWVPHSCKLTSKEVPGETINLQTCLRCPVNYPWLNDPTGDGHY | 3.5.1.41 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|PubMed:30755482}; | chitin catabolic process [GO:0006032]; polysaccharide catabolic process [GO:0000272] | extracellular space [GO:0005615] | chitin binding [GO:0008061]; chitin deacetylase activity [GO:0004099]; zinc ion binding [GO:0008270] | PF01607;PF00057;PF01522; | 2.170.140.10;3.20.20.370;4.10.400.10; | Carbohydrate esterase 4 (CE4) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate + chitosan; Xref=Rhea:RHEA:10464, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9597, ChEBI:CHEBI:15377, ChEBI:CHEBI:17029, ChEBI:CHEBI:30089, ChEBI:CHEBI:57704; EC=3.5.1.41; Evidence={ECO:0000269|PubMed:30755482}; | null | null | null | null | FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin. {ECO:0000269|PubMed:30755482}. | Bombyx mori (Silk moth) |
H9JW43 | CDA8_BOMMO | MKRLSVLCSLLLVAAALGTELPLATPCDEEACKLPDCRCSSTNIPGGLRARDTPQFVTVTFDDGINVINIETYREVLYGRSNSNRCPAGATFYVSHEYTNYQLVNELYNRGFEIALHSISHRTPQAFWADATYQNLVQEIGDQKRQMAHFASIPASAIKGVRIPFLQMSGNTSFQVMADFDLLYDCTWPTTALTNPGLWPYTLHHESIQDCIIPPCPTASIPGPWVLPMISWRDLNNFPCSMVDGCFFTPDRTDEEGWFKFILTNFERHYLGNRAPFGFFVHEWFISSNPAIKRAFVRFMDIINNLNDVFMVNSAEVIDWVKNPVPIDRYRQQQCKFTMPSICRPSFCGPLTGTHNQLSYYMTICNTCPRNYPWVGNPLGQ | 3.5.1.41 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|PubMed:30755482}; | chitin catabolic process [GO:0006032]; polysaccharide catabolic process [GO:0000272] | extracellular space [GO:0005615] | chitin deacetylase activity [GO:0004099]; zinc ion binding [GO:0008270] | PF01522; | 3.20.20.370; | Carbohydrate esterase 4 (CE4) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate + chitosan; Xref=Rhea:RHEA:10464, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9597, ChEBI:CHEBI:15377, ChEBI:CHEBI:17029, ChEBI:CHEBI:30089, ChEBI:CHEBI:57704; EC=3.5.1.41; Evidence={ECO:0000269|PubMed:30755482}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=76.7 mM for GlcNAc(3) {ECO:0000269|PubMed:30755482}; KM=12.3 mM for GlcNAc(4) {ECO:0000269|PubMed:30755482}; KM=15.7 mM for GlcNAc(5) {ECO:0000269|PubMed:30755482}; KM=9.2 mM for GlcNAc(6) {ECO:0000269|PubMed:30755482}; KM=1.926 mg/ml for ethylene glycol chitin {ECO:0000269|PubMed:30755482}; KM=1.599 mg/ml for colloidal chitin {ECO:0000269|PubMed:30755482}; Note=kcat is 7.62 min(-1) for GlcNAc(3) (PubMed:30755482). kcat is 5.59 min(-1) for GlcNAc(4) (PubMed:30755482). kcat is 7.52 min(-1) for GlcNAc(5) (PubMed:30755482). kcat is 9.07 min(-1) for GlcNAc(6) (PubMed:30755482). kcat is 0.097 min(-1) for ethylene glycol chitin (PubMed:30755482). kcat is 0.012 min(-1) for colloidal chitin (PubMed:30755482). {ECO:0000269|PubMed:30755482}; | null | null | null | FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine (GlcNAc) residues in chitin. Shows activity towards the chitinous oligomers GlcNAc(3), GlcNAc(4), GlcNAc(5) and GlcNAc(6), but not GlcNAc or GlcNAc(2). Requires the substrate to occupy subsites 0, +1, and +2 for optimum catalysis. {ECO:0000269|PubMed:30755482}. | Bombyx mori (Silk moth) |
H9L427 | BIPA_SALTY | MIENLRNIAIIAHVDHGKTTLVDKLLQQSGTFDARAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIIYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPLQMQISQLDYNNYVGVIGIGRIKRGKVKPNQQVTIIDSEGKTRNAKVGKVLTHLGLERIDSNIAEAGDIIAITGLGELNISDTICDPQNVEALPALSVDEPTVSMFFCVNTSPFCGKEGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFREIDGRKQEPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDIRPGEVGQRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVILVPPIKMSLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRRANRGQKEE | 3.6.5.- | null | ribosome biogenesis [GO:0042254] | cytosol [GO:0005829]; ribonucleoprotein complex [GO:1990904] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; guanosine tetraphosphate binding [GO:0097216]; ribosome binding [GO:0043022]; rRNA binding [GO:0019843]; tRNA binding [GO:0000049] | PF21018;PF00679;PF00009;PF03144; | 3.30.70.240;2.40.50.250;3.30.70.870;3.40.50.300;2.40.30.10; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, BipA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00849, ECO:0000305|PubMed:18621905}. Note=During exponential growth the GTP-bound state associates 1:1 with 70S ribosomes. Under stress conditions (induction of the stringent response, growth at 42 or 16 degrees Celsius) associates with 30S ribosomal subunits only. {ECO:0000269|PubMed:18621905}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000255|HAMAP-Rule:MF_00849, ECO:0000269|PubMed:18621905, ECO:0000269|PubMed:19803466}; | null | null | null | null | FUNCTION: A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA (By similarity). A ribosome-stimulated GTPase, GTPase activity increases 4 fold in the presence of 70S ribosomes. Binds 70S ribosomes in the presence of GTP or its non-hydrolyzable analog GMPPNP; in the presence of ppGpp or under stress conditions it binds to 30S ribosomal subunits (PubMed:18621905, PubMed:19803466). {ECO:0000255|HAMAP-Rule:MF_00849, ECO:0000269|PubMed:18621905, ECO:0000269|PubMed:19803466}. | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
H9L478 | PDUJ_SALTY | MNNALGLVETKGLVGAIEAADAMVKSANVQLVGYEKIGSGLVTVMVRGDVGAVKAAVDAGSAAASVVGEVKSCHVIPRPHSDVEAILPKSA | null | null | propanediol catabolic process [GO:0051144] | propanediol degradation polyhedral organelle [GO:0031472] | null | PF00936; | 3.30.70.1710; | Bacterial microcompartments protein family | null | SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000269|PubMed:12923081, ECO:0000269|PubMed:24747050}. | null | null | PATHWAY: Polyol metabolism; 1,2-propanediol degradation. {ECO:0000305|PubMed:10498708}. | null | null | FUNCTION: One of the major shell proteins of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. The isolated BMC shell component protein ratio for J:A:B':B:K:T:U is approximately 15:10:7:6:1:1:2 (PubMed:12923081). At least one of PduA or PduJ is required for BMC assembly; it must be encoded as the first gene in the pdu operon (PubMed:27561553, PubMed:33227310). Required for structural integrity of BMCs and to mitigate propionaldehyde toxicity, probably joins facets responsible for BMC closure (PubMed:21239588). Edge residues (particularly Lys-25) are important for function and assembly of the BMC (PubMed:24747050). 80% identical to PduA; although their pore regions appear structurally identical, unlike PduA plays no role in 1,2-PD diffusion into or out of the BMC shell. If pduJ is cloned in the chromosomal position of pduA it is able to complement a pduA deletion; it then has a functional pore as it assumes the transport functions of PduA (PubMed:27561553). Overexpression of this protein leads to aberrant filaments that extend the length of the cell, cross the cleavage furrow and impair division. The filaments form nanotubes with a hollow center (PubMed:33227310). Modeling suggests PduJ is probably the hub for binding multiple enzymes to the interior of the BMC; modeling suggests PduC, PduD, PduG and PduM are targeted to PduJ (Probable). {ECO:0000269|PubMed:12923081, ECO:0000269|PubMed:21239588, ECO:0000269|PubMed:24747050, ECO:0000269|PubMed:27561553, ECO:0000269|PubMed:33227310, ECO:0000305|PubMed:25646976}.; FUNCTION: The 1,2-propanediol (1,2-PD) degradation bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low. {ECO:0000269|PubMed:18296526, ECO:0000305|PubMed:28475631}. | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
H9N289 | NDMA_PSEPU | MEQAIINDEREYLRHFWHPVCTVTELEKAHPSSLGPLAVKLLNEQLVVAKLGDEYVAMRDRCAHRSAKLSLGTVSGNRLQCPYHGWQYDTHGACQLVPACPNSPIPNKAKVDRFDCEERYGLIWIRLDSSFDCTEIPYFSAANDPRLRIVIQEPYWWDATAERRWENFTDFSHFAFIHPGTLFDPNNAEPPIVPMDRFNGQFRFVYDTPEDMAVPNQAPIGSFSYTCSMPFAINLEVSKYSSSSLHVLFNVSCPVDSHTTKNFLIFAREQSDDSDYLHIAFNDLVFAEDKPVIESQWPKDAPADEVSVVADKVSIQYRKWLRELKEAHKEGSQAFRSALLDPVIESDRSYI | 1.14.13.178 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:20966097, ECO:0000269|PubMed:22328667}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:20966097, ECO:0000269|PubMed:22328667}; | alkaloid catabolic process [GO:0009822]; chlorophyll biosynthetic process [GO:0015995] | null | 2 iron, 2 sulfur cluster binding [GO:0051537]; chlorophyllide a oxygenase [overall] activity [GO:0010277]; demethylase activity [GO:0032451]; metal ion binding [GO:0046872] | PF00355;PF19112; | 2.102.10.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=caffeine + H(+) + NADH + O2 = formaldehyde + H2O + NAD(+) + theobromine; Xref=Rhea:RHEA:36267, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16842, ChEBI:CHEBI:27732, ChEBI:CHEBI:28946, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.178; Evidence={ECO:0000269|PubMed:22328667}; CATALYTIC ACTIVITY: Reaction=caffeine + H(+) + NADPH + O2 = formaldehyde + H2O + NADP(+) + theobromine; Xref=Rhea:RHEA:36271, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16842, ChEBI:CHEBI:27732, ChEBI:CHEBI:28946, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.178; Evidence={ECO:0000269|PubMed:22328667}; CATALYTIC ACTIVITY: Reaction=H(+) + NADH + O2 + theophylline = 3-methylxanthine + formaldehyde + H2O + NAD(+); Xref=Rhea:RHEA:36279, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16842, ChEBI:CHEBI:28177, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62208; EC=1.14.13.178; Evidence={ECO:0000269|PubMed:22328667}; CATALYTIC ACTIVITY: Reaction=H(+) + NADPH + O2 + theophylline = 3-methylxanthine + formaldehyde + H2O + NADP(+); Xref=Rhea:RHEA:36275, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16842, ChEBI:CHEBI:28177, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62208; EC=1.14.13.178; Evidence={ECO:0000269|PubMed:22328667}; CATALYTIC ACTIVITY: Reaction=1,7-dimethylxanthine + H(+) + NADH + O2 = 7-methylxanthine + formaldehyde + H2O + NAD(+); Xref=Rhea:RHEA:30315, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16842, ChEBI:CHEBI:25858, ChEBI:CHEBI:48991, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.178; Evidence={ECO:0000269|PubMed:22328667}; CATALYTIC ACTIVITY: Reaction=1,7-dimethylxanthine + H(+) + NADPH + O2 = 7-methylxanthine + formaldehyde + H2O + NADP(+); Xref=Rhea:RHEA:36283, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16842, ChEBI:CHEBI:25858, ChEBI:CHEBI:48991, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.178; Evidence={ECO:0000269|PubMed:22328667}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.1 uM for theophylline (at pH 7.5 and 30 degrees Celsius) {ECO:0000269|PubMed:20966097, ECO:0000269|PubMed:22328667}; KM=37 uM for caffeine (at pH 7.5 and 30 degrees Celsius) {ECO:0000269|PubMed:20966097, ECO:0000269|PubMed:22328667}; KM=53 uM for paraxanthine (at pH 7.5 and 30 degrees Celsius) {ECO:0000269|PubMed:20966097, ECO:0000269|PubMed:22328667}; KM=270 uM for 1-methylxanthine (at pH 7.5 and 30 degrees Celsius) {ECO:0000269|PubMed:20966097, ECO:0000269|PubMed:22328667}; Note=kcat is 190 min(-1) for caffeine (at pH 7.5 and 30 degrees Celsius).; | PATHWAY: Alkaloid degradation. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:20966097, ECO:0000269|PubMed:22328667}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:20966097, ECO:0000269|PubMed:22328667}; | FUNCTION: Involved in the caffeine degradation, which is the essential first step for assimilating the carbon and nitrogen in caffeine. Catalyzes the N1-demethylation of caffeine to produce theobromine and formaldehyde. Also catalyzes the N1-demethylation of theophylline, paraxanthine, and 1-methylxanthine to 3-methylxanthine, 7-methylxanthine, and xanthine, respectively. NADH is the preferred substrate. {ECO:0000269|PubMed:20966097, ECO:0000269|PubMed:22328667}. | Pseudomonas putida (Arthrobacter siderocapsulatus) |
H9T8G6 | CDIA9_BURPE | SLDTTGNVDLTSANVKAGSLDLNAGNKLILDTATQTTHQVSRDGATSDKTTLGPAANLNVAGDASIKTGGDFQQNAGNLNVGGNLNANIGGNWNLGVQQTGEHKVVQRANGVSDTDLNSATGSTVNVGGKSAIGVGGDLTAQGARLDFGQGGTVAAKGNVTFGAASTTSTINANSSGDQGNRSYAETRHGADQALTGTTVKGGDTLNVVSGKDINVIGSTIDLKKGDANLLAAGDVNVGAATETHVYNSRETHSRSGVVSGTKIASSQDATSTVANGSLISADGVSIGSGKDINVQGSTVVGTHDVALNAAHDVNITTSQDTSQSSTTYQEQHSGLMSGGGLSFSVGNSKLAQQNQSSSVTNNASTVGSVDGNLTVNAGNTLHVKGSDLVAGKDVTGTAANIVVDSATDTTHQAQQQQTSKSGLTVGLSGSVGDAINNAISETQAARESAKDSNGRASALHSIAAAGDVAFGGLGAKALLDGAKGPQAPSIGVQVSVGSSHSSMQSSEDQTIQRGSSINAGGNAKLIATGNGTPKDGNITIAGSNVNAANVALVANNQVNLVNTTDTDKTQSSNSSSGSSVGVSIGTNGIGVSASMQRAHGDGNSDAAIQNNTHINASQTATIVSGGDTNVIGANVNANKVVADVGGNLNVASVQDTTVSAAHQSSAGGGFTISQTGGGASFSAQNGHADGNYAGVKEQAGIQAGSGGFDVTVKGNTDLKGAYIGSTADASKNSLTTGTLTTSDIENHSHYSANSAGFSAGASVGVSTKAVGPSSVSGSGGVTPMVFQNDSGDQSATTKSAVSVGAINITKPGEQTQDVANLNRDATNLNGTVSKTPDVQKMLSQQADTMNAAQAAGQTVSQGIGLYADGKRKDAIDAAKAAYERGDLVAMQSYIDQAKSWDEGGASRAGLQATGGALIGGLGGGSVLTAIGGAAGAGTSSLLAGQAEKISKSVGDMTGSSLVGNIAANVAATVGGALVGGSAGAAMASNVELYNAGNDPQKTDDRATIAGLQGLLSRTAAMASDAKAGVWNGMVNVAGVIVNIPNGGPFASPGDPGYVSLDGLKKPYKSGTSIGPDTEFLTPILATLGLGGKAAVGTDAGITSADVATVGNGALKNASGDLSAAANSARNQPYGQGASASQSPGTQGASSGSNISASNGSSSPTTIVASNPVDLNAFDRLNVVDPAVGKFRPGEAGAAAELENYLGGTLQRAPQGSSVDFVFSSGPNNGKTVDFMLTPDTVAQAAKINQFFDKNLNNFMNTLSDHAAAADFVPLDSRFLSEANKTLLVKAIGNLPQKLQAKIILIK | 3.1.-.- | null | null | null | endonuclease activity [GO:0004519]; toxin activity [GO:0090729]; tRNA binding [GO:0000049] | PF18664;PF13332; | null | CdiA toxin family | null | SUBCELLULAR LOCATION: Target cell, target cell cytoplasm {ECO:0000250|UniProtKB:I1WVY3}. Note=Secreted to the cell surface by CdiB, its two partner secretion pathway (TPS) partner. {ECO:0000250|UniProtKB:I1WVY3}. | null | null | null | null | null | FUNCTION: Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion. The C-terminal 160 residues (CT domain) acts as a general tRNA nuclease, and inhibits growth in E.coli upon overexpression. Cleaves specifically within the T-loop of E.coli tRNA2(Arg) (between the post-transcriptionally modified thymidine-T55 and pseudouridine-Y56); also degrades most other tRNAs (PubMed:22435733). Cleaves unmodified tRNA(Gln) and tRNA(Asp), showing the universal post-translational tRNA modifications present in the T-loop are not required for CT activity (PubMed:27445337). Inactive CT domain binds tRNA, probably in a complex with 4 CT domains and 4 tRNAs (PubMed:27445337). Toxic activity is neutralized by coexpression of the cognate immunity protein CdiI in E.coli, but not by non-cognate immunity proteins from other strains of B.pseudomallei (PubMed:22435733, PubMed:27445337). {ECO:0000269|PubMed:22435733, ECO:0000269|PubMed:27445337}.; FUNCTION: The CdiA protein is thought to be exported from the cell through the central lumen of CdiB, the other half of its two-partner system (TPS). The TPS domain probably remains associated with CdiB while the FHA-1 domain forms an extended filament with the receptor-binding domain (RBD) at its extremity; in the secretion arrested state the C-terminus of the RBD domain form a hairpin-like structure as the FHA-2, PT and CT domains are periplasmic. Upon binding to a target cell outer membrane receptor a signal is transmitted to activate secretion. The filament elongates slightly, the rest of CdiA is secreted and the FHA-2 domain becomes stably associated with the target cell's outer membrane where it facilitates entry of the toxic CT domain into the target cell periplasm. From there the toxic CT domain is cleaved and gains access to the target cell cytoplasm via an inner membrane protein. {ECO:0000250|UniProtKB:A0A1S4NYE3, ECO:0000250|UniProtKB:I1WVY3}. | Burkholderia pseudomallei (Pseudomonas pseudomallei) |
H9TB17 | AOXA_CAVPO | MEPSTLYFYVNGRRVTEKNVDPETMLLPYLGRNLRLTGTKYGCGGGGCGACTVMVSRYDRGTGQIRHYPACACLTPLCSLHGAAVTTVEGVGSTRTRLHPVQERIAKSHGTQCGFCTPGMVMSLYALLRSHPQPSEEQLLEALAGNLCRCTGYRPILDAGKTFCKTSGCCQSKENGVCCLDQGVNGVQEAEGEQTSQELCSEEEFVPLDPTQELIFPPELMILAQKQPQKSRVFTGDRVTWISPVTLKDLLEAKAKNPRAPVVMGNTSVGPEMKFKGVFHPVIISPDGIEELSVIKQGNEGLTLGAGLSLAQVQDVLADVVQQLPEEKTQTLCALLKQLRTLAGSQIRNMASLGGHIMSRHLDSDLNPVLAAASCTLHVPSQEGDRQIPLDEHFLSRSPSADLRPQEVLLSVTIPYSRKWEFVSAFRQAQRKRSARAIVNVGMRVFFGAGDGVISELCILYGGVGPAIVCATDACRKLVGRHWTEEMLDEACRLVLGEVAIPGAAPGGRVEFRRTLLVSFLFRFYLQVSQSLSRMDPGRYPSLVGKYESALEDLCLGHHQRTFELQSADAKQLPQDPIGRPIMHLSGIKHTTGEAIYCDDMPLVDRELSLAFVTSSRAHAAILSMDLSEALSLPGVVDIVTAEHLGDANSFAKETLLATDKVLCVGHLVCAVIADSEVQAKRAAEKVKIVYQDLEPLILTIEEAIQHDSFFETERKLESGDVAEAFRTAEQVLEGSIHMGGQEHFYMETQSMLAVPKGEDQEIDLYVSTQFPTYIQEIVASTLKLPVNKVMCHVRRVGGAFGGKVGKTAILAAITAFAALKHCRAVRCILERGEDMLITGGRHPYLGKYKVGFRNNGQVVALDMEHYSNAGSTLDESLMVVEMGLLKMENAYKFPNLRCRGHACKTNLPSNTALRGFGFPQSGLITEACIVEVAARCGLSPEEVREVNMYRGTEQTHYGQEIHTQRLAQCWSECKAKATFSLRRAAVDRFNAGSPWKKRGLAMVPLKFPVGLGSVAMGQAAALVHVYLDGSVLLTHGGIEMGQGVHTKMIQVVSRELKMPMANVHLRGTSTETVPNANVSGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKEWAQAAFDQSISLSAIGYFRGYDADMDWEKGKGHPFEYFVYGAACSEVEIDCLTGNHKNIRTDIVMDVGRSINPALDLGQVEGAFIQGMGLYTSEELKYGPQGALYTRGPDQYKIPAVCDVPAELHVFFLPPSKNSNTLYSSKGLGESGVFLGCSVLFAIWDAVSAARRERGLPGTLALSCPLTPEKIRMACEDRFTKMIPRDTPGSYVPWDVVV | 1.17.3.-; 1.2.3.1 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250|UniProtKB:O54754}; Note=Binds 2 [2Fe-2S] clusters per subunit. {ECO:0000250|UniProtKB:O54754}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:O54754}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O54754}; COFACTOR: Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250|UniProtKB:O54754}; Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. {ECO:0000250|UniProtKB:O54754}; | lipid metabolic process [GO:0006629]; xenobiotic metabolic process [GO:0006805] | cytosol [GO:0005829] | 2 iron, 2 sulfur cluster binding [GO:0051537]; aldehyde oxidase activity [GO:0004031]; FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; iron ion binding [GO:0005506]; molybdopterin cofactor binding [GO:0043546]; NAD binding [GO:0051287]; protein homodimerization activity [GO:0042803] | PF01315;PF03450;PF00941;PF00111;PF01799;PF02738;PF20256; | 3.10.20.30;3.30.465.10;1.10.150.120;3.90.1170.50;3.30.365.10;3.30.390.50;3.30.43.10; | Xanthine dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9224775}. | CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2; Xref=Rhea:RHEA:16829, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067; EC=1.2.3.1; Evidence={ECO:0000250|UniProtKB:O54754}; CATALYTIC ACTIVITY: Reaction=H2O + O2 + retinal = H(+) + H2O2 + retinoate; Xref=Rhea:RHEA:56736, ChEBI:CHEBI:15035, ChEBI:CHEBI:15036, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; Evidence={ECO:0000250|UniProtKB:O54754}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.41 mM for 6-deoxypenciclovir (at 37 degrees Celsius and pH 7) {ECO:0000269|PubMed:9224775}; KM=0.17 mM for famciclovir (at 37 degrees Celsius and pH 7) {ECO:0000269|PubMed:9224775}; Vmax=209 nmol/min/mg enzyme with 6-deoxypenciclovir as substrate {ECO:0000269|PubMed:9224775}; Vmax=439 nmol/min/mg enzyme with famciclovir as substrate {ECO:0000269|PubMed:9224775}; | null | null | null | FUNCTION: Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. May also catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis. {ECO:0000269|PubMed:7786031, ECO:0000269|PubMed:9224775}. | Cavia porcellus (Guinea pig) |
H9XP47 | MBDH_SERMA | MRFDNKVVVITGAGNGMGEAAARRFSAEGAIVVLADWAKEAVDKVAASLPKGRAMAVHIDVSDHVAVEKMMNEVAEKLGRIDVLLNNAGVHVAGSVLETSIDDWRRIAGVDIDGVVFCSKFALPHLLKTKGCIVNTASVSGLGGDWGAAYYCAAKGAVVNLTRAMALDHGGDGVRINSVCPSLVKTNMTNGWPQEIRDKFNERIALGRAAEPEEVAAVMAFLASDDASFINGANIPVDGGATASDGQPKIV | 1.1.1.- | null | null | null | oxidoreductase activity [GO:0016491] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=(R,S)-butane-2,3-diol + NAD(+) = (R)-acetoin + H(+) + NADH; Xref=Rhea:RHEA:75423, ChEBI:CHEBI:15378, ChEBI:CHEBI:15686, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:75460; Evidence={ECO:0000269|PubMed:23666479}; CATALYTIC ACTIVITY: Reaction=(S,S)-butane-2,3-diol + NAD(+) = (S)-acetoin + H(+) + NADH; Xref=Rhea:RHEA:12184, ChEBI:CHEBI:15378, ChEBI:CHEBI:15687, ChEBI:CHEBI:16812, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:23666479}; CATALYTIC ACTIVITY: Reaction=(S)-acetoin + NAD(+) = diacetyl + H(+) + NADH; Xref=Rhea:RHEA:27286, ChEBI:CHEBI:15378, ChEBI:CHEBI:15687, ChEBI:CHEBI:16583, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:23666479}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.1 mM for meso-2,3-butanediol {ECO:0000269|PubMed:23666479}; KM=31.2 mM for (2S,3S)-2,3-butanediol {ECO:0000269|PubMed:23666479}; KM=0.97 mM for (3S/3R)-acetoin {ECO:0000269|PubMed:23666479}; KM=3.3 mM for diacetyl {ECO:0000269|PubMed:23666479}; Note=kcat is 6.2 sec(-1) with meso-2,3-butanediol as substrate. kcat is 1.02 sec(-1) with (2S,3S)-2,3-butanediol as substrate. kcat is 19.7 sec(-1) with (3S/3R)-acetoin as substrate. kcat is 11.5 sec(-1) with diacetyl as substrate. {ECO:0000269|PubMed:23666479}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 for meso-2,3-butanediol oxidation (PubMed:23666479). Optimum pH is 5.0 for (3S/3R)-acetoin reduction and 8.0 for diacetyl reduction (PubMed:23666479). {ECO:0000269|PubMed:23666479}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius for oxidation and reduction reactions. {ECO:0000269|PubMed:23666479}; | FUNCTION: Catalyzes the NAD-dependent oxidation of meso-2,3-butanediol to (3R)-acetoin, and of (2S,3S)-2,3-butanediol to (3S)-acetoin, with much lower efficiency (PubMed:23666479). Can also oxidize several primary alcohols such as glycerol, 1-2-pentanediol and 1,2-propanediol, with lower activity (PubMed:23666479). Cannot use (2R,3R)-2,3-butanediol (PubMed:23666479). In the presence of NADH, catalyzes the reduction of (3R)-acetoin to meso-2,3-butanediol, of (3S)-acetoin to (2S,3S)-2,3-butanediol and of diacetyl to (3S)-acetoin (PubMed:23666479). No activity is detected with NADPH/NADP(+) (PubMed:23666479). {ECO:0000269|PubMed:23666479}. | Serratia marcescens |
I0CME7 | HYAL_CONCN | MRAVVVVTGLVVVVVATALSLPNHDVKSATSSRSSSDYQGSSGDDCDEGLPPPDQPFRVVWNHPDNCERIKLHLPLDDYGIIFNKLRVFLGEEIQTLYDTGPWPYISETGKFINGGLPQSFNHPDNDGETQRILKKHRPENFTGLGVLDFETWRAIYSTNFGPMTIYQNESVKLVKEQHPDYDQKKLTKVAEKEWQQAAKDIMSNKLKIAQEVMPRGHWGYYLYPRTWDNKRDTKFRNDKINWLWRQSTGLYPSIYIYDFSKTESAITKFVSDTVGEAVRVQKEFSPPNTPIYPYVMFQTMDNIFHYEDHLKISLGLSAKMGAAGVVLWGTSKHYKESTRQWQCQQLQEHIRTVLGPLVKNVTQMMTDCSRAICEGHGRCVHNSHDVILGETESQRLSDLCSTRQSRFRDYHCRCYSAWEGACCQTLRPSRCQKREQRNVHGGGDLID | 3.2.1.35 | null | carbohydrate metabolic process [GO:0005975]; hyaluronan catabolic process [GO:0030214] | cytoplasmic vesicle [GO:0031410]; extracellular region [GO:0005576] | hyalurononglucosaminidase activity [GO:0004415] | PF01630; | 3.20.20.70; | Glycosyl hydrolase 56 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35; Evidence={ECO:0000269|PubMed:22412800}; | null | null | null | null | FUNCTION: Hyaluronidase catalyzes the hydrolysis of hyaluronic acid (HA), an anionic, nonsulfated glycosaminoglycan distributed widely throughout connective, epithelial, and neural tissues. In venom, they are known to enhance diffusion of the venom by degrading the extracellular matrix. | Conus consors (Singed cone) |
I0DEB3 | NDB4D_VAEMS | MKTQFVILIVAVVLLQLISHSEAFLGALWNVAKSVFGKRGLRNFDDLDDTFEPEMSEADLKYLQDLLR | null | null | defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | null | null | null | Non-disulfide-bridged peptide (NDBP) superfamily, Short antimicrobial peptide (group 4) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Target cell membrane {ECO:0000250}. Note=Forms a helical membrane channel in the prey. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Cationic amphipathic peptide with antibacterial activities against both Gram-positive and Gram-negative bacteria (PubMed:22342498, PubMed:27912176, PubMed:31212183). Also shows antifungal activities (PubMed:27912176). Is mildly hemolytic against human erythrocytes (PubMed:22342498, PubMed:27912176, PubMed:31212183). In addition, when tested in vitro on the parasite Trypanosoma cruzi (responsible of the Chagas disease), is able to reduce the number of the three forms (epimastigote, trypomastigote and amastigote) (PubMed:33004083). Also shows antiplasmodial and cytotoxic activity (tested on Plasmodium gallinaceum, and MCF-7 breast cancer cell line) (PubMed:33442881). {ECO:0000269|PubMed:22342498, ECO:0000269|PubMed:27912176, ECO:0000269|PubMed:31212183, ECO:0000269|PubMed:33004083, ECO:0000269|PubMed:33442881}. | Vaejovis mexicanus smithi (Mexican scorpion) (Vaejovis smithi) |
I0DF35 | L_SFTS | MNLEVLCGRINVENGLSLGEPGLYDQIYDRPGLPDLDVTVDATGVTVDIGAVPDSASQLGSSINAGLITIQLSEAYKINHDFTFSGLSKTTDRRLSEVFPITHDGSDGMTPDVIHTRLDGTIVVVEFTTTRSHNIGGLEAAYRTKIEKYRDPISRRVDIMENPRVFFGVIVVSSGGVLSNMPLTQDEAEELMYRFCIANEIYTKARSMDADIELQKSEEELEAISRALSFFSLFEPNIERVEGTFPNSEIEMLEQFLSTPADVDFITKTLKAKEVEAYADLCDSHYLKPEKTIQERLEINRCEAIDKTQDLLAGLHARSNKQTSLNRGTVKLPPWLPKPSSESIDIKTDSGFGSLMDHGAYGELWAKCLLDVSLGNVEGVVSDPAKELDIAISDDPEKDTPKEAKITYRRFKPALSSSARQEFSLQGVEGKKWKRMAANQKKEKESHDALSPFLDVEDIGDFLTFNNLLADSRYGDESVQRAVSILLEKASAMQDTELTHALNDSFKRNLSSNVVQWSLWVSCLAQELASALKQHCRAGEFIIKKLKFWPIYVIIKPTKSSSHIFYSLGIRKADVTRRLTGRVFSETIDAGEWELTEFKSLKTCKLTNLVNLPCTMLNSIAFWREKLGVAPWLVRKPCSELREQVGLTFLISLEDKSKTEEIITLTRYTQMEGFVSPPMLPKPQKMLGKLDGPLRTKLQVYLLRKHLDCMVRIASQPFSLIPREGRVEWGGTFHAISGRSTNLENMVNSWYIGYYKNKEESTELNALGEMYKKIVEMEEDKPSSPEFLGWGDTDSPKKHEFSRSFLRAACSSLEREIAQRHGRQWKQNLEERVLREIGTKNILDLASMKATSNFSKDWELYSEVQTKEYHRSKLLEKMATLIEKGVMWYIDAVGQAWKAVLDDGCMRICLFKKNQHGGLREIYVMDANARLVQFGVETMARCVCELSPHETVANPRLKNSIIENHGLKSARSLGPGSININSSNDAKKWNQGHYTTKLALVLCWFMPAKFHRFIWAAISMFRRKKMMVDLRFLAHLSSKSESRSSDPFREAMTDAFHGNREVSWMDKGRTYIKTETGMMQGILHFTSSLLHSCVQSFYKSYFVSKLKEGYMGESISGVVDVIEGSDDSAIMISIRPKSDMDEVRSRFFVANLLHSVKFLNPLFGIYSSEKSTVNTVYCVEYNSEFHFHRHLVRPTLRWIAASHQISETEALASRQEDYSNLLTQCLEGGASFSLTYLIQCAQLLHHYMLLGLCLHPLFGTFMGMLISDPDPALGFFLMDNPAFAGGAGFRFNLWRACKTTDLGRKYAYYFNEIQGKTKGDEDYRALDATSGGTLSHSVMVYWGDRKKYQALLNRMGLPEDWVEQIDENPGVLYRRAANKKELLLKLAEKVHSPGVTSSLSKGHVVPRVVAAGVYLLSRHCFRFSSSIHGRGSTQKASLIKLLMMSSISAMKHGGSLNPNQERMLFPQAQEYDRVCTLLEEVEHLTGKFVVRERNIVRSRIDLFQEPVDLRCKAEDLVSEVWFGLKRTKLGPRLLKEEWDKLRASFAWLSTDPSETLRDGPFLSHVQFRNFIAHVDAKSRSVRLLGAPVKKSGGVTTISQVVRMNFFPGFSLEAEKSLDNQERLESISILKHVLFMVLNGPYTEEYKLEMIIEAFSTLVIPQPSEVIRKSRTMTLCLLSNYLSSRGGSILDQIERAQSGTLGGFSKPQKTFIRPGGGVGYKGKGVWTGVMEDTHVQILIDGDGTSNWLEEIRLSSDARLYDVIESIRRLCDDLGINNRVASAYRGHCMVRLSGFKIKPASRTDGCPVRIMERGFRIRELQNPDEVKMRVRGDILNLSVTIQEGRVMNILSYRPRDTDISESAAAYLWSNRDLFSFGKKEPSCSWICLKTLDNWAWSHASVLLANDRKTQGIDNRAMGNIFRDCLEGSLRKQGLMRSKLTEMVEKNVVPLTTQELVDILEEDIDFSDVIAVELSEGSLDIESIFDGAPILWSAEVEEFGEGVVAVSYSSKYYHLTLMDQAAITMCAIMGKEGCRGLLTEKRCMAAIREQVRPFLIFLQIPEDSISWVSDQFCDSRGLDEESTIMWG | 2.7.7.48; 3.1.-.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=For endonuclease activity. Binds 2 Mn(2+) ions in the active site (PubMed:31914382). The divalent metal ions are crucial for catalytic activity (PubMed:31948728). {ECO:0000269|PubMed:31914382, ECO:0000269|PubMed:31948728}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P27316}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P27316}; Note=For polymerase activity. Initiation activity is stronger in the presence of Mn(2+) than in the presence of Mg(2+). {ECO:0000250|UniProtKB:P27316}; | DNA-templated transcription [GO:0006351]; viral RNA genome replication [GO:0039694] | host cell endoplasmic reticulum [GO:0044165]; host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell Golgi apparatus [GO:0044177]; virion component [GO:0044423] | hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; RNA-dependent RNA polymerase activity [GO:0003968] | PF04196;PF12603;PF15518; | null | Bunyavirales RNA polymerase family | null | SUBCELLULAR LOCATION: Host Golgi apparatus {ECO:0000269|PubMed:29467349}. Host endoplasmic reticulum {ECO:0000269|PubMed:29467349}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:29467349}. Virion {ECO:0000250|UniProtKB:P20470}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539, ECO:0000269|PubMed:32313945}; | null | null | null | null | FUNCTION: RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (By similarity). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs (PubMed:31914382). These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are not polyadenylated. During replication, the polymerase binds the 5' and 3' vRNA extremities at distinct sites (PubMed:32313945). In turn, significant conformational changes occur in the polymerase and in vRNA to initiate active RNA synthesis (By similarity). As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated (By similarity). {ECO:0000250|UniProtKB:A5HC98, ECO:0000250|UniProtKB:P27316, ECO:0000269|PubMed:31914382, ECO:0000269|PubMed:32313945}. | Dabie bandavirus (Severe fever with thrombocytopenia virus) (Huaiyangshan banyangvirus) |
I0IUP3 | MCM8_CHICK | MSRDLRGRGCPRGRGFQGWRGGWRGGWRGGWRGGWRGRTQKVEWKRAPEPASSRLVQSTLDQFIPYKGWKLYFSEAYADKSPFVQKTQAFEKFFMQRIELYDKDEIERKGSILVDYKELIEDRELTKSIPNISTELRDMPQKILQCMGLAIHQVLTKDLERHAAELQVQEGLPLDGEPIINVPLIHARLYNYEPLTQLKNVRANCYGKYIALRGTVVRVSNIKPLCTKLAFVCGTCGDVQSVPLPDGKYTLPTKCLVPECRGRSFTPDRSSPLTATVDWQSVKVQELMSDDQREAGRIPRTIECELVQDLVDSCVPGDVVTITGVVKVSSTEEGASKNKNDKCVFLLYIEANSVSNSKGQKTKNFEEETFQRSFMEFSLKDLYAVQEIQAEENLFRIIVNSLCPAIYGHEIVKAGLALALFGGCQKFVDDKNRIPVRGDPHVLIVGDPGLGKSQMLQAVCNVAPRGVYVCGNTSTSSGLTVTLSRDGASGDFALEAGALVLGDQGICGIDEFDKMGSQHQALLEAMEQQSISLAKAGIVCSLPARTSIVAAANPVGGHYNKAKTVSENLKMGSALLSRFDLVFILLDTPNEDHDHLLSEHVMAIRAGKQAVCSSAVVSRTNVQDRSVLEVVSDRPLLERLKISPGENFDAIPHQLLRKYVGYARQYVHPHLSPEAAQVLQEFYLELRKQNQGASSTPITTRQLESLIRLTEARSRLELREKCTKEDAEDVIEIMKYSMLGTYSDEFGKLDFERSQHGSGMSNRSQAKRFVSALSSIAERTYSNLFDLQQLRQVAKELQIRVFDFESFIESLNDQGYLLKKGSRLYQLQTM | 3.6.4.12 | null | DNA damage response [GO:0006974]; double-strand break repair via homologous recombination [GO:0000724] | MCM complex [GO:0042555]; MCM8-MCM9 complex [GO:0097362]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; single-stranded DNA binding [GO:0003697]; single-stranded DNA helicase activity [GO:0017116] | PF00493;PF17855;PF17207; | 2.20.28.10;2.40.50.140;3.40.50.300; | MCM family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22771115}. Note=Localizes to nuclear foci and colocalizes with RAD51. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; | null | null | null | null | FUNCTION: Component of the MCM8-MCM9 complex, a complex involved in homologous recombination repair following DNA interstrand cross-links and plays a key role during gametogenesis. The MCM8-MCM9 complex probably acts as a hexameric helicase required to process aberrant forks into homologous recombination substrates and to orchestrate homologous recombination with resection, fork stabilization and fork restart. {ECO:0000269|PubMed:22771115}. | Gallus gallus (Chicken) |
I0IUP4 | MCM9_CHICK | MALRADQVSLIGQVFESYLLQHHRDDILGILRQGDDEAHYPVLVDALTLFETNMEIGEYFNAFPSQVLPIFDGALRRAAMAVLQAATPSPELRMKPNLHARISGLPICPELTREHIPKTRDVGHFLSVTGTVIRTSLVKVLEFERSYICNKCKHVFVAKADFEQYYAFCRPSACLNEEGCNSTKFTCLSGTSSSPSSCRDYQEIKIQEQVQRLSVGSIPRCMVVVLEDDLVDSCKSGDDITVYGVVMQRWKPFHQDARCDLELVLKANYVKVNNEQLAGVTIDEEVRKEFEDFWEKHRNNPLAGRNEILASLCPQVFGLYLVKLAVAMVLAGGVQRIDATGTRIRGESHLLLVGDPGTGKSQFLKYAVKITPRSVLTAGIGSTSAGLTVTAVKDFGEWNLEAGALVLADGGLCCIDEFNSIKEHDRTSIHEAMEQQTISVAKAGLVCKLNTRTTILAATNPKGHYDPAESVSVNIALGSPLLSRFDLVLVLLDTKNEEWDRIISSFILQNKGCPSKSEKLWSMEKMKTYFCLIKRIQPKLSDESNLILVRYYQMQRQSDCRNAARTTIRLLESLIRLAEAHARLMFRDTVTLEDAVTVVSVMESSMQGGALLGAINALHTSFPENPMTQYRMQCELILERLELHDLLHKELQRLDRLQKETYCQLQPEETSFSTITGCLNKNTFESKQKSQSEPSDQQKINSYPQPSLPKSNCEGDKHPEALRNPTPGNNISTKRLSRLNKRSDDGSLGWFDRLEDRNTDAEETFWKTSPLPKTSPDNMALKTMSKSSCSEEGNSSVPRKEDGMRGSLRTVTLCAPLEQDKVSEISSKRTEERKCFSSEANIQDPTSASASVQESVITQRVSKSLQRLHTEKSHRFFTSTQNSEANALPSVLPVSGLLDLSSDTDSVVGDENNSASAAVKHAVISMRKRSKGQAEKEAKAVSSHEPEITDGESPPAAKLAKFSFRPRTKLDDSSEKKNAEFPLFPSENTVKPGEQPQGEQLQKDCCPPEKRKMTLTCLGRKGLEKQSIGSKGNEEQLSQALGKEMGGNALIHSDVTLDVVSPPPTEKRREGEEKLGGPSTVRVCSSTLENLSKFCFASRPDSKSEAPPTIKTDTNNKESHSPLLKVHVSNPNKRKSFALGNASKDSVVTRKSLFSIAELDDATLDFDWD | 3.6.4.12 | null | DNA damage response [GO:0006974]; double-strand break repair via homologous recombination [GO:0000724] | MCM complex [GO:0042555]; MCM8-MCM9 complex [GO:0097362]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; single-stranded DNA binding [GO:0003697]; single-stranded DNA helicase activity [GO:0017116] | PF00493;PF17855;PF17207; | 2.40.50.140;3.40.50.300; | MCM family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22771115}. Note=Localizes to nuclear foci and colocalizes with RAD51. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; | null | null | null | null | FUNCTION: Component of the MCM8-MCM9 complex, a complex involved in homologous recombination repair following DNA interstrand cross-links and plays a key role during gametogenesis. The MCM8-MCM9 complex probably acts as a hexameric helicase required to process aberrant forks into homologous recombination substrates and to orchestrate homologous recombination with resection, fork stabilization and fork restart. {ECO:0000269|PubMed:22771115}. | Gallus gallus (Chicken) |
I0J1I6 | BSR_PSETA | MPFSRTLLALSLGMALLQNPAFAAPPLSMTDGVAQVNTQDSNAWVEINKAAFEHNIRTLQTALAGKSQICAVLKADAYGHGIGLLMPSVIAMGVPCVGVASNEEARVVRESGFKGQLIRVRTAALSELEAALPYNMEELVGNLDFAVKASLIAEDHGRPLVVHLGLNSSGMSRNGVDMTTAQGRRDAVAITKVPNLEVRAIMTHFAVEDAADVRAGLKAFNQQAQWLMNVAQLDRSKITLHAANSFATLEVPESHLDMVRPGGALFGDTVPSHTEYKRVMQFKSHVASVNSYPKGNTVGYGRTYTLGRDSRLANITVGYSDGYRRAFTNKGIVLINGHRVPVVGKVSMNTLMVDVTDAPDVKSGDEVVLFGHQGKAEITQAEIEDINGALLADLYTVWGNSNPKILKDQ | 5.1.1.10 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000269|PubMed:19300994}; | peptidoglycan biosynthetic process [GO:0009252] | cytosol [GO:0005829]; periplasmic space [GO:0042597] | alanine racemase activity [GO:0008784]; arginine racemase activity [GO:0047679]; lysine racemase activity [GO:0018113]; methionine racemase activity [GO:0018111]; ornithine racemase activity [GO:0050157]; pyridoxal phosphate binding [GO:0030170] | PF00842;PF01168; | 3.20.20.10; | Alanine racemase family, Bsr subfamily | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000269|PubMed:19300994}. Note=Is translocated into the periplasm via a Tat-independent protein translocation pathway and, therefore, must have been translocated via the Sec route. {ECO:0000269|PubMed:19300994}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid = a D-alpha-amino acid; Xref=Rhea:RHEA:18317, ChEBI:CHEBI:59869, ChEBI:CHEBI:59871; EC=5.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000269|PubMed:19300994, ECO:0000269|PubMed:20564572}; CATALYTIC ACTIVITY: Reaction=L-lysine = D-lysine; Xref=Rhea:RHEA:22864, ChEBI:CHEBI:32551, ChEBI:CHEBI:32557; Evidence={ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000269|PubMed:19300994, ECO:0000269|PubMed:20564572}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22866; Evidence={ECO:0000269|PubMed:19300994}; CATALYTIC ACTIVITY: Reaction=L-arginine = D-arginine; Xref=Rhea:RHEA:18069, ChEBI:CHEBI:32682, ChEBI:CHEBI:32689; Evidence={ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000269|PubMed:19300994, ECO:0000269|PubMed:20564572}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18071; Evidence={ECO:0000269|PubMed:19300994}; CATALYTIC ACTIVITY: Reaction=L-ornithine = D-ornithine; Xref=Rhea:RHEA:11584, ChEBI:CHEBI:46911, ChEBI:CHEBI:57668; Evidence={ECO:0000269|PubMed:19300994, ECO:0000269|PubMed:20564572}; CATALYTIC ACTIVITY: Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249, ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; Evidence={ECO:0000269|PubMed:19300994, ECO:0000269|PubMed:20564572}; CATALYTIC ACTIVITY: Reaction=L-methionine = D-methionine; Xref=Rhea:RHEA:12492, ChEBI:CHEBI:57844, ChEBI:CHEBI:57932; Evidence={ECO:0000269|PubMed:19300994}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.4 mM for L-lysine {ECO:0000269|PubMed:20564572}; KM=2.4 mM for D-lysine {ECO:0000269|PubMed:20564572}; KM=1.2 mM for L-arginine {ECO:0000269|PubMed:20564572}; KM=1.2 mM for D-arginine {ECO:0000269|PubMed:20564572}; KM=3.7 mM for L-ornithine {ECO:0000269|PubMed:20564572}; KM=3.6 mM for D-ornithine {ECO:0000269|PubMed:20564572}; KM=15.7 mM for L-alanine {ECO:0000269|PubMed:20564572}; KM=15 mM for D-alanine {ECO:0000269|PubMed:20564572}; Note=kcat is 109.0 sec(-1) with L-lysine as substrate. kcat is 104.0 sec(-1) with D-lysine as substrate. kcat is 119.0 sec(-1) with L-arginine as substrate. kcat is 119.0 sec(-1) with D-arginine as substrate. kcat is 87.7 sec(-1) with L-ornithine as substrate. kcat is 87.3 sec(-1) with D-ornithine as substrate. kcat is 2.4 sec(-1) with L-alanine as substrate. kcat is 2.6 sec(-1) with D-alanine as substrate. {ECO:0000269|PubMed:20564572}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:19300994}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 65 degrees Celsius. {ECO:0000269|PubMed:19300994}; | FUNCTION: Amino-acid racemase able to utilize a broad range of substrates. Is mostly active with lysine and arginine and, to a lesser extent, with ornithine, whereas is about 10 times less active with alanine, methionine and ethionine. With phenylalanine as substrate only a trace activity is detectable, and is inactive with glutamate. Plays a key role in the catabolism of D-arginine and D-lysine, that allows P.taetrolens strain NBRC 3460 to grow on these basic D-amino acids as a sole carbon source. {ECO:0000269|PubMed:19300994}. | Pseudomonas taetrolens |
I1C083 | RLT1_RHIO9 | MYFEEGRLFFIKSQFNGRVLDVEDGSTEDDANIIVYTQKYEDCLNQLWRYENGYFINAKSAKVLDIRGGEMQPESQIIQYAQKMVEEAANQRWAIDEDGYIFCEARPDLVLDIQGAEDEDCVPVILYERREGEVSANQRWELVPFEG | 3.2.2.22 | null | depurination [GO:0045007]; negative regulation of translation [GO:0017148]; symbiont-mediated perturbation of host translation [GO:0019057] | extracellular region [GO:0005576] | rRNA N-glycosylase activity [GO:0030598]; toxin activity [GO:0090729] | PF00652; | 2.80.10.50; | Ribosome-inactivating protein family, Type 1 RIP subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33462434}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.; EC=3.2.2.22; Evidence={ECO:0000269|PubMed:33462434}; | null | null | null | null | FUNCTION: N-glycosylase that inhibits protein synthesis in the host by depurinating ribosomal rRNA, and thus acts as a ribosomal inactivating protein (RIP) (PubMed:33462434). Promotes vascular permeability in the host and induces necrosis and apoptosis of host alveolar epithelial cells (PubMed:33462434). {ECO:0000269|PubMed:33462434}. | Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar) |
I1C4E4 | COTH2_RHIO9 | MKLSLTIVSSSFLVAIAHAASVQFNLIAPSATDVKVSVNGQQVALTASDPNVPYFTGSAEVGGTEESFERSLAGITNSTFNDFYNRPVTYANLPQLPWPIENDPQWTRKGKKAEIFDDNYIPSVFFHGDDSQVQDLVKNVPKDKVTGTLTFIGSNYVHSFANVSFGIHGAGKKHNNAKQSWKWTLSGTDTMGNRNHFKLRHMEEDPTQIRERLYADILHAMGTYANETTMVRLFINGQGFGTFNMLDDITEFSYINAMFYGGNPPATLGPLFDGASGADFIYHPGNLDGYSSWKPNKDNANGEGYEAFDPLCKAWNETDYTDNTAIANFEKMFDTEHFLRFMVIEYLTAHWDGYWMGQTNDGAYRDPSDNNKWYFLDQDFDATFGVNLDVPENKDFISVSYKDFPSRYPAGVMANGLLQNADKKAKFEQYLTETVRVLFNNVTLTNRVLAIHNFLSPDLEWDRSIVQQSPGTNFGWTFEQTSQNLWQGVSAPNNNGGGAEWGLVEYIAAKSQAMAKEFNITIVSEPVGPPAANGTATSTNDGGNTHTAAGESKPASSSESSGSKIASQSVSGASRSAVSTVLLGVTALVATAIF | null | null | adhesion of symbiont to host endothelial cell [GO:0044652]; symbiont entry into host [GO:0044409] | plasma membrane [GO:0005886]; side of membrane [GO:0098552] | host cell surface receptor binding [GO:0046789] | PF08757; | null | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24355926}; Lipid-anchor, GPI-anchor {ECO:0000255}. | null | null | null | null | null | FUNCTION: Promotes invasion of host epithelial cells by adhering to receptors on the host cell surface to facilitate endocytosis of the pathogen into host cells (PubMed:24355926). Binds HSPA5/BiP protein on the cell surface of host epithelial cells (PubMed:24355926). {ECO:0000269|PubMed:24355926}. | Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar) |
I1CFE1 | COTH3_RHIO9 | MKLSIISAAFLVAITHAASIKFNVIAPNATDVKVSVNGQQVTLTASDANVPYFTGSAEVGASKTYKYVAGGTEESFDRSLDGITNSTLNDFYNRPVTYANLPQLPWPIEKDPQWTRSGSKADIFDDNYIPSVFFHGDDSQVQNVVKNVPADRISGTLTFIGSNYVYSFQNVSFGIHGAGKKHNNAKQSWNWILSGSDTMGNRNFFKLRHMEEDPTQIRERLYSDILHAMGTYANDATMVRLFINNQGFGTFNMLDDITQFSYINAKFYNGKPPATLGPLYDGASGADFLYHPGNLDGYSSWVANTANPNGEAYEALDPLCKAWNETTYTDNTAIANFEKMFDLDRFMRFMVIEYLTADWDGYWMGQTNDGAYRDPTDNNKWYFLDQDFDGTFGVNLAAPEGNAFLDVSYKDFPSRYPGAVMINNLLQNADKKATFEKYLTETVRVLFNNVTLTNRVLALHNFLLPDLEWDRSIVQQSPGINFGWTFDQVTQNLWQGVTAPNNNGGGAAFGLVEYIAAKAQAVAKEFNISIVSQPVGPPSANGTTAAAPAPAAGNSTGKGGNQSISSSASSNKTSAQSTSGASRSKTAPIVLAISALALLVF | null | null | adhesion of symbiont to host endothelial cell [GO:0044652]; adhesion of symbiont to host epithelial cell [GO:0044651]; symbiont entry into host [GO:0044409] | plasma membrane [GO:0005886]; side of membrane [GO:0098552] | host cell surface receptor binding [GO:0046789] | PF08757; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24355926}; Lipid-anchor, GPI-anchor {ECO:0000255}. | null | null | null | null | null | FUNCTION: Promotes invasion of host epithelial cells by adhering to receptors on the host cell surface to facilitate endocytosis of the pathogen into host cells (PubMed:24355926, PubMed:32487760). Binds HSPA5/BiP protein on the cell surface of host nasal epithelial cells (PubMed:24355926). {ECO:0000269|PubMed:24355926, ECO:0000269|PubMed:32487760}. | Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar) |
I1GN76 | VRN1_BRADI | MGRGKVQLKRIENKINRQVTFSKRRSGLLKKAHEISVLCDAEVALIIFSTKGKLYEFATDSCMDKILERYERYSYAEKVLVSTESEIQGNWCHEYRKLKAKVETIQKCQKHLMGEDLESLNLKELQQLEQQLESSLKHIRSRKNQLMHESISELQRKERSLQEENKALQKELVEKQKAHTQQAQWEQTHPQTSSSSSSMQREAPPTTNISNRPAAAGERTEEAAGQAQARVGLPPWMVSHISG | null | null | cold acclimation [GO:0009631]; negative regulation of vernalization response [GO:0010221]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of vernalization response [GO:0010220]; regulation of photoperiodism, flowering [GO:2000028]; regulation of transcription by RNA polymerase II [GO:0006357]; vernalization response [GO:0010048] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF01486;PF00319; | 3.40.1810.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}. | null | null | null | null | null | FUNCTION: Component of a grass-specific mechanism of vernalization, a process by which prolonged cold exposure provides competence to flower in daylengths longer than 12 hours (PubMed:28584114, PubMed:28690631). Involved in the exit of vernalization and confers flowering competency at the expense of freezing tolerance, probably by promoting the expression of VRN3; this process is essential in cv. Bd29-1 for flowering but seems do not occur in cv. Bd21 (PubMed:28584114, PubMed:28690631). {ECO:0000269|PubMed:28584114, ECO:0000269|PubMed:28690631}. | Brachypodium distachyon (Purple false brome) (Trachynia distachya) |
I1GQE7 | C85A1_BRADI | MVLAVLIGVLVGIVLVSSLLLRWNEVRYSRKQGLPPGTMGWPLFGETTEFLKQGPSFMKARRLRYGSLFRTHILGCPTVVCMDPELNRQMLQQGEGRGFVPGYPQSMLDILGRNNIAAVHGPLHRAMRGSMLALVRPASIRSSLLPKIDAFMRSHLHGWAGDLVDIQDKTKEMALLSALRQIAGITAGPLSDALKTELYTLVLGTISLPINLPGTSYYQGFQARKKLVSMLEKMIAERRSSGLVHNDMLDALLSGNDGTRERLSDEQIIDLIITLIYSGYETMSTTSMMAVKYLSDHPKALEELRKEHFDIRKGKSPEEAIDYNDFKSMTFTRAVIFETLRLATVVNGLLRKTTQDVEMNGYVIPKGWRIYVYTREINYDPCLYPDPMTFNPWRWLEKNMESHPHFMLFGGGGRMCPGKEVGTAEIATFLHYFVTRYRWEEEGTNTILKFPRVEAPNGLHIRVQNY | 1.14.14.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | brassinosteroid biosynthetic process [GO:0016132]; brassinosteroid homeostasis [GO:0010268]; microtubule bundle formation [GO:0001578]; skotomorphogenesis [GO:0009647]; sterol metabolic process [GO:0016125] | membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=6-deoxoteasterone + O2 + reduced [NADPH--hemoprotein reductase] = 6alpha-hydroxyteasterone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69959, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20716, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188499; Evidence={ECO:0000269|PubMed:32146811}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69960; Evidence={ECO:0000269|PubMed:32146811}; CATALYTIC ACTIVITY: Reaction=6alpha-hydroxytyphasterol + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] + teasterone; Xref=Rhea:RHEA:69963, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:26863, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188495; Evidence={ECO:0000269|PubMed:32146811}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69964; Evidence={ECO:0000269|PubMed:32146811}; CATALYTIC ACTIVITY: Reaction=3-dehydro-6-deoxoteasterone + O2 + reduced [NADPH--hemoprotein reductase] = 3-dehydro-6alpha-hydroxyteasterone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69947, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20710, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188496; Evidence={ECO:0000269|PubMed:32146811}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69948; Evidence={ECO:0000269|PubMed:32146811}; CATALYTIC ACTIVITY: Reaction=3-dehydro-6alpha-hydroxyteasterone + O2 + reduced [NADPH--hemoprotein reductase] = 3-dehydroteasterone + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69951, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20000, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188496; Evidence={ECO:0000269|PubMed:32146811}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69952; Evidence={ECO:0000269|PubMed:32146811}; CATALYTIC ACTIVITY: Reaction=6-deoxotyphasterol + O2 + reduced [NADPH--hemoprotein reductase] = 6alpha-hydroxytyphasterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69939, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20717, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188495; Evidence={ECO:0000269|PubMed:32146811}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69940; Evidence={ECO:0000269|PubMed:32146811}; CATALYTIC ACTIVITY: Reaction=6alpha-hydroxytyphasterol + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] + typhasterol; Xref=Rhea:RHEA:69943, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:27173, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188495; Evidence={ECO:0000269|PubMed:32146811}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69944; Evidence={ECO:0000269|PubMed:32146811}; CATALYTIC ACTIVITY: Reaction=6-deoxocastasterone + O2 + reduced [NADPH--hemoprotein reductase] = 6alpha-hydroxycastasterone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69875, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20712, ChEBI:CHEBI:20760, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:32146811}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69876; Evidence={ECO:0000269|PubMed:32146811}; CATALYTIC ACTIVITY: Reaction=6alpha-hydroxycastasterone + O2 + reduced [NADPH--hemoprotein reductase] = castasterone + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69879, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20760, ChEBI:CHEBI:23051, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:32146811}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69880; Evidence={ECO:0000269|PubMed:32146811}; CATALYTIC ACTIVITY: Reaction=3-dehydro-6-deoxoteasterone + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = 3-dehydroteasterone + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70039, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20000, ChEBI:CHEBI:20710, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:32146811}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70040; Evidence={ECO:0000269|PubMed:32146811}; CATALYTIC ACTIVITY: Reaction=6-deoxocastasterone + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = castasterone + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70031, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20712, ChEBI:CHEBI:23051, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:32146811}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70032; Evidence={ECO:0000269|PubMed:32146811}; CATALYTIC ACTIVITY: Reaction=6-deoxoteasterone + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase] + teasterone; Xref=Rhea:RHEA:70043, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20716, ChEBI:CHEBI:26863, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:32146811}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70044; Evidence={ECO:0000269|PubMed:32146811}; CATALYTIC ACTIVITY: Reaction=6-deoxotyphasterol + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase] + typhasterol; Xref=Rhea:RHEA:70035, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20717, ChEBI:CHEBI:27173, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:32146811}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70036; Evidence={ECO:0000269|PubMed:32146811}; | null | PATHWAY: Plant hormone biosynthesis; brassinosteroid biosynthesis. {ECO:0000269|PubMed:32146811}. | null | null | FUNCTION: Involved in reduction steps of the biosynthesis of plant campesterol-derivative steroids, ending to castasterone (CS) but missing brassinolide (BL) (PubMed:32146811). Catalyzes the C6-oxidation step in brassinosteroids biosynthesis; the conversion of 6-deoxoteasterone (6-deoxoTE) to teasterone (TE), 3-dehydro-6-deoxoteasterone (6-deoxo3DT, 6-deoxo-3-DHT) to 3-dehydroteasterone (3DT, 3-DHT), 6-deoxotyphasterol (6-deoxoTY) to typhasterol (TY) and of 6-deoxocastasterone (6-deoxoCS) to castasterone (CS) (PubMed:32146811). {ECO:0000269|PubMed:32146811}. | Brachypodium distachyon (Purple false brome) (Trachynia distachya) |
I1GTC2 | BDTIR_BRADI | MASSGLSSRRSIMASRLTASAEAVNEPRRGAVVSRRVEYDEESLAGAGGESRYEVFINHRGVDTKRTVARLLYDRLAQAGLRGFLDNMSMRPGDRLEERIGSAIRECTVAVAIFSPSYCDSEYCLRELAMLVESRKAIIPIFYDIKPSDLLLPQAVADSEVYLPRDLERFKFALREAKHTVGITYDSATGDMAELVSAAADAVMYNMEKMETVQRRETMILSRL | 3.2.2.-; 3.2.2.6 | null | defense response [GO:0006952]; NAD catabolic process [GO:0019677]; positive regulation of programmed cell death [GO:0043068]; signal transduction [GO:0007165] | null | NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; NADP+ nucleosidase activity [GO:0050135] | PF13676; | 3.40.50.10140; | null | null | null | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence={ECO:0000269|PubMed:31439793}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence={ECO:0000269|PubMed:31439793}; CATALYTIC ACTIVITY: Reaction=H2O + NADP(+) = ADP-D-ribose 2'-phosphate + H(+) + nicotinamide; Xref=Rhea:RHEA:19849, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:58349, ChEBI:CHEBI:58673; Evidence={ECO:0000269|PubMed:31439793}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19850; Evidence={ECO:0000269|PubMed:31439793}; CATALYTIC ACTIVITY: Reaction=NAD(+) = 2'cADPR + H(+) + nicotinamide; Xref=Rhea:RHEA:75299, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:194248; Evidence={ECO:0000305|PubMed:36174646}; | null | null | null | null | FUNCTION: An NAD(+) hydrolase (NADase). Upon activation catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide; NAD(+) cleavage triggers a defense system that promotes cell death (PubMed:31439793). In addition to ADPR, also generates a cyclization variant of cyclic ADPR termed v-cADPR (2'cADPR) (PubMed:31439793). Also hydrolyzes NADP(+), but not other NAD(+)-related molecules (PubMed:31439793). v-cADPR activates ThsA, an NAD(+) hydrolase in B.cereus (AC J8G6Z1) (PubMed:34853457). Probably makes 2'cADPR; the cADPR made by this protein is bound by cmTad1 (AC P0DW61) and activates ThsA from B.cereus (PubMed:36174646). Boiling cmTad1 bound to the cyclic nucleotide releases 2'cADPR, strongly suggesting it is the product of this protein (Probable) (PubMed:36174646). {ECO:0000269|PubMed:31439793, ECO:0000269|PubMed:34853457, ECO:0000305|PubMed:36174646}. | Brachypodium distachyon (Purple false brome) (Trachynia distachya) |
I1H7R8 | C90B1_BRADI | MAAMMASITSELLFFLPYILLALLTFYTTTVAKCHRWRRTEEKRRCPNLPPGAIGWPFIGETFGYLRAHPATSVGRFMEEHIARYGKIYRSSLFGDRTVVSADAGLNRYILQNEGKLFECSYPRSIGGILGKWSMLVLVGDPHREMRAISLNFLSSLRLRAVLLPEVERHTLLVLRHWPSASPAVFSAQHEAKKFTFNLMAKNIMSMDPGEEETERLRLEYITFMKGVVSAPLNFPGTAYWKALKSRATILGVIERKMEDRLQKMNKEDSSIEEDDLLGWAMKQSNLSKEQILDLLLSLLFAGHETSSMALALAIFFLEGCPKAVQELREEHLEIARRQRLRGECKLSWEDYKDMVFTQCVINETLRLGNVVRFLHRKVIRDVHYKGYDIPSGWKILPVLAAVHLDSSLYEDPSRFNPWRWKGNASGVAQSGNFMPYGGGTRLCAGSELAKLEMAIFLHHLVLNFRWELAEPDQAFVYPFVDFPKGLPIRVHRIAQEEEKSVLTVDI | 1.14.14.178 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | brassinosteroid biosynthetic process [GO:0016132]; brassinosteroid homeostasis [GO:0010268]; jasmonic acid mediated signaling pathway [GO:0009867]; leaf shaping [GO:0010358]; response to brassinosteroid [GO:0009741]; sterol metabolic process [GO:0016125]; unidimensional cell growth [GO:0009826] | endoplasmic reticulum [GO:0005783]; membrane [GO:0016020] | fatty acid alpha-hydroxylase activity [GO:0080132]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; steroid 22-alpha hydroxylase activity [GO:0010012] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a C27-steroid + O2 + reduced [NADPH--hemoprotein reductase] = a (22S)-22-hydroxy C27-steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70059, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188919, ChEBI:CHEBI:188920; EC=1.14.14.178; Evidence={ECO:0000269|PubMed:32146811}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70060; Evidence={ECO:0000269|PubMed:32146811}; CATALYTIC ACTIVITY: Reaction=a C28-steroid + O2 + reduced [NADPH--hemoprotein reductase] = a (22S)-22-hydroxy C28-steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70063, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188921, ChEBI:CHEBI:188922; EC=1.14.14.178; Evidence={ECO:0000269|PubMed:32146811}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70064; Evidence={ECO:0000269|PubMed:32146811}; CATALYTIC ACTIVITY: Reaction=campesterol + O2 + reduced [NADPH--hemoprotein reductase] = (22S)-22-hydroxycampesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69835, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28623, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:72331; Evidence={ECO:0000269|PubMed:32146811}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69836; Evidence={ECO:0000269|PubMed:32146811}; CATALYTIC ACTIVITY: Reaction=campestanol + O2 + reduced [NADPH--hemoprotein reductase] = 6-deoxycathasterone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69831, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20714, ChEBI:CHEBI:36799, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:32146811}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69832; Evidence={ECO:0000269|PubMed:32146811}; | null | PATHWAY: Plant hormone biosynthesis; brassinosteroid biosynthesis. {ECO:0000269|PubMed:32146811}. | null | null | FUNCTION: Involved in reduction steps of the biosynthesis of plant campesterol-derivative steroids, ending to castasterone (CS) but missing brassinolide (BL) (PubMed:32146811). Catalyzes the conversion of campesterol (CR) to (22S)-22-hydroxycampesterol (22-OHCR, 22-hydroxyCR) and of campestanol (CN) to 6-deoxycathasterone (6-deoxoCT) (PubMed:32146811). {ECO:0000269|PubMed:32146811}. | Brachypodium distachyon (Purple false brome) (Trachynia distachya) |
I1JNS6 | GIP1_SOYBN | MPPPLPSLCNFNLAILFLFLTPTFQIPLIAPISKDDTTQLYTLSVFLKTPLQPTKLHLHLGSSLSWVLCDSTYTSSSSHHIPCNTPLCNSFPSNACSNNSSLCALFPENPVTRNTLLDTALIDSLALPTYDASSSLVLISDFIFSCATAHLLQGLAANALGLASLGRSNYSLPAQISTSLTSPRSFTLCLPASSANTGAAIFASTASSFLFSSKIDLTYTQLIVNPVADTVVTDNPQPSDEYFINLTSIKINGKPLYINSSILTVDQTGFGGTKISTAEPYTVLETSIYRLFVQRFVNESSAFNLTVTEAVEPFGVCYPAGDLTETRVGPAVPTVDLVMHSEDVFWRIFGGNSMVRVAKGGVDVWCLGFVDGGTRGRTPIVIGGHQLEDNLMQFDLDSNRFGFTSTLLLQDAKCSNLKVNNFANGIK | 3.4.23.- | null | defense response [GO:0006952]; proteolysis [GO:0006508] | apoplast [GO:0048046] | aspartic-type endopeptidase activity [GO:0004190] | PF14541;PF14543; | 2.40.70.10; | Peptidase A1 family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast {ECO:0000305|PubMed:28082413}. | null | null | null | null | null | FUNCTION: Involved in plant defense against Phytophtora sojae (PubMed:28082413). Contributes positively to soybean resistance against P.sojae (PubMed:28082413). Binds the P.sojae xyloglucanase XEG1 and inhibits its cell wall degrading enzyme activity and its contribution as P.sojae virulence factor (PubMed:28082413). XEG1 acts as an important virulence factor during P.sojae infection but also acts as a pathogen-associated molecular pattern (PAMP) in soybean and solanaceous species, where it can trigger defense responses including cell death (PubMed:26163574). {ECO:0000269|PubMed:26163574, ECO:0000269|PubMed:28082413}.; FUNCTION: (Microbial infection) Possesses stronger binding affinity with XLP1, a truncated paralog of P.sojae XEG1 which has no enzyme activity. Is impaired in its inhibitor activity towards the P.sojae xyloglucanase XEG1 when hijacked by XLP1 binding. {ECO:0000269|PubMed:28082413}. | Glycine max (Soybean) (Glycine hispida) |
I1MRZ6 | DAT32_SOYBN | MEISGTVLRQVSYVSGYGTHTRSRGLAPRFGVRMGMGSGFCDEGHLRYYQDTKKVLTPKKKLKLLKGFSKLGLASDPEKLAMFYDLQQNLTSDAGDVLLRELEAARAKEKEVKKKRKQEKKAKLKAAKMNCESSSSSSSESSDSDCGCDQVVDMNTFRAGVGVGVGVGVGVVAPAPVEESPLPKTAPIVEDANAHCVAMELCSKNDIYVSSASNGFKNESAVVTSAPQKRIEVCMGNKCKRSGAAALMQEFEKVVGVEGVAVVACKCMGKCKTAPNVKVQNSVDHNSLAQGLDDSVKIPANPLCIGVGLEDVDAIVARYFWESHTDIGMAGAGAATAT | 2.3.1.20 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250|UniProtKB:Q9C5W0}; | lipid metabolic process [GO:0006629]; triglyceride biosynthetic process [GO:0019432] | cytoplasm [GO:0005737] | diacylglycerol O-acyltransferase activity [GO:0004144]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872] | null | 3.40.30.10; | Diacylglycerol acyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:35693158}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; Evidence={ECO:0000269|PubMed:35693158}; | null | PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis. {ECO:0000269|PubMed:35693158}. | null | null | FUNCTION: Involved in triacylglycerol (TAG) biosynthesis (PubMed:35693158). Catalyzes the acylation of the sn-3 hydroxy group of sn-1,2-diacylglycerol using acyl-CoA (PubMed:35693158). Incorporates preferentially monounsaturated fatty acids (MUFAs), especially oleic acid (C18:1) and to some extent palmitoleic acid (C16:1), into TAGs accumulating in seeds oil (PubMed:35693158). Can also use, with low efficiency, hexadecanoic acid (C16:0), linoleic acid (C18:2) and linolenic acid (C18:3) as acyl-CoA substrates (PubMed:35693158). {ECO:0000269|PubMed:35693158}. | Glycine max (Soybean) (Glycine hispida) |
I1RAQ3 | CFMN1_GIBZE | MKLSVFTSVLLAGLVAAQQEKLPKCAQPCVDQYTTGGGVAGCGQLDIKCICSNKNFLSGIACCLEKECDAQGKETAVKYAKQICATAGVTDLPDDVTCDKSAASSGTASGTATGATTPTSSDSTNTASATGGSSTVEPNAGAREGAAGFIGVGMAMLLAL | null | null | effector-mediated suppression of host innate immune response [GO:0140403] | cell septum [GO:0030428]; cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576] | metal ion binding [GO:0046872] | PF05730; | null | RBT5 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Cell septum {ECO:0000269|PubMed:36577386}. Cytoplasm {ECO:0000269|PubMed:36577386}. Secreted {ECO:0000269|PubMed:36577386}. Note=Present at the cell surface of invading hyphae growing intra- and intercellularly in the host, and in conidia (PubMed:36577386). Present in septa of conidia (PubMed:36577386). Present in the cytoplasm of germ tubes and in hyphae (PubMed:36577386). {ECO:0000269|PubMed:36577386}. | null | null | null | null | null | FUNCTION: Suppresses host programmed cell death during infection by binding to Z.mays WAK17 isoform 2 and Z.mays LRR5, to prevent activation of Z.mays WAK17 isoform 1 and the downstream hypersensitive response. {ECO:0000269|PubMed:36577386}. | Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum) |
I1RBR4 | CP51B_GIBZE | MGLLQELAGHPLAQQFQELPLGQQVGIGFAVFLVLSVVLNVLNQLLFRNPNEPPMVFHWFPFVGSTITYGMDPPTFFRENRAKHGDVFTFILLGKKTTVAVGPAGNDFILNGKLKDVCAEEIYTVLTTPVFGKDVVYDCPNAKLMEQKKFMKIALTTEAFRSYVPIISSEVRDYFKRSPDFKGKSGIADIPKKMAEITIFTASHALQGSAIRSKFDESLAALYHDLDMGFTPINFMLHWAPLPWNRKRDHAQRTVAKIYMDTIKERRAKGNNESEHDMMKHLMNSTYKNGIRVPDHEVAHMMIALLMAGQHSSSSTSSWIMLRLAQYPHIMEELYQEQVKNLGADLPPLTYEDLAKLPLNQAIVKETLRLHAPIHSIMRAVKSPMPVPGTKYVIPTSHTLLAAPGVSATDSAFFPNPDEWDPHRWEADSPNFPRMASKGEDEEKIDYGYGLVSKGSASPYLPFGAGRHRCIGEHFANAQLQTIVAEVVREFKFRNVDGGHTLIDTDYASLFSRPLEPANIHWERRQ | 1.14.14.154 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P10614}; | ergosterol biosynthetic process [GO:0006696] | endoplasmic reticulum membrane [GO:0005789] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:138031; EC=1.14.14.154; Evidence={ECO:0000305|PubMed:23442154}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54029; Evidence={ECO:0000305|PubMed:23442154}; CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-hydroxymethyl steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68060, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:176901; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68061; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=a 14alpha-hydroxymethyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-formyl steroid + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68064, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:176901, ChEBI:CHEBI:176902; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68065; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=a 14alpha-formyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68068, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138031, ChEBI:CHEBI:176902; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68069; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=lanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:25286, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16521, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.154; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25287; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; CATALYTIC ACTIVITY: Reaction=lanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxylanosterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75103, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16521, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166806; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75104; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-hydroxylanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxolanosterol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75107, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681, ChEBI:CHEBI:166806; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75108; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-oxolanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75111, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75112; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=eburicol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 14-demethyleburicol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75439, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:70315, ChEBI:CHEBI:194330; Evidence={ECO:0000305|PubMed:23442154}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75440; Evidence={ECO:0000305|PubMed:23442154}; CATALYTIC ACTIVITY: Reaction=eburicol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxyeburicol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75427, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:70315, ChEBI:CHEBI:194328; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75428; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-hydroxyeburicol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxoeburicol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75431, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:194328, ChEBI:CHEBI:194329; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75432; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-oxoeburicol + O2 + reduced [NADPH--hemoprotein reductase] = 14-demethyleburicol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75435, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:194329, ChEBI:CHEBI:194330; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75436; Evidence={ECO:0000250|UniProtKB:P10614}; | null | PATHWAY: Steroid metabolism; ergosterol biosynthesis. {ECO:0000305|PubMed:23442154}. | null | null | FUNCTION: Together with cyp51A and cyp51C, encodes the sterol 14alpha-demethylase that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (PubMed:20955812, PubMed:23442154). Essential for ascospore production (PubMed:23442154). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (By similarity). In filamentous fungi, during the initial step of this module, lanosterol (lanosta-8,24-dien-3beta-ol) can be metabolized to eburicol (By similarity). Sterol 14alpha-demethylase catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of both these sterols in the form of formate, and converts eburicol and lanosterol to 14-demethyleburicol (4,4,24-trimethylergosta-8,14,24(28)-trienol) and 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, respectively, which are further metabolized by other enzymes in the pathway to ergosterol (Probable). Can also use substrates not intrinsic to fungi, such as 24,25-dihydrolanosterol (DHL), producing 4,4'-dimethyl-8,14-cholestadien-3-beta-ol, but at lower rates than the endogenous substrates (By similarity). {ECO:0000250|UniProtKB:P10614, ECO:0000250|UniProtKB:Q4WNT5, ECO:0000269|PubMed:20955812, ECO:0000269|PubMed:23442154, ECO:0000305|PubMed:23442154}. | Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum) |
I1RC73 | FGSR_GIBZE | MPPRRSHKKSRAGCRRCKNRKIKCDEVHPRCGNCAKHGVPCDFSNPDVLEELAISTNTSTESVGAPTPSPAPTVNFNSAPRTPLTRPRAPSSPARAPRPNPSPPTSVYSQPSISSSTNTIDHGERMLELRLMHHYTNVTSKTLLTNSPAAEDIWQRAVPQMAFSGNGKTYLADAILSVAALHLRSMSPNDKALVRASHAYSASSLSAFGASLGAGITPENAEALFLTATLIAFQASASRIFVKDDGDAAPGDPTVRYVPPLSWFHAFQGVKTVVANSWQWIHHSDIVKVIIDSQPSFQLNLNPRSPDSFFGHMLEGLADELSNEDPRLVASTTQAYSHAVSVLNWAHKNYHAAAALTFTATVSKRYVDLVDARRPRALAILACFFALLKRMDNVWWLQDVARREVMGLVSLFEPGSKWWRHLEWPIRIAVLDGSSIPQDIWGTELEEQAPEQQNVLGSMTQHIEMFAEMLNQHTQPPIPIADEDLIVPDSPD | null | null | null | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; zinc ion binding [GO:0008270] | PF11951;PF00172; | 4.10.240.10; | null | PTM: Phosphorylation at Thr-82, Ser-92, Ser-102, thr-117 and ser-305 by HOG1 is required for regulating expression of ergosterol biosynthesis genes. {ECO:0000269|PubMed:30874562}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30874562}. | null | null | null | null | null | FUNCTION: Transcription factor that targets gene promoters containing 2 conserved CGAA repeat sequences (PubMed:30874562). Positively regulates the expression of ergosterol biosynthesis genes including CYP51A and CYP51B encoding the sterol 14-alpha demethylase, and ERG6A and ERG6B encoding the sterol 24-C-methyltransferase (PubMed:30874562). {ECO:0000269|PubMed:30874562}. | Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum) |
I1REI8 | CFM1_GIBZE | MKYSVAFVALAAVAAQAQSLADVPKCAIPCLDKAIASETSCDKTDLACVCKGFSAVRSKATSCVIDECGTDVAINEVLPATENLCKNPPKESEAKSTAEEEKPTTTAAATSTLVVVTTSAEVVETTAAATTTVAPIIPTTAAEEPATSTPAAATPTKGPEQANGAAGLKGLGALAMAAFAALAL | null | null | effector-mediated suppression of host innate immune response [GO:0140403] | cell septum [GO:0030428]; cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277] | metal ion binding [GO:0046872] | PF05730; | null | RBT5 family | null | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:36577386}. Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Cell septum {ECO:0000269|PubMed:36577386}. Cytoplasm {ECO:0000269|PubMed:36577386}. Secreted {ECO:0000269|PubMed:36577386}. Note=Present at the cell surface of invading hyphae growing intra- and intercellularly in the host, and in conidia (PubMed:36577386). Present in septa of conidia (PubMed:36577386). Present in the cytoplasm of germ tubes and in hyphae (PubMed:36577386). {ECO:0000269|PubMed:36577386}. | null | null | null | null | null | FUNCTION: Suppresses host programmed cell death during infection by binding to Z.mays WAK17 isoform 2 and Z.mays LRR5, to prevent activation of Z.mays WAK17 isoform 1 and the downstream hypersensitive response. {ECO:0000269|PubMed:36577386}. | Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum) |
I1RII8 | XYNB_GIBZE | MVSFTYLLAAVSAVTGAVAAPNPTKVDAQPPSGLLEKRTSPTTGVNNGFYFSFWTDTPSAVTYTNGNGGQFSMNWNGNRGNHVGGKGWNPGAARTIKYSGDYRPNGNSYLAVYGWTRNPLVEYYIVENFGTYNPSSGAQKKGEINIDGSIYDIAVSTRNCAPSIEGDCKTFQQYWSVRRNKRSSGSVNTGAHFNAWAQAGLRLGSHDYQILAVEGYQSSGQATMTVSG | 3.2.1.8 | null | xylan catabolic process [GO:0045493] | extracellular region [GO:0005576] | endo-1,4-beta-xylanase activity [GO:0031176] | PF00457; | 2.60.120.180; | Glycosyl hydrolase 11 (cellulase G) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15629130, ECO:0000269|PubMed:22313372}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; Evidence={ECO:0000269|PubMed:15629130, ECO:0000269|PubMed:22313372, ECO:0000269|Ref.7}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.2 mg/ml for wheat flour arabinoxylan {ECO:0000269|PubMed:15629130, ECO:0000269|PubMed:22313372, ECO:0000269|Ref.7}; KM=4.3 mg/ml for soluble oat spelt xylan {ECO:0000269|PubMed:15629130, ECO:0000269|PubMed:22313372, ECO:0000269|Ref.7}; KM=11.9 mg/ml for soluble birchwood xylan {ECO:0000269|PubMed:15629130, ECO:0000269|PubMed:22313372, ECO:0000269|Ref.7}; Vmax=18.4 umol/min/mg enzyme toward xylan {ECO:0000269|PubMed:15629130, ECO:0000269|PubMed:22313372, ECO:0000269|Ref.7}; Vmax=61.7 umol/min/mg enzyme toward arabinoxylan {ECO:0000269|PubMed:15629130, ECO:0000269|PubMed:22313372, ECO:0000269|Ref.7}; | PATHWAY: Glycan degradation; xylan degradation. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:15629130, ECO:0000269|PubMed:22313372, ECO:0000269|Ref.7}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:15629130, ECO:0000269|PubMed:22313372, ECO:0000269|Ref.7}; | FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Plays an important role in causing fusarium head blight (FHB) on cereal crops. Induces cell death and hydrogen peroxide accumulation in infected wheat leaves. {ECO:0000269|PubMed:22313372, ECO:0000269|PubMed:23337356, ECO:0000269|PubMed:24779355, ECO:0000269|Ref.7}. | Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum) |
I1RJR2 | CP51A_GIBZE | MFHLLIYPLWVLVALFAVIIANLLYQQLPRRPDEPPLVFHWFPFFGNAVAYGLDPCGFFEKCREKHGDVFTFILFGRKIVACLGVDGNDFVLNSRLQDANAEEVYGPLTIPVFGSDVVYDCPNSKLMEQKKFVKFGLTQKALESHVQLIEREVLDYVETDPSFSGRTSTIDVPKAMAEITIFTASRSLQGEEVRRKLTAEFAALYHDLDLGFRPVNFLFPWLPLPHNRKRDAAHIKMREVYMDIINDRRKGGIRTEDGTDMIANLMGCTYKNGQPVPDKEIAHMMITLLMAGQHSSSSASSWIVLHLASSPDITEELYQEQLVNLSVNGALPPLQYSDLDKLPLLQNVVKETLRVHSSIHSILRKVKRPMQVPNSPYTITTDKVIMASPTVTAMSEEYFENAKTWNPHRWDNRAKEEVDTEDVIDYGYGAVSKGTKSPYLPFGAGRHRCIGEKFAYVNLGVIVATLVRNFRLSTIDGRPGVPETDYTSLFSRPAQPAFIRWERRKKI | 1.14.14.154 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P10614}; | bile acid biosynthetic process [GO:0006699]; cholesterol homeostasis [GO:0042632]; sterol biosynthetic process [GO:0016126] | endoplasmic reticulum membrane [GO:0005789] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxysterol 7-alpha-hydroxylase activity [GO:0008396]; steroid 7-alpha-hydroxylase activity [GO:0008387] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:138031; EC=1.14.14.154; Evidence={ECO:0000305|PubMed:23442154}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54029; Evidence={ECO:0000305|PubMed:23442154}; CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-hydroxymethyl steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68060, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:176901; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68061; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=a 14alpha-hydroxymethyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-formyl steroid + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68064, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:176901, ChEBI:CHEBI:176902; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68065; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=a 14alpha-formyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68068, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138031, ChEBI:CHEBI:176902; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68069; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=lanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:25286, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16521, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.154; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25287; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; CATALYTIC ACTIVITY: Reaction=lanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxylanosterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75103, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16521, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166806; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75104; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-hydroxylanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxolanosterol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75107, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681, ChEBI:CHEBI:166806; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75108; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-oxolanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75111, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75112; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=eburicol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 14-demethyleburicol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75439, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:70315, ChEBI:CHEBI:194330; Evidence={ECO:0000305|PubMed:23442154}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75440; Evidence={ECO:0000305|PubMed:23442154}; CATALYTIC ACTIVITY: Reaction=eburicol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxyeburicol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75427, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:70315, ChEBI:CHEBI:194328; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75428; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-hydroxyeburicol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxoeburicol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75431, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:194328, ChEBI:CHEBI:194329; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75432; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-oxoeburicol + O2 + reduced [NADPH--hemoprotein reductase] = 14-demethyleburicol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75435, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:194329, ChEBI:CHEBI:194330; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75436; Evidence={ECO:0000250|UniProtKB:P10614}; | null | PATHWAY: Steroid metabolism; ergosterol biosynthesis. {ECO:0000305|PubMed:23442154}. | null | null | FUNCTION: Together with cyp51B and cyp51C, encodes the sterol 14alpha-demethylase that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (PubMed:20955812, PubMed:23442154). CYP51A encodes the sterol 14-alpha-demethylase induced on ergosterol depletion and is responsible for the intrinsic variation in azole sensitivity (PubMed:20955812, PubMed:23442154). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (By similarity). In filamentous fungi, during the initial step of this module, lanosterol (lanosta-8,24-dien-3beta-ol) can be metabolized to eburicol (By similarity). Sterol 14alpha-demethylase catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of both these sterols in the form of formate, and converts eburicol and lanosterol to 14-demethyleburicol (4,4,24-trimethylergosta-8,14,24(28)-trienol) and 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, respectively, which are further metabolized by other enzymes in the pathway to ergosterol (Probable). Can also use substrates not intrinsic to fungi, such as 24,25-dihydrolanosterol (DHL), producing 4,4'-dimethyl-8,14-cholestadien-3-beta-ol, but at lower rates than the endogenous substrates (By similarity). {ECO:0000250|UniProtKB:P10614, ECO:0000250|UniProtKB:Q4WNT5, ECO:0000269|PubMed:20955812, ECO:0000269|PubMed:23442154, ECO:0000305|PubMed:23442154}. | Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum) |
I1RL14 | DPFGD_GIBZE | MAQSVPPASSHGQLTVGEVGTSVNSVPYARHEEIIRAPLTYLLNLPGKDVRSKMIAAFNQWLKIPEDKLDVIKRIIMLLHNASLLLDDIQDSSKLRRGLPVSHSIFGIAQTINAANYAFFLAQQELPKLGDARAFEIFTEELLHLHRGQGMDIYWRDASICPTEEEYFTMVSNKTGGLFRLAVKLMQLASESDKDYVPLVNVLGVIFQIRDDYLNLQSGNYAKNKGFGEDLTEGKFSFPIIHSIRSNPANIQLSSILKQRTTDIDVKLFAVGYIESTGSFEHCRRKLVELTAEARAIMENIADGRSEDLESYACILLSKLILYNRLTYKVPAAQVIHGASGGYSTAPKPRILAQQIATVRAPHLQYAT | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | alcohol biosynthetic process [GO:0046165]; ketone biosynthetic process [GO:0042181]; mycotoxin biosynthetic process [GO:0043386]; terpenoid biosynthetic process [GO:0016114] | null | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000250|UniProtKB:Q12051}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:32286350}. | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of diterpenoid pyrones (PubMed:32286350). The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpfgA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpfgD through the action of the prenyltransferase dpfgC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpfgE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpfgB (Probable). The short chain dehydrogenase/reductase dpfgG then oxidizes the 8S hydroxy group to a ketone and the short chain dehydrogenase/reductase dpfgH reduces the ketone to the 8R hydroxy group to yield higginsianin B (PubMed:32286350). Higginsianin B is further methylated by the methyltransferase dpfgI to produce the intermediate named FDDP B (PubMed:32286350). The cytochrome P450 monooxygenase dfgpJ then catalyzes a three-step oxidation at C-27 to generate a carboxylic acid as well as C-26 hydroxylation (PubMed:32286350). Finally, methyltransferase dpfgK methylates the carboxylic acid generated by dpfgJ, yielding the final diterpenoid pyrones from the pathway which were named FDDP D and FDDP E (PubMed:32286350). {ECO:0000269|PubMed:32286350, ECO:0000305|PubMed:32286350}. | Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum) |
I1RNG8 | ATG1_GIBZE | MAGPQESSTSSGSRKSGSRAVGQFNIGSEIGKGSFAQVYLGWHKETKAAVAIKSVELERLNKKLRENLYSEIQILKTLRHPHIVALHDCIESTSHINLIMEYCELGDLSLFIKKREKLATHPATHDMARKYPSMPNSGLHEVVIRHFLKQLTSALEFLRSKNYVHRDVKPQNLLLLPSQPFRDQRSRPVMQASQDSLIPISGLASLPMLKLADFGFARVLPSTSLADTLCGSPLYMAPEILRYERYDAKADLWSVGTVLYEMSTGRPPFRARNHVELLRKIEAAEDVIKFPREVSITPELKALIRSLLKRSPVERLSFENFFTHQVVTSEIPGLVEDDIPKSLRQESRDPRSAFQSGSPSLSSRSPRQTGHQSPTEALVSRSPRDQQPRSPQVGSPGGSRYARRSNESQRTTGNSPREGGEGLGIRRPVAQHAMTAPVQQVAYDSVTGRNRASPPTSLLDQVRRNRALSNPPITEEERAAQDVALEREYVVVERRHVEVNALADELAANEKLGDASQRSGPITRRYTQQGAPTSTTGAISTPYSRNALATQPRHDRKSSYEKSLSASPGSASSAISKAIQDASLRLFGFKVPPLRASPKGPSPPLYQAFPTYPTPQAPVGLLGDGRNVQGTDEDGKAAQTIEELATRSDCVYGFAEVKYKQLVPLAPSADHILGGLEPEQLVNEEDGLTVEAIVALSEEALVLYVKSLTLLARAMDIASLWWSKKSRGDTGTGLSAAAAQTVVQRINAVVQWVRQRFNEVLEKSEIVRLKLTEAQKQLPDDHPSHPSNHGTESIASSAGSPTKQVYLTPGISAEKLMYDRALEMSRAAAIDEVTNENLSGCEISYITAIRMLEAVLDNDEGSGSETRRLSTGKEAEREAVKEVSGGELDSDEEAHVRKRRLAAVRKKQQMIAEANSKTNLVYQQAVRRRSGDMTPRSVPSHASS | 2.7.11.1 | null | autophagosome assembly [GO:0000045]; axon extension [GO:0048675]; negative regulation of collateral sprouting [GO:0048671]; phosphorylation [GO:0016310]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of autophagy [GO:0010508]; protein transport [GO:0015031]; response to starvation [GO:0042594]; reticulophagy [GO:0061709] | autophagosome [GO:0005776]; cytosol [GO:0005829]; phagophore assembly site membrane [GO:0034045] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF12063;PF21127;PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, APG1/unc-51/ULK1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53104}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P53104}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P53104}; | null | null | null | null | FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes (By similarity). Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome (By similarity). Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production (By similarity). Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates (By similarity). Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9. Catalyzes phosphorylation of ATG4, decreasing the interaction between ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of ATG8 (By similarity). Autophagy is required for proper vegetative growth, asexual/sexual reproduction, and full virulence (PubMed:28894236). Autophagy is particularly involved in the biosynthesis of deoxynivalenol (DON), an important virulence determinant (PubMed:28894236). {ECO:0000250|UniProtKB:P53104, ECO:0000269|PubMed:28894236}. | Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum) |
I1S489 | GRA7_GIBZE | MFPGDMESKASSMNGDQPSSPTPSSSTSVTIPTYTPTSMYDQELQFSRSVAKHVYEAAATLRAAFLCGFQPYTDVASFAHDEIVSQLHYWSSFISFVNDPANNQAFTRMDILEVTRALVQCAEDTVLAGNDIHMIVAHLQIPQSEKGRIIKTFVTANSMLGDQPEVEVSNLVRSSLDGESTVYVIFGGQGNGDGYFAELAELYEVYQPLVGDLVRSASDLFRHLTDKMDVNDCFSEGMELMAWIDKDNDTPIPSRPYLLSSAISFPLITLLQLLHFKISFHYSGCSFKDVQRFLAGVTGHSQGIIAAAAIAAVDSPASFHELSLQAMTVSFSMGVRIHQYYGPQVLPQLITEACLAEGKPIPTPMLSVRGLSIETLATTIQDLNKSLPRTKVQLEVGLRNNDSNYVITGDPMSLRGLCTHFDHKKKALDIVYQFLPAAAPYHNSYLSIAASRAIEDCQEIILRGCDLKMPVFSTVDGSDLRNNEGANLVPDLIRMVCCQVVNWPAALNMPGATHILDFGPGGAQGVGVLANSMKAGQGVRVIHATVLNGLNTELGYKPDLFDRSRKASERVSKPQPWVNSFQPTLTRFTENKLVVSTRFTRLFLQPPIMVAAMTPTTTSWDFVAAVMKAGFHAELACGGFHDRDSLSAAITAIANQVEPGTGITCNVIYSSPTSLRWQIDELEKLVAAGYQIDGLSIGAGVPSVEVVQGYVERLQLQHIALKPGSTEAIERTLKIAKALQPLPVVLQWTGGRGGGHHSNQDFHAPLISMYGKIRAQDNVVLVVGSGFGGPSDTLPYITGKWASDMGLPPMPVDGILLGSRVMVAKEAHTSTEAKHLIVATEGAPDDEWSGTYSRPTGGVLSVISEMRQPIHKIATRAVRLWHELDQTIFHLGPKERVAEITRRRDEIIRRLNHDYHRVWFGCSGPTRDPVELDEMTYSEVLHRFVELAYVTAEHRWVHLSWKKLFSELLTRTMSRLHRTSDSRSETLVDDLDDPYSTLATLTDASAQLITYEDSIYFLQLFRRRGQKPVPFIPVLDADFETWFKKDSLWQSEDIAAVPNHDAQRVCILHGPVAAQYSTKVDEPVGEILGNIHTAWVTAILQTHYQGQSELVPVFDNSPFHASQVESSKTNTELSTPPLNHGLWTLEQWIVHIVQSRDKNLNWAKALLASPRVLCGRRLVPNPFITTLSGLRSMDIHVAETTKTGVGAGFTFFKIPLEETHQDLLDLTLQSNNEISIQISHYPTLQSAPITLTHHMSCQFSKLAMNKSLSDRSAMIRDFYRRIWLGTSHESSHKSIYDKFECEPYTVTADAIRKYNDCTRLPTSMPPTSWATSEVPLDFAVVIAWKALVKPLFSRELEADILKLLHVSNEITLHSDHSPPMVHDVLHTESQVTEVVLQPSGKMVQVEAHVFRGKSCILDLKTRFLLVGNDTHRDHLFRRSILPPSEILLEDEISAMQLVQSSWFQPLRDTSDLVGKRVVFQLEDLMQFHENGQIRCHQITGCAMLDGSIVGNCYLETPDDAYLSLMGNILSQQTGSSSQPAIFETPLLLFEEQEISFTAPTCEQTIAYSAASGDSNPIHVSPVFASLAGLSSPIVHGMHISAEVLQIVYTWLCASSMSRLKKSHVLFAGKVCTGDRLAVSMKHTAMHRGLRVVEVQIHKNMAEELVFVGTYEIEQPLTALVFTGQGSQKKGMGMDLRDKSAAARRIWDTADDHFQHEYGFRITDIVRHDPPSLTVHFGGVHGRRVRSNYMALTYERVASDGQIIEAKLFPTINENTTKYVFSSESGLLSSTQFTQPALGLMELAIMADLEARQLIPSNVTFAGHSLGEYSALMAVGHIMPLEVFISTVFYRGLVMQSTVTYDHHGRSKYAMCAVDPTRVSTDFDGQKLGWLVTQIASEGQWLLEVVNHNVIDSQYVCAGEAIALHCLGVVLDRIHYASKSFFDDGSFDLTDCIRESVKEIRKDRSKVVLSRSKASIPLKGLDVPFHSSHLRSGVDPFRRRLQRSIKLDNASPTKLIGRYIPNLTGKPFEVTRQYFNEVLRLTGSIPIQQALESWDRVASTI | 1.3.1.9; 2.3.1.38; 2.3.1.39; 2.3.1.86; 3.1.2.14; 4.2.1.59 | null | long-chain fatty acid biosynthetic process [GO:0042759] | fatty acid synthase complex [GO:0005835] | (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity [GO:0004317]; [acyl-carrier-protein] S-acetyltransferase activity [GO:0004313]; [acyl-carrier-protein] S-malonyltransferase activity [GO:0004314]; enoyl-[acyl-carrier-protein] reductase (NADH) activity [GO:0004318]; fatty acid synthase activity [GO:0004312]; fatty acyl-[ACP] hydrolase activity [GO:0016297]; fatty-acyl-CoA synthase activity [GO:0004321] | PF00698;PF08354;PF17951;PF17828;PF13452;PF01575;PF16073; | 1.20.1050.120;1.20.930.70;3.30.1120.100;3.30.70.3320;3.30.70.3330;6.10.60.10;3.20.20.70;3.10.129.10;3.40.366.10; | Fungal fatty acid synthetase subunit beta family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+); Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83139; EC=2.3.1.86; Evidence={ECO:0000250|UniProtKB:Q8TGA1}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA; Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479, ChEBI:CHEBI:78446; EC=2.3.1.38; Evidence={ECO:0000250|UniProtKB:Q8TGA1}; CATALYTIC ACTIVITY: Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP]; Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449; EC=2.3.1.39; Evidence={ECO:0000250|UniProtKB:Q8TGA1}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000250|UniProtKB:Q8TGA1}; CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9; Evidence={ECO:0000250|UniProtKB:Q8TGA1}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) + holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14; Evidence={ECO:0000250|UniProtKB:Q8TGA1}; | null | PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:30395461}. | null | null | FUNCTION: Fatty acid synthase subunit beta; part of the gene cluster that mediates the biosynthesis of gramillins A and B, bicyclic lipopeptides that induce cell death in maize leaves but not in wheat leaves (PubMed:30395461). The nonribosomal peptide synthetase GRA1 incorporates respectively a glutamic adic (Glu), a leucine (Leu), a serine (Ser), a hydroxyglutamine (HOGln), a 2-amino decanoic acid, and 2 cysteins (CysB and CysA) (Probable). The biosynthesis of 2-amino decanoic acid incorporated in gramillins could be initiated by a fatty acid synthase composed of the alpha and beta subunits FGSG_00036 and FGSG_11656 (Probable). The cytochrome P450 monooxygenase FGSG_15680 could hydroxylate the fatty acid chain (Probable). Subsequent oxidation to the ketone by the oxidoreductase FGSG_00048 and transamination by aminotransferase FGSG_00049 could form 2-amino-decanoic acid (Probable). On the other hand, FGSG_15680 could also be responsible for the HO-modified glutamine at the gamma-position (Probable). Whether hydroxylation occurs on the fully assembled product or on the Gln residue prior to assembly into the gramillins requires further proof (Probable). The thioredoxin FGSG_00043 could also be required for the disulfide-bond formation between CysA and CysB (Probable). The specific involvement of the remaining proteins from the cluster is more difficult to discern, but could have broader regulatory (FGSG_00040 and FGSG_11657) or enzymatic functions (FGSG_00044 and FGSG_00045) (Probable). The final C-domain of GRA1 does not possess the expected sequence of a termination CT domain, often implicated in macrocyclization and release of a cyclopeptidein fungal NRPs; and the thioesterase FGSG_00047 may act in concert with the terminal C-domain of GRA1 to catalyze the formation of the macrocyclic anhydride and release of the products (Probable). {ECO:0000269|PubMed:30395461, ECO:0000305|PubMed:30395461}. | Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum) |
I1S9X9 | ATG9_GIBZE | MASNIFSRIKSPSGGSQSFYQQLRSGEDPEYDPGLDEENLGHRFDDFQAEGMDIGDSSMTVESVAPGSKGKGKATFRPTAHARSSGITSPRWQQDDDGDNEVPASLLMEPKDLDPPASPPNKRATNPGSSRTPASVGPSSARTRAQWEAATAQQQLHQDHPYTTPMGPQPIPVARGTMSNNPREKALWRWVNTSNLDSFMRDVYDYFEGGGLWCILCANALWLFQCIDYSRVPDSRSLHEVIVPQCTRKMSGLWNFAIWLYTFFFIWKCVQYFVEIRRLTYIRDFYIYLLDIPEQDMQTISWQDVVARIMALREENPKTATNISPRLRQFMGSQSKERLDALDIANRLMRKENYLIAMINKDILDLSLPVPFLRGRQMFSKTMEWYLQYCILDMAFNELGQVQQDFLRPDRRRLLSQKLRQRFLFAGFLNLLFAPVVLAYVVIVYFFTYYYEYQKDPKQAAARKYTSLAEWKFRQFNELPHIFYERLHMSYPFATRYIDQFPKRITEAVARTIAFMSGAITAILAIGSVLDSELFLNFEITKDRPVIFYLGVFAAIWATTRGMVSEETLVFNPEYALRNVIEYTRYVPDHWKNKLHSSEVKQEFSELYKMKVVIFLEEMMGIVTTPMLLLFSLPRCSDQIVDFFREFTIHVDGLGYVCSFAVFDFQKGPGNTGPQGPRPDVREDYYSTKHGKMAASYYGFLDNYAANPKTGIPGHLPPGPKPSFHPPPSFPGIGSPTLAADMQGSHIGRTGTETGRARSRAPGGRGPRIGVMPQPSPMASMLLDQHHQPPGGNMVARSLHASRYPRGYRGESQIIEETEASSIRRNGEDDELYEPGGALGESVWETSPARGVTRENSAANTEDPEAGVLGLIYQLQQTQRPRRGGGMV | null | null | lipid droplet disassembly [GO:1905691]; lipid transport [GO:0006869]; macroautophagy [GO:0016236]; protein localization to phagophore assembly site [GO:0034497] | autophagosome membrane [GO:0000421]; cytoplasmic vesicle membrane [GO:0030659]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; phagophore assembly site membrane [GO:0034045]; vacuolar membrane [GO:0005774] | guanyl-nucleotide exchange factor activity [GO:0005085] | PF04109; | null | ATG9 family | PTM: Phosphorylated by ATG1 (By similarity). ATG1 phosphorylation is required for ATG18 interaction and preautophagosome elongation (By similarity). {ECO:0000250|UniProtKB:Q12142}. | SUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12142}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12142}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12142}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12142}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:Q12142}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663, ChEBI:CHEBI:57262; Evidence={ECO:0000250|UniProtKB:Q12142}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895, ChEBI:CHEBI:64612; Evidence={ECO:0000250|UniProtKB:Q12142}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)(out); Xref=Rhea:RHEA:67920, ChEBI:CHEBI:58088; Evidence={ECO:0000250|UniProtKB:Q12142}; | null | null | null | null | FUNCTION: Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Required for mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking (By similarity). Autophagy is required for proper vegetative growth, asexual/sexual reproduction, and full virulence (PubMed:28894236, PubMed:30044782). Autophagy is particularly involved in the biosynthesis of deoxynivalenol (DON), an important virulence determinant (PubMed:28894236). Required for aerial hyphae development and lipid droplet degradation in response to starvation (PubMed:30044782). {ECO:0000250|UniProtKB:Q12142, ECO:0000269|PubMed:28894236, ECO:0000269|PubMed:30044782}. | Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum) |
I1SB12 | MNCO_MICNN | MRSAFILALGLITASADALVTRGAIEACLSAAGVPIDIPGTADYERDVEPFNIRLPYIPTAIAQTQTTAHIQSAVQCAKKLNLKVSAKSGGHSYASFGFGGENGHLMVQLDRMIDVISYNDKTGIAHVEPGARLGHLATVLNDKYGRAISHGTCPGVGISGHFAHGGFGFSSHMHGLAVDSVVGVTVVLADGRIVEASATENADLFWGIKGAGSNFGIVAVWKLATFPAPKVLTRFGVTLNWKNKTSALKGIEAVEDYARWVAPREVNFRIGDYGAGNPGIEGLYYGTPEQWRAAFQPLLDTLPAGYVVNPTTSLNWIESVLSYSNFDHVDFITPQPVENFYAKSLTLKSIKGDAVKNFVDYYFDVSNKVKDRFWFYQLDVHGGKNSQVTKVTNAETAYPHRDKLWLIQFYDRYDNNQTYPETSFKFLDGWVNSVTKALPKSDWGMYINYADPRMDRDYATKVYYGENLARLQKLKAKFDPTDRFYYPQAVRPVK | 1.1.3.-; 1.1.3.5 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:17154316}; Note=Binds 1 FAD per subunit in a bicovalent manner. {ECO:0000269|Ref.6}; | null | extracellular region [GO:0005576] | FAD binding [GO:0071949]; glucose oxidase activity [GO:0046562]; metal ion binding [GO:0046872] | PF08031;PF01565; | 3.30.465.10;3.40.462.20; | Oxygen-dependent FAD-linked oxidoreductase family | PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-N1-histidyl FAD linkage. {ECO:0000269|Ref.6}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11179980}. | CATALYTIC ACTIVITY: Reaction=beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2; Xref=Rhea:RHEA:11428, ChEBI:CHEBI:15379, ChEBI:CHEBI:15903, ChEBI:CHEBI:16217, ChEBI:CHEBI:16240; EC=1.1.3.5; Evidence={ECO:0000269|PubMed:11179980}; CATALYTIC ACTIVITY: Reaction=D-galactose + O2 = D-galactono-1,5-lactone + H2O2; Xref=Rhea:RHEA:59312, ChEBI:CHEBI:4139, ChEBI:CHEBI:15379, ChEBI:CHEBI:15945, ChEBI:CHEBI:16240; EC=1.1.3.5; Evidence={ECO:0000269|PubMed:11179980}; CATALYTIC ACTIVITY: Reaction=D-cellobiose + O2 = D-cellobiono-1,5-lactone + H2O2; Xref=Rhea:RHEA:59316, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17057, ChEBI:CHEBI:17863; EC=1.1.3.5; Evidence={ECO:0000269|PubMed:11179980, ECO:0000269|Ref.3}; CATALYTIC ACTIVITY: Reaction=beta-lactose + O2 = H2O2 + lactobiono-1,5-lactone; Xref=Rhea:RHEA:59352, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:36218, ChEBI:CHEBI:143068; EC=1.1.3.5; Evidence={ECO:0000269|PubMed:11179980}; CATALYTIC ACTIVITY: Reaction=D-maltose + O2 = D-maltobiono-1,5-lactone + H2O2; Xref=Rhea:RHEA:59344, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17306, ChEBI:CHEBI:143029; EC=1.1.3.5; Evidence={ECO:0000269|PubMed:11179980, ECO:0000269|Ref.3}; CATALYTIC ACTIVITY: Reaction=D-xylose + O2 = D-xylono-1,5-lactone + H2O2; Xref=Rhea:RHEA:59324, ChEBI:CHEBI:15379, ChEBI:CHEBI:15867, ChEBI:CHEBI:16240, ChEBI:CHEBI:53455; Evidence={ECO:0000269|PubMed:11179980}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.97 mM for oxygen {ECO:0000269|PubMed:17154316}; KM=19 mM for cellobiose (at pH 6 and 30 degrees Celsius) {ECO:0000269|PubMed:11179980}; KM=59 mM for cellobiose (at pH 6 and 40 degrees Celsius) {ECO:0000269|PubMed:11179980}; KM=51 uM for cellobiose (at pH 7.2 and 25 degrees Celsius) {ECO:0000269|Ref.3}; KM=59 uM for cellotriose (at pH 7.2 and 25 degrees Celsius) {ECO:0000269|Ref.3}; KM=66 uM for cellotetraose (at pH 7.2 and 25 degrees Celsius) {ECO:0000269|Ref.3}; KM=42 mM for glucose (at pH 6 and 40 degrees Celsius) {ECO:0000269|PubMed:11179980}; KM=11 mM for maltose (at pH 6 and 40 degrees Celsius) {ECO:0000269|PubMed:11179980}; KM=12 mM for maltose (at pH 7.2 and 25 degrees Celsius) {ECO:0000269|Ref.3}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5-7. {ECO:0000269|PubMed:11179980}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:11179980}; | FUNCTION: Catalyzes the selective oxidation of C1 hydroxyl moieties on mono-, oligo- and polysaccharides with concomitant reduction of molecular oxygen to hydrogen peroxide. This results in the formation of the corresponding lactones, which typically undergo spontaneous hydrolysis. Carbohydrate oxidase is able to oxidize a variety of substrates including D-glucose, D-galactose, D-xylose, D-maltose, D-cellobiose, and lactose. In addition, among various oligosaccharides, the enzyme preferred tetrameric dextrins, indicating a favorable interaction of four linked glucose units with the substrate binding pocket. {ECO:0000269|PubMed:11179980, ECO:0000269|Ref.2, ECO:0000269|Ref.3}. | Microdochium nivale (Pink snow mold) (Lanosa nivalis) |
I1TEM1 | T3O_CATRO | MEFHESSPFVFITRGFIFIAISIAVLRRIISKKTKTLPPGPWKLPLIGNLHQFLGSVPYQILRDLAQKNGPLMHLQLGEVSAIVAASPQMAKEITKTLDLQFADRPVIQALRIVTYDYLDISFNAYGKYWRQLRKIFVQELLTSKRVRSFCSIREDEFSNLVKTINSANGKSINLSKLMTSCTNSIINKVAFGKVRYEREVFIDLINQILALAGGFKLVDLFPSYKILHVLEGTERKLWEIRGKIDKILDKVIDEHRENSSRTGKGNGCNGQEDIVDILLRIEEGGDLDLDIPFGNNNIKALLFDIIAGGTETSSTAVDWAMSEMMRNPHVMSKAQKEIREAFNGKEKIEENDIQNLKYLKLVIQETLRLHPPAPLLMRQCREKCEIGGYHIPVGTKAFINVWAIGRDPAYWPNPESFIPERFDDNTYEFTKSEHHAFEYLPFGAGRRMCPGISFGLANVELPLALLLYHFNWQLPDGSTTLDMTEATGLAARRKYDLQLIATSYA | 1.14.14.50 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | indole alkaloid biosynthetic process [GO:0035835] | endoplasmic reticulum membrane [GO:0005789] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25850027}; Single-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=16-methoxytabersonine + O2 + reduced [NADPH--hemoprotein reductase] = (3R)-1,2-didehydro-3-hydroxy-16-methoxy-2,3-dihydrotabersonine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52480, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58930, ChEBI:CHEBI:136640; EC=1.14.14.50; Evidence={ECO:0000269|PubMed:25918424}; CATALYTIC ACTIVITY: Reaction=(-)-tabersonine + O2 + reduced [NADPH--hemoprotein reductase] = (3R)-1,2-didehydro-3-hydroxy-2,3-dihydrotabersonine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55024, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:57893, ChEBI:CHEBI:58210, ChEBI:CHEBI:138462; EC=1.14.14.50; Evidence={ECO:0000269|PubMed:25918424}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.1 uM for tabersonine {ECO:0000269|PubMed:25918424}; Note=The KM is mesured in the presence of a saturating amount of tabersonine 3-reductase, the enzyme converting the unstable intermediate produced by the reaction. {ECO:0000269|PubMed:25918424}; | PATHWAY: Alkaloid biosynthesis; vindoline biosynthesis. | null | null | FUNCTION: Cytochrome P450 catalyzing the monooxygenation of 16-methoxytabersonine, 16-hydroxytabersonine and tabersonine, but not of 2,3-dihydrotabersonine (PubMed:25918424). Converts the C2,C3 alkene of tabersonine and 16-methoxytabersonine to the epoxides, which then spontaneously open to form the corresponding imine alcohols (PubMed:25850027). Inactive in converting amyrin to ursolic acid (PubMed:22837051). {ECO:0000269|PubMed:22837051, ECO:0000269|PubMed:25850027, ECO:0000269|PubMed:25918424}. | Catharanthus roseus (Madagascar periwinkle) (Vinca rosea) |
I1WVY3 | CDIA2_BURP2 | MNKNRYRVVFNRARGALMVVQENGRASHGSGSRDARAGVVPAWLSLSPFALRHVALAVLVAAGVVPIWVNAQVVAGGAHAPSVIQTQNGLQQVNINRPGASGVSMNTYNQFDVPKPGIILNNSPINVQTQLGGIIGGNPNFQAGDAARLIVNQVNSNNPSFIRGKVEIGGAAAQLVIANQAGLVVDGGGFLNTSRATLTTGNPNFGPDGSLTGFNVNQGLISVVGAGLDTANVDQVDLLARAVQINAKAYAKTLNVVAGSNQVDYNTLNATPIAANGPAPTIAIDVSQLGGMYANRVFLVSSENGVGVANAGDIAAQAGDLTLQANGRLVLSGHTNAAGNMSLSASGGIQNSGVTYGKQSVTITTGADLTNSGALTAQQNLTANVGSLNSTGTLGAGINVDSTVGTSGDLNVTSSGQLTATGTNSAAGNATFTGSGVNLSNSATAANGNLALTATAGDVNLAGSTVSAKGAVNAQASGTVVNDRGNLSSGAGMTLGGGSLSNQGGRANSQGPLSVQMAGTVSNQNGMLSSQSTADVRGSAIQNNAGLIQSAGKQTIAGASIDNSAGRLISLNADGLSVTATGALTNAAGANVSGDPGGVIGGKGDVTVQGNTVTNSGSMSADATLHVIGQSVDNGNGALHAGQTTTVDAGNHLSNAGGRVEGQSAVLNGATLDNSQGTVNAATVSLNGTTLLNHGGTVTQTGTGPMTVAITDTLDNSNNGLIQTRSTDLSLTSTTLINDNGGTITHVGPGTLTVGNGSGTVSNKAGAIASNGRTVLQGKTIDNSAGSASGQTGLSVNAADSITNLGGKLTSNANVDVTAGGALVNDGGELGSKTAATTIHSASLSNLNGKIVSPTLTATVAGLLDNSQNGDFEANQLALTAANLKNQGGHISQWQSGPTTLAVSGTLDNSNGGVIQTNSTDLTLAPAVLDNSKGTITHGGTGTLTLTPGNGAGALQNTGGTIGTNGQAIVKAGSLDNGSGVIAAKLGLSATIAGAMNNTQGLMRSNAALSIISNGALSNHQGHIEAGTPGDTSTLSIQAASIDNTDGAVHDFGTGKMTVQGGSQIVNSHAGGVDGMGQMTGQGDVTIGAASISNTQGGQLMGANLLIQGATLDNSGGQVGNVANATGDVNVAMSGAVTNTNGSITSTRDLSVAASTLLGGGAYSAARDAAINLQGDFTTTPQTQFNIGRDLTFTLPGTFANSANLQSVHNLTVNAGNIVNTGAMTAGSLLSTHSGDLTNYGAMVGGSVAIQASGTVSNLGPVALIGASDTSGLLEIVAHDIENRDDTTLGDSMPTTTIFGLGKVALAGGKDANGNYTNAALINNSSAAIQSGASMELHADKVTNTRRVMQTSGNTSQVDPALLQQLGISMSGCAAYYIAACSGQDVHWINLFHDPNYPDYDPAPIIAALKLQPGGVFTVPPNGGQWNSGYQYTTYEGKATANTVTKLSPGAQIASGGDLDASTVKTFQNYWSSVTAAGNIKQPASLDMDGWGATGQQAPGVTVVYSGYYHYNNYDNSEHNWTLPFGDKPFVGGPGGYTQAAPADVRQYSLPDYRSTWGANGTISGNGVSVNNTAANATIPSLGLLPGQAVPGLTIGTVSGNASGTQSGAAAIKGGTPTWVDPVIASATAVNVLSNLTIPQGGLYRPNSAPNPTYLIETNPAFTRMNNFLSSDYYLNQIGVNPLTTEKRLGDGFYEQQLVRNQVTQLTGKAVLGPYTDLQGMYQSLMLAGAEWSKSLNLPLGMSLSAQQVAALTTNVIIMQTETVGGQQVLVPVVYLAKADQQNANGPLITAGNIDLKNTQVFTNSGTVKADTTLALQGKQIDNAFGALQSGGLTSLDTTGNVDLTSANVKAGSLDLNAGNKLILDTATQTTHQVSRDGATSDKTTLGPAANLNVAGDASIKTGGDFQQNAGNLNVGGNLNANIGGNWNLGVQQTGEHKVVQRANGVSDTDLNSATGSTVNVGGKSAIGVGGDLTAQGARLDFGQGGTVAAKGNVTFGAASTTSTINANSSGDQGNRSYAETRHGSDQALTGTTVKGGDTLNVVSGKDINVIGSTIDLKKGDANLLAAGDVNVGAVTERHVYNSRETHSRSGVVSGTKIASSQDATSTVANGSLISADGVSIGSGKDINVQGSTVVGTHDVALNAAHDVNITTSQDTSQSSTTYQEQHSGLMSGGGLSFSVGNSKLAQQNQSSSVTNNASTVGSVDGNLTVNAGNTLHVKGSDLVAGKDVTGTAANIVVDSATDTTRQAQQQQTSKSGLTVGLSGSVGDAINNAISETQAARESAKDSNGRASALHSIAAAGDVAFGGLGAKALLDGAKGPQAPSIGVQVSVGSSHSSMQSSEDQTIQRGSSINAGGNAKLIATGNGTPKDGNITIAGSNVNAANVALIANNQVNLVNTTDTDKTQSSNSSSGSSVGVSIGTNGIGVSASMQRAHGDGNSDAAIQNNTHINASQTATIVSGGDTNVIGANVNANKVVADVGGNLNVASVQDTTVSAAHQSSAGGGFTISQTGGGASFSAQNGHADGNYAGVNEQAGIQAGSGGFDVTVKGNTDLKGAYIASTADASKNSLTTGTLTTSDIENHSHYSANSAGFSAGASVGVSTKAVGPSSVSGSGGVTPMVFQNDSGDQSATTKSAVSAGAINITKPGEQTQDVANLNRDATNLNGTVSKTPDVQKMLSQQADTMNAAQAAGQTVSQGIGLYADGKRKDAIDAAKAAYERGDLVAMQSYIDQAKSWDEGGASRAGLQATGGALIGGLGGGSVLTAIGGAAGAGTSSLLAGQAEKISKSVGDMTGSSLVGNIAANVAATVGGALVGGSAGAAMASNVELYNAGNDPQKTDDRATIAGLQGLLNQAVAAGAKGLSTIANARNAIGNAISGALDSAADQFGTLMKRDAEGKMSQSPAELVSQGVANGINTVLGSKGGEPPLAGPSAVAVDSLTGQAANAALGATDRTPPSNAILSNSNSDNNSTQGSQSGTVTKTPNPEATGSLSGKPTQIPPLSDEVTTRSLIRENQSAVTLANKGYDVVQNPEVLGPKNPDYTINGQVFDNYAPATGNVRNIATTISNKVSSGQASNIVVNLADSSASPAAIEAQINSYPIPGLGKVIVIDKLGNITIIKPKGN | 3.1.-.- | null | null | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; membrane [GO:0016020] | RNA endonuclease activity [GO:0004521]; toxin activity [GO:0090729]; tRNA binding [GO:0000049]; tRNA-specific ribonuclease activity [GO:0004549] | PF18451;PF13018;PF05594;PF13332;PF05860; | 3.40.1350.120;2.160.20.10; | CdiA toxin family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Secreted {ECO:0000305|PubMed:25174572}. Target cell, target cell cytoplasm {ECO:0000305|PubMed:25174572}. Note=Secreted to the cell surface by CdiB, its two partner secretion pathway (TPS) partner (Probable). Probably translocated into the target cell cytoplasm as intracellular CdiI inhibits tRNase activity. Toxin translocation into the target cell depends on the proton motive force (pmf) of the target cell, but not on tolA or tonB. The pmf is probably required for translocation across the target cell inner membrane from its periplasm. {ECO:0000269|PubMed:25174572, ECO:0000305}. | null | null | null | null | null | FUNCTION: Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion. The C-terminal 301 residues (the CT fragment) cleaves near the C-terminus of E.coli tRNA1B(Ala), probably preventing tRNA charging, and inhibits growth in E.coli. A truncated CT fragment (residues 2948-3122) has tRNA endonuclease activity on several B.thailandensis tRNAs as well as tRNA2(Arg) where it cleaves after A-70 and U-71 (PubMed:22435733, PubMed:25174572). Inactive CT domain binds tRNA, probably in a 1:1 complex (PubMed:27445337). Toxic activity is neutralized by coexpression of the cognate immunity protein CdiI in E.coli, but not by non-cognate immunity proteins from other strains of B.pseudomallei (PubMed:22435733, PubMed:23236156). May use lipopolysaccharide as its target cell receptor (PubMed:25786241). Probably gains access to the cytoplasm of target cells (B.thailandensis strain E264) by using integral inner membrane protein BTH_II0599 (PubMed:25786241, PubMed:26305955). Protein BTH_I0359 is also implicated in an unknown fashion in CDI in B.thailandensis strain E264 (PubMed:25786241). {ECO:0000269|PubMed:22435733, ECO:0000269|PubMed:23236156, ECO:0000269|PubMed:25174572, ECO:0000269|PubMed:25786241, ECO:0000269|PubMed:26305955, ECO:0000269|PubMed:27445337}.; FUNCTION: Expression of this cdiAIB locus in B.thailandensis confers protection against other bacteria carrying the locus; growth inhibition requires cellular contact. {ECO:0000269|PubMed:22435733}.; FUNCTION: The CdiA protein is thought to be exported from the cell through the central lumen of CdiB, the other half of its two-partner system (TPS). The TPS domain probably remains associated with CdiB while the FHA-1 domain forms an extended filament with the receptor-binding domain (RBD) at its extremity; in the secretion arrested state the C-terminus of the RBD domain form a hairpin-like structure as the FHA-2, PT and CT domains are periplasmic. Upon binding to a target cell outer membrane receptor (possibly a lipoprotein in this CDI) a signal is transmitted to activate secretion. The filament elongates slightly, the rest of CdiA is secreted and the FHA-2 domain becomes stably associated with the target cell's outer membrane where it facilitates entry of the toxic CT domain into the target cell periplasm. From there the toxic CT domain is cleaved and gains access to the target cell cytoplasm via an inner membrane protein (probably inner membrane protein BTH_II0599). {ECO:0000250|UniProtKB:A0A1S4NYE3, ECO:0000305|PubMed:25786241, ECO:0000305|PubMed:26305955}. | Burkholderia pseudomallei (strain 1026b) |
I1Z695 | EREC2_ORYSJ | MTTTTTTRLLLAAILLAVAAADDDGQTLLEIKKSFRNVDNVLYDWAGDGAPRRYCSWRGVLCDNVTFAVAALNLSGLNLGGEISPAIGNLKSVESIDLKSNELSGQIPDEIGDCTSLKTLDLSSNNLGGDIPFSISKLKHLENLILKNNQLVGMIPSTLSQLPNLKILDLAQNKLNGEIPRLIYWNEVLQYLGLRSNNLEGSLSPEMCQLTGLWYFDVKNNSLTGIIPDTIGNCTSFQVLDLSYNRLTGEIPFNIGFLQVATLSLQGNNFSGPIPSVIGLMQALAVLDLSFNQLSGPIPSILGNLTYTEKLYLQGNRLTGSIPPELGNMSTLHYLELNDNQLTGFIPPELGKLTGLFDLNLANNNLEGPIPDNISSCMNLISFNAYGNKLNGTVPRSLHKLESITYLNLSSNYLSGAIPIELAKMKNLDTLDLSCNMVAGPIPSAIGSLEHLLRLNFSNNNLVGYIPAEFGNLRSIMEIDLSSNHLGGLIPQEVGMLQNLILLKLESNNITGDVSSLINCFSLNVLNVSYNNLAGIVPTDNNFSRFSPDSFLGNPGLCGYWLGSSCYSTSHVQRSSVSRSAILGIAVAGLVILLMILAAACWPHWAQVPKDVSLCKPDIHALPSSNVPPKLVILHMNMAFLVYEDIMRMTENLSEKYIIGYGASSTVYKCVLKNCKPVAIKKLYAHYPQSLKEFETELETVGSIKHRNLVSLQGYSLSPAGNLLFYDYLENGSLWDVLHAGSSKKQKLDWEARLRIALGAAQGLAYLHHDCNPRIIHRDVKSKNILLDKDYEAHLADFGIAKSLCTSKTHTSTYVMGTIGYIDPEYACTSRLNEKSDVYSYGIVLLELLTGKKPVDNECNLHHLILSKAADNTVMEMVDPDIADTCKDLGEVKKVFQLALLCSKRQPSDRPTMHEVVRVLDCLVYPDPPSKPALPPALPQSSTVPSYVNEYVSLRGGSTLSCENSSSASDAELFLKFGEVISQNTE | 2.7.11.1 | null | heat acclimation [GO:0010286]; phosphorylation [GO:0016310]; regulation of cell growth [GO:0001558] | membrane [GO:0016020]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; receptor serine/threonine kinase binding [GO:0033612] | PF00560;PF13855;PF08263;PF00069; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000305|PubMed:29692796}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000305|PubMed:29692796}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000305|PubMed:29692796}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000305|PubMed:29692796}; | null | null | null | null | FUNCTION: Receptor kinase that may be involved in the regulation of cell proliferation and cell growth. {ECO:0000269|PubMed:29692796}. | Oryza sativa subsp. japonica (Rice) |
I2C090 | VCO3_OPHHA | MEGMALYLVAALLIGFPGSSHGALYTLITPGVLRTDTEEQILVEAHGDNTPKQLDIFVHDFPRKQKILFQKRVDMNPAGDMLVTPTIKIPAEEVSKDSRQNQYVVVQVTGPQVRLEKVVLLSYQSGFVFIQTDKGIYTPGSPVLYRVFSMDHNMRQMDKTVVVEFQTPEGIVVSSNRIDLNFTRPYNLPELGSLGTWKIVAKYEHSPENYTAYFDVRKYVLPSFEVHLQPSEKSFYIDGNENFHVSITARYLYGEEVEGVAFVLFGVKIDGAKKSIPDSLTRIPILDGDGEATLKRDTLRSRFPNLNELVGHTLYASVTVITESGSDMVATEQSGIHIVTSPYQIYFTKTPKYFKPGMPYELTVYVTNPDGSPAAKVPVVSEAIHSEGTTLSDGTAKLILNTPLDTQSLLITVRTNHGDLPRERQATKSMTATAYQTQGGSGNYLHVAITSTEIKPGDNLPVNFNVRGNANSLNQVKYFTYLVGRQPKGAGQNLVAMNLRITPDLIPSFRFVAYYQVGNNEIVADSVWVDVKDTCMGTLVVKGASLTDNQIHMPGAAMKIKLEGDPGAQVGLVAVDKAVYVLNDKYKISQAKIWDTIEKSDFGCTAGGGQNNLGVFEDAGLALTTSTNLNTKQRSDTKCPQPANRRRRSSVLLLDSKASKAAQFQDQDLRKCCEDSMHENPMGYTCEKRAKYIQEGDACKAAFLECCRYIKGILDENQWESGLFLPRNDNEDGFIQDSDIIPRTDFPKSWLWHTVQLTEQPNSNGISSKTMSIYLKESITTWEVLAVSFTPTKGICVAEPYEIKVMKDFFIDLRVPYSVVRKEQVEIRAVLYNYAGRDIYVRVELLYNPAFCSASTEEQRYRQQFTIKALSSRAVPFVIVPLQQGLHDIEVRASVQGWESVSDGVKKKLKVVPEGVQKCIVTIIKLDPRAKGVDGTQREVVKARKLDDKVPDTEIETKITIQADPVAQIIENSIDGSKLNHLIITPSGCGEQNMIRMTAPVIATYYLDTTEQWETLGRNHRNEAVKQIMTGYAQQMVYKKANHSYAAFTNRASSTWLTAYVVKVFAMATKMVAGISHEIICGGVRWLILNRQQPDGAFKENAPVLSGTMQGGIQGDESEVTVTAFTLVALLESKTICNDSVNSLDSSIKKATDYLLKKYEKLQRPYTTALTAYALAAADRLNDDRVLMAASTGKNRWEEYNAHTHNVEGTSYALLALLKMKKFDQTGPIVRWLTDQNFYGGTYGQTQATVMLFQALAEYKIQMPTHKDLNLDIIIKLPERELPLHYRLDATNAILARTAETKLNQDFTVSASGDGTATMTILTVYNAQLQEKANVCNKFHLDVSVENIHLNFKHAKGAKGALMLKICMRYLGEVDSTMTIIDISMLTGFLPDAEDLTRLSEGVDRYISRYEVDNNMAQKVAVIIYLDKVSHSEDECLQFKILKHFEVGFIQPGSVKVYSYYNLDEQCTKFYHPDKGTGLLNKICVGNICRCAAETCSLLSQQEKIDLPLRIQKACASNVDYVYKTKLLRIEEKDGYDIYVMDVLEVIKPGTDENPQANARQYISQRKCQEALNLNVNDDYLIWGLRSDLWPMKDKFSYLITKNTWIERWPHEDECQDEEFQNLCLDFAHLSNILTIFGCPT | null | null | complement activation [GO:0006956]; inflammatory response [GO:0006954] | extracellular space [GO:0005615] | endopeptidase inhibitor activity [GO:0004866]; metal ion binding [GO:0046872]; toxin activity [GO:0090729] | PF00207;PF07703;PF07677;PF01821;PF21406;PF21308;PF17790;PF01835;PF17791;PF17789;PF01759;PF07678; | 1.50.10.20;2.20.130.20;2.40.50.120;2.60.120.1540;2.60.40.1930;2.60.40.1940;6.20.50.160;2.60.40.690;1.20.91.20;2.60.40.10; | Venom complement C3 homolog family | PTM: First processed by the removal of 4 Arg residues by furin-type protease, forming two chains, alpha and gamma/beta precursor, linked by a disulfide bond. Probably, a cobrin-like protease cleaves the C3a-like domain and then the C3d-like domain, generating the mature venom factor (OVF) (By similarity). {ECO:0000250}.; PTM: The beta chain is not glycosylated. {ECO:0000269|PubMed:22561424}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Complement-activating protein in cobra venom. It is a structural and functional analog of complement component C3b, the activated form of C3. It binds factor B (CFB), which is subsequently cleaved by factor D (CFD) to form the bimolecular complex OVF/Bb. OVF/Bb is a C3/C5 convertase that cleaves both complement components C3 and C5. Structurally, it resembles the C3b degradation product C3c, which is not able to form a C3/C5 convertase. Unlike C3b/Bb, OVF/Bb is a stable complex and completely resistant to the actions of complement regulatory factors H (CFH) and I (CFI). Therefore, OVF continuously activates complement (By similarity). As a result, OVF exhibits complement-depleting activity. {ECO:0000250, ECO:0000269|PubMed:22561424}. | Ophiophagus hannah (King cobra) (Naja hannah) |
I2CYZ4 | D4FAD_CHLRE | MNATMQRSAVAGRTSGKVATTARASSMARPRLPIAGRVARRSAVTVRAVAEPVVVDKAVEAPAKPVPSGGDPWEDEKWTKYKWTVYRGVAYDLTPYLDRHPGGRWLLNLAIGRDATALFESYHLRPEVAASMLKRLPVLADFPVDAVPPSPRPNDSELYNAIRERVRKEVFKGTEIKGAHRSGSEGAAFAVLGYAAAMYALYTYDANPLTGALLGLGGAWIGLTIQHCGNHGAMSTNPVVNNLMGLTNDLAGGSSLMWRYHHQVSHHIHCNDDALDEDVFSAFPMLRFDDRLPKAWYHQFQHVYMWALFPFLQLVFQIGDWQALLTNRTVGATLYGASNFERQTLIAGKLAHYFLLYGLPAFLHGPTAMLGGAAGYLFTQSIVLAATFAVSHNVPETKPLDPGPTRENLDESAVTRDWGVQQVLTSANWGGVIGNFFTGGLNLQIEHHLFPAISFMHYPAISKIVADECKQRGIPYSHYDTLPEILGRFVRYMKEVGAAPQKPVKRDGEMLMLSKF | 1.14.19.31 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:O00767}; | long-chain fatty acid biosynthetic process [GO:0042759]; unsaturated fatty acid biosynthetic process [GO:0006636] | chloroplast [GO:0009507]; chloroplast membrane [GO:0031969] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water [GO:0016717] | PF00173;PF00487; | 3.10.120.10; | Fatty acid desaturase type 1 family | null | SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305|PubMed:22562471}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a (7Z,10Z,13Z,16Z,19Z)-docosapentaenoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46252, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:88266, ChEBI:CHEBI:88267; EC=1.14.19.31; Evidence={ECO:0000305|PubMed:22562471}; CATALYTIC ACTIVITY: Reaction=a (7Z,10Z,13Z,16Z)-docosatetraenoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (4Z,7Z,10Z,13Z,16Z)-docosapentaenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46256, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:88264, ChEBI:CHEBI:88265; EC=1.14.19.31; Evidence={ECO:0000305|PubMed:22562471}; | null | null | null | null | FUNCTION: Fatty acid desaturase that introduces a cis double bond at the 4-position in 16-carbon polyunsaturated fatty acids that contain a Delta(7) double bond, resulting in the production of 16 carbon fatty acid (7Z,10Z,13Z)-hexadeca-7,10,13-trienoate. {ECO:0000269|PubMed:22562471}. | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
I2DBY1 | DYP_AURAJ | MRLSPVFVALLSGLLAADLGLARSVAPRVADSPAAVTGTRKTSLLKNVAGLPPVPSAAQVAATSLNTDDIQGDILVGMHKQKQLFYFFAINDPATFKTHLASDIAPVVASVTQLSNVATQPLVALNIAFSNTGLLALGVTDNLGDSLFANGQAKDATSFKESTSSWVPQFAGTGIHGVIILASDTTDLIDQQVASIESTFGSSISKLYSLSASIRPGNEAGHEMFGFLDGIAQPAINGFNTPLPGQNIVDAGVIITGATNDPITRPSWAVGGSFLAFRQLEQLVPEFNKYLLDNAPAGSGSLQARADLLGARMVGRWKSGAPIDLTPTADDPALGADAQRNNNFTYSHAGFDLGSDQSHCPFSAHIRKTRPRADLGGSLTPPNLSAGANSIMRSGIPYGPEVTSAESASNTTTQERGLAFVAYQAQLSQGFHFLQQTWADNANFPPGKTPATVGLDPIIGQNNGQPRVVNGLLPSNSSASLSIPQFVVSHGGEYFFSPPISAIGGRLSA | 1.11.1.19; 1.11.1.7 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:23235158, ECO:0000269|PubMed:25495127, ECO:0000269|PubMed:25542606, ECO:0000269|Ref.7}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently. {ECO:0000269|PubMed:23235158, ECO:0000269|PubMed:25495127, ECO:0000269|PubMed:25542606, ECO:0000269|Ref.7}; | null | cytosol [GO:0005829]; extracellular region [GO:0005576] | heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601] | PF21105;PF20628; | null | DyP-type peroxidase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23111597}. | CATALYTIC ACTIVITY: Reaction=2 H2O2 + Reactive Blue 5 = 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H(+) + 2 H2O + phthalate; Xref=Rhea:RHEA:28086, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:17563, ChEBI:CHEBI:63950, ChEBI:CHEBI:63955, ChEBI:CHEBI:64278; EC=1.11.1.19; Evidence={ECO:0000269|PubMed:19756587, ECO:0000269|PubMed:23111597, ECO:0000269|PubMed:25153532, ECO:0000269|PubMed:25495127, ECO:0000269|PubMed:25542606}; CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; Evidence={ECO:0000269|PubMed:19756587, ECO:0000269|PubMed:23111597, ECO:0000269|PubMed:25153532, ECO:0000269|PubMed:25495127, ECO:0000269|PubMed:25542606}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) (ABTS) (Dye-decolorizing peroxidase AauDyP1, at pH 4.5) {ECO:0000269|PubMed:19756587}; KM=283 uM for ABTS (Dye-decolorizing peroxidase AauDyP1, at pH 3) {ECO:0000269|PubMed:25153532}; KM=20 uM for ABTS (Dye-decolorizing peroxidase AauDyP2, at pH 4.5) {ECO:0000269|PubMed:19756587}; KM=10 uM for H(2)O(2) (Dye-decolorizing peroxidase AauDyP1) {ECO:0000269|PubMed:19756587}; KM=5 uM for H(2)O(2) (Dye-decolorizing peroxidase AauDyP2) {ECO:0000269|PubMed:19756587}; KM=23 uM for Reactive Blue 5 (Dye-decolorizing peroxidase AauDyP1, at pH 3) {ECO:0000269|PubMed:19756587}; KM=3.1 uM for Reactive Blue 5 (Dye-decolorizing peroxidase AauDyP1, at pH 3) {ECO:0000269|PubMed:25495127}; KM=15 uM for Reactive Blue 5 (Dye-decolorizing peroxidase AauDyP2, at pH 3) {ECO:0000269|PubMed:19756587}; KM=27 uM for 2,6-Dimethoxyphenol (DMP)(Dye-decolorizing peroxidase AauDyP1, at pH 4.5) {ECO:0000269|PubMed:19756587}; KM=27 uM for DMP (Dye-decolorizing peroxidase AauDyP1, at pH 5) {ECO:0000269|PubMed:25542606}; KM=23 uM for DMP (Dye-decolorizing peroxidase AauDyP2, at pH 4.5) {ECO:0000269|PubMed:19756587}; Vmax=134 umol/min/mg enzyme toward Reactive Blue 5 (Dye-decolorizing peroxidase AauDyP1, at pH 3) {ECO:0000269|PubMed:19756587}; Vmax=375 umol/min/mg enzyme toward Reactive Blue 5 (Dye-decolorizing peroxidase AauDyP2, at pH 3) {ECO:0000269|PubMed:19756587}; Vmax=331 umol/min/mg enzyme toward ABTS (Dye-decolorizing peroxidase AauDyP1, at pH 4.5) {ECO:0000269|PubMed:19756587}; Vmax=471 umol/min/mg enzyme toward ABTS (Dye-decolorizing peroxidase AauDyP2, at pH 4.5) {ECO:0000269|PubMed:19756587}; Vmax=105 umol/min/mg enzyme toward DMP (Dye-decolorizing peroxidase AauDyP1, at pH 4.5) {ECO:0000269|PubMed:19756587}; Vmax=130 umol/min/mg enzyme toward DMP (Dye-decolorizing peroxidase AauDyP2, at pH 4.5) {ECO:0000269|PubMed:19756587}; Vmax=315 umol/min/mg enzyme toward H(2)O(2) (Dye-decolorizing peroxidase AauDyP1, at pH 4.5) {ECO:0000269|PubMed:19756587}; Vmax=348 umol/min/mg enzyme toward H(2)O(2) (Dye-decolorizing peroxidase AauDyP2, at pH 4.5) {ECO:0000269|PubMed:19756587}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5 for oxidation of 2,6-dimethoxyphenol (PubMed:23111597). Retains 100% activity after incubation at pH 2.5 for 4 hours (PubMed:19756587, PubMed:23111597, PubMed:25153532). Retains >60% activity after incubation at pH 2-11 at 4 degrees Celsius (PubMed:25153532). Retains >60% activity after incubation at pH 3-9 at room temperature (PubMed:25153532). {ECO:0000269|PubMed:19756587, ECO:0000269|PubMed:23111597, ECO:0000269|PubMed:25153532}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Retains >80% activity after incubation at temperatures up to 60 degrees Celsius for 10 minutes. Retains 50% activity after incubation at 65.5 degrees Celsius for 10 minutes. Activity is lost after incubation at 70 degrees Celsius for 10 minutes. {ECO:0000269|PubMed:25153532}; | FUNCTION: Manganese-independent peroxidase that is able to convert a large number of compounds, but its physiological substrate is not known. In addition to classic peroxidase substrates (e.g. 2,6-dimethoxyphenol), oxidizes dyes such as Reactive Blue 5 and Reactive Black 5. {ECO:0000269|PubMed:19756587, ECO:0000269|PubMed:23111597, ECO:0000269|PubMed:25153532, ECO:0000269|PubMed:25495127, ECO:0000269|PubMed:25542606}. | Auricularia auricula-judae (Judas ear fungus) (Tremella auricula-judae) |
I2G9B4 | VKT_MACLN | MSSGGLLLLLGLLTLWAELTPVSSQDRPKFCYLPADPAECNAYMPRFYYDSASNKCKEFIYGGCRGNANNFKNRAECRHTCVASRKGIQPRIASN | null | null | null | extracellular space [GO:0005615] | serine-type endopeptidase inhibitor activity [GO:0004867] | PF00014; | 4.10.410.10; | Venom Kunitz-type family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23262217}. | null | null | null | null | null | FUNCTION: Serine protease inhibitor that inhibits trypsin. Exhibits an anti-tumor effect and displays integrin inhibitory activity without being cytotoxic. Is able to dose-dependently inhibit the adhesion, migration and invasion of human glioblastoma U87 cells. Also impairs the function of alpha-v/beta-3 (ITGAV/ITGB3) and to a lesser extent, the activity of alpha-v/beta-6 (ITGAV/ITGB6), alpha-v/beta-5 (ITGAV/ITGB5), alpha-1/beta-1 (ITGA1/ITGB1) and alpha-5/beta-1 (ITGA5/ITGB1) integrins. {ECO:0000269|PubMed:23262217}. | Macrovipera lebetina transmediterranea (Blunt-nosed viper) (Vipera lebetina transmediterranea) |
I2HAA0 | TBC8_CAEEL | MQMFRHSSADMWRAKKPTLERRSTDGRRSSIVDWINGLSDNNNYKSDHWVEKHDEGCERMTRNGSVCAVEESEPDVPTQHREVLLTKLKIEIKNIMAEHGAKKYLNLNSPYVTSLCIAVDACIMDGLRRRLLTLFNSPSSMSLLQIIAKSNGPAQQVLDQTREIEELRTSAIPVHLIWIREALYLKSLSTIINHFIDSKSVRRYYDNSALLLDPVKGRLVATLMMAPCMVTYRRMSNRIEQEATAEELVEGATRGSTSTVPSRPPLSITRQVSSIAASVERNGSVSRDYVFSLHHSCKSTLLYGKNNVCVAMNGSDFAKGYMSLQKFYDGNLSLKWVPNQLMHASSQPSSGHSNNGEFTNIWKNTINIEMQDIIYIHLHQKDEISPTCLTFVNCEGVQSAPFQLPAGQHSIAFLSSLETGLAPLLRLDPPLWVGTTKEKILPRLRKRSTAVANPAMLDYVFRLVRTSGVEPAPEDIEDPLAPTSHSPPIHDNCVSLPNSPYIVDNVDSIVNFQIGTACQSMRNQIMARAFYGWLTYVRHLRTIRTHLLHLVDTKTLICDDDCDPVDEKFWKQARAEPTEENEKEFLKRVYWRGIEGINTKEVRRMAWPYLLGLFEWNESPESRLEQFTSQYWQDIEEWRVLEAEVRRRDEEAFRAARARKAASPVREESCDVFEDPNEPTCSQHYDRENLITLFRANLHRIDKDVERCDRNLMFFSNKDNLESLRRVMYTYVRRNLEEGYTQGMCDLLAPLLVTFEDEALTLECFSLLMLRQRGKFPQRPGMSKCLLNLRSLIQVVDPQIYALISDIDYAQALSFAFRWFLLDFKRELSYECTYKVWEVIWAAQRLRITDDFAIFFGLATITNYHDVLITNNFDYTDMIKFFNEMAERHDCSRLLSSARTHVKCLQNLVQHLK | null | null | dense core granule maturation [GO:1990502] | cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; early endosome [GO:0005769]; Golgi medial cisterna [GO:0005797]; Golgi trans cisterna [GO:0000138] | GTPase activator activity [GO:0005096]; small GTPase binding [GO:0031267] | PF12068;PF00566;PF02759; | 1.20.58.900;2.30.29.230;1.10.8.270;1.10.472.80; | RUTBC family | null | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:22654674}. Early endosome {ECO:0000269|PubMed:22654674}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:22654674}; Peripheral membrane protein {ECO:0000269|PubMed:22654674}. Note=Co-localizes with ric-19 at cytoplasmic vesicle membranes in neurons. {ECO:0000269|PubMed:22654674}. | null | null | null | null | null | FUNCTION: Interacts with numerous Rab family members, functioning as Rab effector for some, and as GTPase activator for others (PubMed:22654674). GTPase activator for rab-2 (PubMed:22654674). In association with ric-19 activates rab-2 during dense core vesicle maturation in cholinergic motoneurons (PubMed:22654674). {ECO:0000269|PubMed:22654674}. | Caenorhabditis elegans |
I3L5V6 | SARM1_PIG | MVLTILFSAYKLCRFFAMSSPRPGAERLAVPGPDGGGGAGPWWTAGGRGPREVSPGVGAEVQGALERALPELQQALSALKQAGGGRAVGAGLAEVFQLVEEAWLLPAMGREVAQGLCDAIRLEGGLDLLLRLLQAPELETRVQAARLLEQILVAENRRDRVARIGLGVILNLAKEREPVELARSVAGILEHMFKHSEETCQRLVAAGGLDAVLYWCRRTDPALLRHCALALANCAMHGGQAAQRRMVEKRAAEWLFPLAFSKEDELLRLHACLAVAVLATNKEVEREVERSGTLALVEPLVASLDPGRFARCLVDASDTSQGRGPDDLQRLVPLLDSSRMEAQCIGAFYLCAEAVIMHIKNRNKVFSDIGAIQSLKRLVSYSTNGTTSALAKRALRLLGEEVPRPILPCVASWKEAEVQTWLQQIGFSQYCESFREQQVDGDLLLRLTEEELQTDLGMKSGITRKRFFRELTELKTFANYATCDRSNLADWLGSLDPRFRQYTYGLVSCGLDRSLLHRVSEQQLLEDCGIRLGVHRVRILTAAREMLHSPLPCTGSKPSGDVPDVFISYRRNSGSQLASLLKVHLQLHGFSVFIDVEKLEAGKFEDKLIQSIMSARNFVLVLSAGALDKCMQDHDCKDWVHKEIVTALSCGKNIVPVIDGFEWPEPHTLPEDMQAVLTFNGIKWSHEYQEATIEKIIRFLQGRSSRDSSAGSDTSLEGAAPMGPT | 3.2.2.-; 3.2.2.6 | null | cell differentiation [GO:0030154]; innate immune response [GO:0045087]; NAD catabolic process [GO:0019677]; negative regulation of MyD88-independent toll-like receptor signaling pathway [GO:0034128]; nervous system development [GO:0007399]; protein localization to mitochondrion [GO:0070585]; regulation of dendrite morphogenesis [GO:0048814]; response to axon injury [GO:0048678]; signal transduction [GO:0007165] | axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; microtubule [GO:0005874]; mitochondrion [GO:0005739]; synapse [GO:0045202] | NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; NADP+ nucleosidase activity [GO:0050135]; signaling adaptor activity [GO:0035591] | PF07647;PF13676; | 1.25.10.10;3.40.50.10140;1.10.150.50; | SARM1 family | PTM: Phosphorylation at Ser-549 by JNK kinases (MAPK8, MAPK9 and /or MAPK10) enhance the NAD(+) hydrolase (NADase) activity. Phosphorylation at Ser-549 and subsequent activation takes place in response to oxidative stress conditions and inhibits mitochondrial respiration. {ECO:0000250|UniProtKB:Q6SZW1}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6SZW1}. Cell projection, axon {ECO:0000250|UniProtKB:Q6PDS3}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q6PDS3}. Synapse {ECO:0000250|UniProtKB:Q6PDS3}. Mitochondrion {ECO:0000250|UniProtKB:Q6SZW1}. Note=Associated with microtubules. {ECO:0000250|UniProtKB:Q6PDS3}. | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence={ECO:0000250|UniProtKB:Q6SZW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence={ECO:0000250|UniProtKB:Q6SZW1}; CATALYTIC ACTIVITY: Reaction=NAD(+) = cyclic ADP-beta-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:38611, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:73672; Evidence={ECO:0000250|UniProtKB:Q6SZW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38612; Evidence={ECO:0000250|UniProtKB:Q6SZW1}; CATALYTIC ACTIVITY: Reaction=H2O + NADP(+) = ADP-D-ribose 2'-phosphate + H(+) + nicotinamide; Xref=Rhea:RHEA:19849, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:58349, ChEBI:CHEBI:58673; Evidence={ECO:0000250|UniProtKB:Q6SZW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19850; Evidence={ECO:0000250|UniProtKB:Q6SZW1}; | null | null | null | null | FUNCTION: NAD(+) hydrolase, which plays a key role in axonal degeneration following injury by regulating NAD(+) metabolism (By similarity). Acts as a negative regulator of MYD88- and TRIF-dependent toll-like receptor signaling pathway by promoting Wallerian degeneration, an injury-induced form of programmed subcellular death which involves degeneration of an axon distal to the injury site (PubMed:22366489). Wallerian degeneration is triggered by NAD(+) depletion: in response to injury, SARM1 is activated and catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR), cyclic ADPR (cADPR) and nicotinamide; NAD(+) cleavage promoting cytoskeletal degradation and axon destruction (By similarity). Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules (By similarity). Can activate neuronal cell death in response to stress (By similarity). Regulates dendritic arborization through the MAPK4-JNK pathway (By similarity). Involved in innate immune response: inhibits both TICAM1/TRIF- and MYD88-dependent activation of JUN/AP-1, TRIF-dependent activation of NF-kappa-B and IRF3, and the phosphorylation of MAPK14/p38 (By similarity). {ECO:0000250|UniProtKB:Q6PDS3, ECO:0000250|UniProtKB:Q6SZW1, ECO:0000269|PubMed:22366489}. | Sus scrofa (Pig) |
I3LM39 | CGAS_PIG | MAARRGKSTRTASEVGAAGPRASARSVNGAPTVPEAARPGARRNGPSRASGCRREKSGPDPREKPQVRTRTARAEDQAEGPSAPSERVEPPSAQGASLLRAGSCRAREARSARELRPQAGATELAAPARMEAPPGAWKLQTVLEKVRLSRHEISEAAEVVNWVVEHLLRRLQGGESEFKGVALLRTGSYYERVKISAPNEFDVMFKLEVPRIQLEEYCNSGAHYFVKFKRNPGGNPLEQFLEKEILSASKMLSKFRKIIKEEIKNIEGVTVERKRRGSPAVTLLISKPKEISVDIILALESKSSWPASTQKGLPISQWLGAKVKNNLKRQPFYLVPKHAKEGSGFQEETWRLSFSHIEKDILKNHGQSKTCCEIDGVKCCRKECLKLMKYLLEQLKKKFGNRRELAKFCSYHVKTAFFHVCTQDPHDNQWHLKNLECCFDNCVAYFLQCLKTEQLANYFIPGVNLFSRDLIDKPSKEFLSKQIEYERNNGFPVFW | 2.7.7.86 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:23722159}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8C6L5}; Note=Binds 1 Mg(2+) per subunit (PubMed:23722159). Is also active with Mn(2+). Mn(2+)-activated enzyme forms an inverted pppGp(2'-5')A intermediate, suggesting a non-canonical but accelerated 2',3'-cGAMP cyclization without substrate flip-over. Mn(2+) ions are coordinated by triphosphate moiety of the inverted substrate, independent of the catalytic triad residues (By similarity) (PubMed:23722159). {ECO:0000250|UniProtKB:Q8C6L5, ECO:0000269|PubMed:23722159}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8C6L5}; Note=Undergoes a liquid-like phase transition after binding to DNA, which is dependent on zinc. {ECO:0000250|UniProtKB:Q8N884}; | activation of innate immune response [GO:0002218]; cAMP-mediated signaling [GO:0019933]; cellular response to exogenous dsRNA [GO:0071360]; defense response to virus [GO:0051607]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; innate immune response [GO:0045087]; negative regulation of double-strand break repair via homologous recombination [GO:2000042]; paracrine signaling [GO:0038001]; positive regulation of cellular senescence [GO:2000774]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of type I interferon production [GO:0032481] | cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; site of double-strand break [GO:0035861] | 2',3'-cyclic GMP-AMP synthase activity [GO:0061501]; ATP binding [GO:0005524]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; molecular condensate scaffold activity [GO:0140693]; nucleosome binding [GO:0031491]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; poly-ADP-D-ribose modification-dependent protein binding [GO:0160004]; protein homodimerization activity [GO:0042803] | PF03281;PF20266; | 1.10.1410.40;3.30.460.90; | Mab-21 family | PTM: The N-terminal disordered part (1-134) is phosphorylated by AURKB during the G2-M transition, blocking CGAS liquid phase separation and preventing activation. Phosphorylation at Tyr-190 by BLK promotes cytosolic retention. Localizes into the nucleus following dephosphorylation at Tyr-190 (By similarity). Phosphorylation at Ser-410 activates the nucleotidyltransferase activity. Dephosphorylation at Ser-410 by PPP6C impairs its ability to bind GTP, thereby inactivating it (By similarity). Phosphorylation at Ser-188 by PRKDC inhibits its cyclic GMP-AMP synthase activity by impairing homodimerization and activation (By similarity). Phosphorylation at Ser-278 by AKT (AKT1, AKT2 or AKT3) suppresses the nucleotidyltransferase activity. Phosphorylation at Ser-278 by CDK1 during mitosis leads to its inhibition, thereby preventing CGAS activation by self-DNA during mitosis. Dephosphorylated at Ser-278 by protein phosphatase PP1 upon mitotic exit (By similarity). {ECO:0000250|UniProtKB:Q8C6L5, ECO:0000250|UniProtKB:Q8N884}.; PTM: Ubiquitinated at Lys-389 via 'Lys-48'-linked polyubiquitin chains, leading to its SQSTM1-mediated autophagic degradation. Interaction with TRIM14 promotes recruitment of USP14, leading to deubiquitinate Lys-389 and stabilize CGAS. Ubiquitinated at Lys-359 by RNF185 via 'Lys-27'-linked polyubiquitination, promoting CGAS cyclic GMP-AMP synthase activity (By similarity). Monoubiquitination at Lys-322 by TRIM56 promotes oligomerization and subsequent activation (By similarity). Monoubiquitination by TRIM41 promotes CGAS activation (By similarity). Ubiquitination at Lys-260 via 'Lys-48'-linked polyubiquitination promotes its degradation. Deubiquitination at Lys-260 by USP29 promotes its stabilization. Deubiquitinated by USP27X, promoting its stabilization (By similarity). Ubiquitinated at Lys-386 via 'Lys-63'-linked polyubiquitin chains by MARCHF8, leading to the inhibition of its DNA binding ability (By similarity). {ECO:0000250|UniProtKB:Q8C6L5, ECO:0000250|UniProtKB:Q8N884}.; PTM: Sumoylated at Lys-206 by TRIM38 in uninfected cells and during the early phase of viral infection, promoting its stability by preventing ubiquitination at Lys-260 and subsequent degradation. Desumoylated by SENP2 during the late phase of viral infection. Sumoylation at Lys-322, Lys-359 and Lys-369 prevents DNA-binding, oligomerization and nucleotidyltransferase activity. Desumoylation at Lys-322, Lys-359 and Lys-369 by SENP7 relieves inhibition and activates CGAS. {ECO:0000250|UniProtKB:Q8C6L5}.; PTM: Polyglutamylated by TTLL6 at Glu-261, leading to impair DNA-binding activity. Deglutamylated by AGBL5/CCP5 and AGBL6/CCP6. {ECO:0000250|UniProtKB:Q8C6L5}.; PTM: Acetylation at Lys-359, Lys-369 and Lys-389 inhibits the cyclic GMP-AMP synthase activity. Deacetylated upon cytosolic DNA challenge such as viral infections. Acetylation by KAT5 increases the cyclic GMP-AMP synthase activity by promoting DNA-binding and subsequent activation. {ECO:0000250|UniProtKB:Q8N884}.; PTM: Proteolytically cleaved by apoptotic caspases during apoptosis, leading to its inactivation. The damage of the nucleus and the mitochondria during apoptosis leads to leakage of nuclear and mitochondrial DNA, which activate CGAS: cleavage and inactivation during apoptosis in required to prevent cytokine overproduction. Cleaved by CASP7 and CASP3 during virus-induced apoptosis, thereby inactivating it and preventing cytokine overproduction. Cleaved by CASP1 upon DNA virus infection; the cleavage impairs cGAMP production. Also cleaved by the pyroptotic CASP4 during non-canonical inflammasome activation; does not cut at the same sites than CASP1. {ECO:0000250|UniProtKB:Q8C6L5}.; PTM: Degraded via selective autophagy following interaction with IRGM. IRGM promotes CGAS recruitment to autophagosome membranes, promoting its SQSTM1/p62-dependent autophagic degradation. {ECO:0000250|UniProtKB:Q8N884}.; PTM: Poly-ADP-ribosylation at Glu-165 by PARP1 impairs DNA-binding, thereby preventing the cyclic GMP-AMP synthase activity. {ECO:0000250|UniProtKB:Q8N884}.; PTM: Palmitoylation at Cys-449 by ZDHHC18 impairs DNA-binding, thereby preventing the cyclic GMP-AMP synthase activity (By similarity). Palmitoylation at Cys-379 and Cys-380 by ZDHHC9 promotes homodimerization and cyclic GMP-AMP synthase activity (By similarity). Depalmitoylation at Cys-379 and Cys-380 by LYPLAL1 impairs homodimerization and cyclic GMP-AMP synthase activity (By similarity). {ECO:0000250|UniProtKB:Q8N884}.; PTM: Monomethylated at Lys-481 by SETD7 (By similarity). Monomethylation promotes interaction with SGF29, preventing interaction between PARP1 nad SGF29. Demethylation by RIOX1 promotes interaction with PARP1, followed by PARP1 inactivation (By similarity). {ECO:0000250|UniProtKB:Q8C6L5}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8C6L5}. Chromosome {ECO:0000250|UniProtKB:Q8C6L5}. Cell membrane {ECO:0000250|UniProtKB:Q8C6L5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8C6L5}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8C6L5}. Note=Mainly localizes in the nucleus, and at low level in the cytosol (By similarity). On chromosomes, enriched on centromeric satellite and LINE DNA repeat elements. Exported from the nucleus to the cytosol in a XPO1/CRM1 via the nuclear export signal in response to DNA stimulation (By similarity). Outside the nucleus, localizes at the cell membrane as a peripheral membrane protein in resting conditions: association to the cell membrane is mediated via binding to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) (By similarity). Localization at the cell membrane is required to limit the recognition of self-DNA. Following detection of double-stranded DNA (dsDNA), released from the cell membrane into the cytosol in order to signal. Upon transfection with dsDNA forms punctate structures that co-localize with DNA and Beclin-1 (BECN1). Phosphorylation at Tyr-190 promotes cytosolic retention. In response to translation stress, translocates to the cytosol and associates with collided ribosomes (By similarity). {ECO:0000250|UniProtKB:Q8C6L5, ECO:0000250|UniProtKB:Q8N884}. | CATALYTIC ACTIVITY: Reaction=ATP + GTP = 2',3'-cGAMP + 2 diphosphate; Xref=Rhea:RHEA:42064, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:143093; EC=2.7.7.86; Evidence={ECO:0000269|PubMed:23722159}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42065; Evidence={ECO:0000269|PubMed:23722159}; | null | null | null | null | FUNCTION: Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity (PubMed:23722159). Catalysis involves both the formation of a 2',5' phosphodiester linkage at the GpA step and the formation of a 3',5' phosphodiester linkage at the ApG step, producing c[G(2',5')pA(3',5')p] (PubMed:23722159). Acts as a key DNA sensor: directly binds double-stranded DNA (dsDNA), inducing the formation of liquid-like droplets in which CGAS is activated, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates STING1, thereby triggering type-I interferon production. Preferentially binds long dsDNA (around 45 bp) and forms ladder-like networks that function cooperatively to stabilize individual cGAS-dsDNA complexes. Acts as a key foreign DNA sensor, the presence of double-stranded DNA (dsDNA) in the cytoplasm being a danger signal that triggers the immune responses. Has antiviral activity by sensing the presence of dsDNA from DNA viruses in the cytoplasm. Also acts as an innate immune sensor of infection by retroviruses by detecting the presence of reverse-transcribed DNA in the cytosol (By similarity). Detection of retroviral reverse-transcribed DNA in the cytosol may be indirect and be mediated via interaction with PQBP1, which directly binds reverse-transcribed retroviral DNA. Also detects the presence of DNA from bacteria (By similarity). 2',3'-cGAMP can be transferred from producing cells to neighboring cells through gap junctions, leading to promote STING1 activation and convey immune response to connecting cells. 2',3'-cGAMP can also be transferred between cells by virtue of packaging within viral particles contributing to IFN-induction in newly infected cells in a cGAS-independent but STING1-dependent manner. Also senses the presence of neutrophil extracellular traps (NETs) that are translocated to the cytosol following phagocytosis, leading to synthesis of 2',3'-cGAMP (By similarity). In addition to foreign DNA, can also be activated by endogenous nuclear or mitochondrial DNA (By similarity). When self-DNA leaks into the cytosol during cellular stress (such as mitochondrial stress, DNA damage, mitotic arrest or senescence), or is present in form of cytosolic micronuclei, CGAS is activated leading to a state of sterile inflammation. Acts as a regulator of cellular senescence by binding to cytosolic chromatin fragments that are present in senescent cells, leading to trigger type-I interferon production via STING1 and promote cellular senescence. Also involved in the inflammatory response to genome instability and double-stranded DNA breaks: acts by localizing to micronuclei arising from genome instability. Micronuclei, which are frequently found in cancer cells, consist of chromatin surrounded by their own nuclear membrane: following breakdown of the micronuclear envelope, a process associated with chromothripsis, CGAS binds self-DNA exposed to the cytosol, leading to 2',3'-cGAMP synthesis and subsequent activation of STING1 and type-I interferon production (By similarity). In a healthy cell, CGAS is however kept inactive even in cellular events that directly expose it to self-DNA, such as mitosis, when cGAS associates with chromatin directly after nuclear envelope breakdown or remains in the form of postmitotic persistent nuclear cGAS pools bound to chromatin (By similarity). Nuclear CGAS is inactivated by chromatin via direct interaction with nucleosomes, which block CGAS from DNA binding and thus prevent CGAS-induced autoimmunity. Also acts as a suppressor of DNA repair in response to DNA damage: inhibits homologous recombination repair by interacting with PARP1, the CGAS-PARP1 interaction leading to impede the formation of the PARP1-TIMELESS complex (By similarity). In addition to DNA, also sense translation stress: in response to translation stress, translocates to the cytosol and associates with collided ribosomes, promoting its activation and triggering type-I interferon production (By similarity). {ECO:0000250|UniProtKB:Q8C6L5, ECO:0000250|UniProtKB:Q8N884, ECO:0000269|PubMed:23722159}. | Sus scrofa (Pig) |
I3LMB3 | PLM_PIG | MASLSHILVLWVGILTVVNAEAPQEHDPFTYDYQSLRIGGLIIAGILFILGILIVLSRRCRCKFNQQQSLGKMRSPHLAAQFSSESC | null | null | negative regulation of protein glutathionylation [GO:0010734]; positive regulation of sodium ion export across plasma membrane [GO:1903278]; potassium ion transport [GO:0006813]; sodium ion transport [GO:0006814] | apical plasma membrane [GO:0016324]; caveola [GO:0005901]; intercalated disc [GO:0014704]; sarcolemma [GO:0042383]; sodium:potassium-exchanging ATPase complex [GO:0005890]; T-tubule [GO:0030315] | sodium channel regulator activity [GO:0017080]; transmembrane transporter binding [GO:0044325] | PF02038; | 1.20.5.780; | FXYD family | PTM: Major plasma membrane substrate for cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) in several different tissues. Phosphorylated in response to insulin and adrenergic stimulation. Phosphorylation at Ser-83 stimulates sodium/potassium-transporting ATPase activity while the unphosphorylated form inhibits sodium/potassium-transporting ATPase activity. Phosphorylation increases tetramerization, decreases binding to ATP1A1 and reduces inhibition of ATP1A1 activity. Phosphorylation at Ser-75 leads to greatly reduced interaction with ATP1A1, ATP1A2 and ATP1A3. May be phosphorylated by DMPK. {ECO:0000250|UniProtKB:O00168, ECO:0000250|UniProtKB:O08589, ECO:0000250|UniProtKB:P56513}.; PTM: Palmitoylation increases half-life and stability and is enhanced upon phosphorylation at Ser-83 by PKA. {ECO:0000250|UniProtKB:O00168}. | SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P56513}; Single-pass type I membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O08589}; Single-pass type I membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000250|UniProtKB:O08589}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O08589}. Note=Detected in the apical cell membrane in brain. In myocytes, localizes to sarcolemma, t-tubules and intercalated disks. {ECO:0000250|UniProtKB:O08589}. | null | null | null | null | null | FUNCTION: Associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na(+) out of the cell and K(+) into the cell. Inhibits NKA activity in its unphosphorylated state and stimulates activity when phosphorylated. Reduces glutathionylation of the NKA beta-1 subunit ATP1B1, thus reversing glutathionylation-mediated inhibition of ATP1B1. Contributes to female sexual development by maintaining the excitability of neurons which secrete gonadotropin-releasing hormone. {ECO:0000250|UniProtKB:O08589, ECO:0000250|UniProtKB:P56513, ECO:0000250|UniProtKB:Q9Z239}. | Sus scrofa (Pig) |
I3M072 | APOA1_ICTTR | MKAVVLTVAVLFLTGSQARHFWQQDEPQSSWDRIKDFATVYLDAVKDSGRDYVTQFETSALGKQLNLKLLDNWDSLSSTVSKVREQIGPVSQDFWDKLEKDTVSLRQEMNKDLEEVKRKVQPYLDEFQKRWQEDVERYRQQVEPLSKELREGARQKLLELHEKLSPLGQEMRDRARTHVDALRTHLAPYSDELRQRLAARLEALKEGSSFAEYQAKATEHLSALGEKAKPALEDLRQGLLPVLESLKLSFWSAVDEATKKLNTQ | null | null | adrenal gland development [GO:0030325]; blood vessel endothelial cell migration [GO:0043534]; cholesterol biosynthetic process [GO:0006695]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol import [GO:0070508]; endothelial cell proliferation [GO:0001935]; G protein-coupled receptor signaling pathway [GO:0007186]; glucocorticoid metabolic process [GO:0008211]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein particle remodeling [GO:0034375]; integrin-mediated signaling pathway [GO:0007229]; lipid storage [GO:0019915]; lipoprotein biosynthetic process [GO:0042158]; negative regulation of cell adhesion molecule production [GO:0060354]; negative regulation of cytokine production involved in immune response [GO:0002719]; negative regulation of heterotypic cell-cell adhesion [GO:0034115]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interleukin-1 beta production [GO:0032691]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; negative regulation of very-low-density lipoprotein particle remodeling [GO:0010903]; phosphatidylcholine biosynthetic process [GO:0006656]; phospholipid efflux [GO:0033700]; phospholipid homeostasis [GO:0055091]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of cholesterol metabolic process [GO:0090205]; positive regulation of phagocytosis [GO:0050766]; positive regulation of phospholipid efflux [GO:1902995]; positive regulation of Rho protein signal transduction [GO:0035025]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; protein stabilization [GO:0050821]; regulation of Cdc42 protein signal transduction [GO:0032489]; regulation of intestinal cholesterol absorption [GO:0030300]; regulation of protein phosphorylation [GO:0001932]; reverse cholesterol transport [GO:0043691]; triglyceride homeostasis [GO:0070328]; vitamin transport [GO:0051180] | endocytic vesicle [GO:0030139]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; apolipoprotein A-I receptor binding [GO:0034191]; chemorepellent activity [GO:0045499]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; high-density lipoprotein particle binding [GO:0008035]; high-density lipoprotein particle receptor binding [GO:0070653]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein homodimerization activity [GO:0042803] | PF01442; | 1.20.5.20;6.10.140.380;1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: Glycosylated. {ECO:0000250|UniProtKB:P02648}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:P02648}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02647}. | null | null | null | null | null | FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. {ECO:0000250|UniProtKB:P02647}. | Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus tridecemlineatus) |
I3PB36 | CNL_PETHY | MDELPKCGANYVPLTPLTFLTRAFKSYANRTSIIYAGARFTWEQTYKRCCRLASSLQSLNIVKNDVVSVLAPNVPATYEMHFAVPMAGAVLNTINTRLDPMNIAIILKHSEAKLLFVDYEYLEKARKALELLMSTNFITAQNSKKISMPQVILIDDLYSPTRIQQQDQLEYEQLVHQGNPEYAPENIVDDEWDPIVLNYTSGTTSEPKGVVYSHRGAFLSTLNTIMGWEMGTEPVYLWSLPMFHINGWTLTWGIAARGGTNVCIRNTTAQEIYSNITLHKVTHMCCAPTVFNILLEAKPHERREITTPVQVMVGGAPPPTTLIGKIEELGFHVVHCYGITEAGGTTLVCEWQSEWNKLSREDQANLKARQGISVLALEDVDVKNSKTMQSVPHNGKTMGEICLRGSSIMKGYFKNDKANSQVFKNGWFLTGDVAVIHQDGYLEIKDRCKDIIISGGENISSIEVENAILKHPSVIEAAVVAMPHPRWGETPCAFVIKTKNPEIKEADIIVHCKKELPGFMVPKHVQFLEELPKTGTGKVKKLQLREMAKSFGIFDNANQTSQILDLPARL | 6.2.1.-; 6.2.1.12 | COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:22649270}; | cinnamic acid biosynthetic process [GO:0009800]; cinnamic acid metabolic process [GO:0009803]; circadian rhythm [GO:0007623]; green leaf volatile biosynthetic process [GO:0010597]; phenylpropanoid metabolic process [GO:0009698]; phytoalexin biosynthetic process [GO:0052315]; response to ethylene [GO:0009723] | peroxisome [GO:0005777] | (E)-caffeate-CoA ligase activity [GO:0106286]; 4-coumarate-CoA ligase activity [GO:0016207]; ATP binding [GO:0005524]; CoA-ligase activity [GO:0016405]; trans-cinnamate-CoA ligase activity [GO:0106290] | PF00501;PF13193; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:22649270, ECO:0000269|PubMed:22771854}. Note=Located in the peroxisomes of flower petal limb cells. {ECO:0000269|PubMed:22771854}. | CATALYTIC ACTIVITY: Reaction=(E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:19641, ChEBI:CHEBI:12876, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:85008, ChEBI:CHEBI:456215; EC=6.2.1.12; Evidence={ECO:0000269|PubMed:22649270}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19642; Evidence={ECO:0000269|PubMed:22649270}; CATALYTIC ACTIVITY: Reaction=(E)-caffeate + ATP + CoA = (E)-caffeoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:36299, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57770, ChEBI:CHEBI:87136, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:22649270}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36300; Evidence={ECO:0000269|PubMed:22649270}; CATALYTIC ACTIVITY: Reaction=(E)-cinnamate + ATP + CoA = (E)-cinnamoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:64788, ChEBI:CHEBI:15669, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57252, ChEBI:CHEBI:57287, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:22649270}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64789; Evidence={ECO:0000269|PubMed:22649270}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=285.7 uM for trans-cinnamic acid {ECO:0000269|PubMed:22649270}; KM=550.4 uM for 4-coumaric acid {ECO:0000269|PubMed:22649270}; KM=1024.4 uM for caffeic acid {ECO:0000269|PubMed:22649270}; KM=775.2 uM for CoA {ECO:0000269|PubMed:22649270}; Vmax=7401.7 pmol/sec/mg enzyme with trans-cinnamic acid as substrate {ECO:0000269|PubMed:22649270}; Vmax=3890.7 pmol/sec/mg enzyme with 4-coumaric acid as substrate {ECO:0000269|PubMed:22649270}; Vmax=3742.7 pmol/sec/mg enzyme with caffeic acid as substrate {ECO:0000269|PubMed:22649270}; Vmax=7179.7 pmol/sec/mg enzyme with CoA acid as substrate {ECO:0000269|PubMed:22649270}; Note=kcat is 0.472 sec(-1) with trans-cinnamic acid as substrate (PubMed:22649270). kcat is 0.248 sec(-1) with 4-coumaric acid as substrate (PubMed:22649270). kcat is 0.238 sec(-1) with caffeic acid as substrate (PubMed:22649270). kcat is 0.458 sec(-1) with CoA as substrate (PubMed:22649270). {ECO:0000269|PubMed:22649270}; | PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis. {ECO:0000269|PubMed:22649270}.; PATHWAY: Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene biosynthesis; 3,4',5-trihydroxystilbene from trans-4-coumarate: step 1/2. {ECO:0000269|PubMed:22649270}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8 with cinnamic acid as a substrate. {ECO:0000269|PubMed:22649270}; | null | FUNCTION: Involved in the biosynthesis of floral volatile benzenoid/phenylpropanoid (FVBP) scent (e.g. benzylbenzoate, phenylethylbenzoate, and methylbenzoate) (PubMed:22649270, PubMed:22771854). Catalyzes the formation of CoA esters of cinnamic acid, and, with lower efficiency, of 4-coumaric acid and caffeic acid (PubMed:22649270). {ECO:0000269|PubMed:22649270, ECO:0000269|PubMed:22771854}. | Petunia hybrida (Petunia) |
I3PB37 | 4CL1_PETHY | MPMETETNQGDLIFRSKLPDIYIPKHLPLHSYCFENISEFSSRPCLINGANNHIYTYADVELTSRKVAAGLNKLGIQQKDTIMILLPNSPEFVFAFMGASYLGAISTMANPLFTPAEVVKQAKASNAKLIITQACFVNKVKDYAFDNNLNVICIDSAPEGCIHFSELTQADEHDIPDVKIQSDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENANLYMHSEDVLMCVLPLFHIYSLNSVLLCGLRVGAAILIMQKFDIVQFCELIEKYKVTIGPFVPPIVLAIAKSPVVDNYDLSSVRTVMSGAAPLGKELEDAVRIKFPNAKLGQGYGMTEAGPVLAMCLAFAKEPFDIKSGACGTVVRNAEMKIVDPDTGCSLPRNQPGEICIRGDQIMKGYLNDPAATTRTIDKEGWLHTGDIGYIDNDDELFIVDRLKELIKYKGFQVAPAELEALLLNHPNISDAAVVPMKDEQAGEVPVAFVVRSNGSDITEDEVKDFVSKQVIFYKRIKRVFFVETVPKSPSGKILRKDLRARLAAGVPN | 6.2.1.-; 6.2.1.12; 6.2.1.25 | null | cinnamic acid biosynthetic process [GO:0009800]; cinnamic acid metabolic process [GO:0009803]; circadian rhythm [GO:0007623]; ferulate metabolic process [GO:0033494]; phenylpropanoid metabolic process [GO:0009698]; phytoalexin biosynthetic process [GO:0052315] | cytosol [GO:0005829] | (E)-caffeate-CoA ligase activity [GO:0106286]; 4-coumarate-CoA ligase activity [GO:0016207]; ATP binding [GO:0005524]; benzoate-CoA ligase activity [GO:0018858]; CoA-ligase activity [GO:0016405]; trans-cinnamate-CoA ligase activity [GO:0106290]; trans-feruloyl-CoA synthase activity [GO:0050563] | PF00501;PF13193; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22649270}. | CATALYTIC ACTIVITY: Reaction=(E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:19641, ChEBI:CHEBI:12876, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:85008, ChEBI:CHEBI:456215; EC=6.2.1.12; Evidence={ECO:0000269|PubMed:22649270}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19642; Evidence={ECO:0000269|PubMed:22649270}; CATALYTIC ACTIVITY: Reaction=(E)-caffeate + ATP + CoA = (E)-caffeoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:36299, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57770, ChEBI:CHEBI:87136, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:22649270}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36300; Evidence={ECO:0000269|PubMed:22649270}; CATALYTIC ACTIVITY: Reaction=ATP + benzoate + CoA = AMP + benzoyl-CoA + diphosphate; Xref=Rhea:RHEA:10132, ChEBI:CHEBI:16150, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57369, ChEBI:CHEBI:456215; EC=6.2.1.25; Evidence={ECO:0000269|PubMed:22649270}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10133; Evidence={ECO:0000269|PubMed:22649270}; CATALYTIC ACTIVITY: Reaction=(E)-cinnamate + ATP + CoA = (E)-cinnamoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:64788, ChEBI:CHEBI:15669, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57252, ChEBI:CHEBI:57287, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:22649270}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64789; Evidence={ECO:0000269|PubMed:22649270}; CATALYTIC ACTIVITY: Reaction=(E)-ferulate + ATP + CoA = (E)-feruloyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:36251, ChEBI:CHEBI:29749, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:87305, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:22649270}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36252; Evidence={ECO:0000269|PubMed:22649270}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=149.4 uM for trans-cinnamic acid {ECO:0000269|PubMed:22649270}; KM=16.4 uM for 4-coumaric acid {ECO:0000269|PubMed:22649270}; KM=47.8 uM for caffeic acid {ECO:0000269|PubMed:22649270}; KM=15.2 uM for ferulic acid {ECO:0000269|PubMed:22649270}; KM=9008 uM for benzoic acid {ECO:0000269|PubMed:22649270}; KM=9.9 uM for CoA {ECO:0000269|PubMed:22649270}; Vmax=14680 pmol/sec/mg enzyme with trans-cinnamic acid as substrate {ECO:0000269|PubMed:22649270}; Vmax=25797 pmol/sec/mg enzyme with 4-coumaric acid as substrate {ECO:0000269|PubMed:22649270}; Vmax=63200 pmol/sec/mg enzyme with caffeic acid as substrate {ECO:0000269|PubMed:22649270}; Vmax=41377 pmol/sec/mg enzyme with ferulic acid as substrate {ECO:0000269|PubMed:22649270}; Vmax=95.9 pmol/sec/mg enzyme with benzoic acid as substrate {ECO:0000269|PubMed:22649270}; Vmax=8451 pmol/sec/mg enzyme with CoA acid as substrate {ECO:0000269|PubMed:22649270}; Note=kcat is 0.847 sec(-1) with trans-cinnamic acid as substrate (PubMed:22649270). kcat is 1.488 sec(-1) with 4-coumaric acid as substrate (PubMed:22649270). kcat is 3.645 sec(-1) with caffeic acid as substrate (PubMed:22649270). kcat is 2.39 sec(-1) with ferulic acid as substrate (PubMed:22649270). kcat is 0.0007 sec(-1) with benzoic acid as substrate (PubMed:22649270). kcat is 0.487 sec(-1) with CoA as substrate (PubMed:22649270). {ECO:0000269|PubMed:22649270}; | PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis. {ECO:0000269|PubMed:22649270}.; PATHWAY: Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene biosynthesis; 3,4',5-trihydroxystilbene from trans-4-coumarate: step 1/2. {ECO:0000269|PubMed:22649270}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 with cinnamic acid as a substrate. {ECO:0000269|PubMed:22649270}; | null | FUNCTION: Catalyzes the formation of CoA esters of trans-cinnamic acid, 4-coumaric acid, ferulic acid, benzoic acid and caffeic acid. {ECO:0000269|PubMed:22649270}. | Petunia hybrida (Petunia) |
I3PLQ6 | SOMT2_PAPSO | MEIHLESQEQEMKYQSQIWNQICGTVDTSVLRCAIQLGIFDAIHNSGKPMITLTELSSIVSSPSSSSIEPCNLYRLVRYLSQMDLISIGECLNEATVSLTGTSKLLLRNQEKSLIDWVLAISCEMMVVVWHELSSSVSTPADEPPIFQKVHGKNALELAGEFPEWNDLINNAMTSDTSVTKPALIQGCGKILNGVTSLIDVGGGHGATMAYIVEAFPHIKGAVIDLPHVVEAAPERPGVEFISGDIFKSISNADAVLLKYVLHNWEDTECVNLLKRCKEAVPADKGKVIIMDLVIDDDDNSILTQAKLSLDLTVMNHGGGRERTKEDWRNLIEMSGFSRHEIIPISAMPSIIVAYP | 2.1.1.117; 2.1.1.352 | null | alkaloid metabolic process [GO:0009820]; melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259] | null | (S)-scoulerine 9-O-methyltransferase activity [GO:0030777]; acetylserotonin O-methyltransferase activity [GO:0017096]; protein dimerization activity [GO:0046983] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family, COMT subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(S)-scoulerine + S-adenosyl-L-methionine = (S)-tetrahydrocolumbamine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:23808, ChEBI:CHEBI:15378, ChEBI:CHEBI:17129, ChEBI:CHEBI:17772, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.117; Evidence={ECO:0000269|PubMed:22535422}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23809; Evidence={ECO:0000305|PubMed:22535422}; CATALYTIC ACTIVITY: Reaction=(S)-S-adenosyl-L-methionine + 3-O-acetyl-4'-O-demethylpapaveroxine = 3-O-acetylpapaveroxine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:57396, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:141643, ChEBI:CHEBI:141645, ChEBI:CHEBI:142094; EC=2.1.1.352; Evidence={ECO:0000269|PubMed:29723437}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57397; Evidence={ECO:0000305|PubMed:29723437}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=73.3 uM for (S)-scoulerine {ECO:0000269|PubMed:22535422}; KM=69.6 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:22535422}; Vmax=145.8 nmol/min/mg enzyme with (S)-scoulerine as substrate {ECO:0000269|PubMed:22535422}; Vmax=134 nmol/min/mg enzyme with S-adenosyl-L-methionine as substrate {ECO:0000269|PubMed:22535422}; | PATHWAY: Alkaloid biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Methyltransferase involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine (PubMed:22535422, PubMed:27378283, PubMed:29610307, PubMed:29723437). Catalyzes the conversion of (S)-scoulerine to (S)-tetrahydrocolumbamine (PubMed:22535422). The heterodimers SOMT2-SOMT3 and SOMT2-6OMT convert 3-O-acetyl-4'-O-demethylpapaveroxine to 3-O-acetylpapaveroxine, where SOMT2 is the catalytic subunit (PubMed:27378283, PubMed:29723437). {ECO:0000269|PubMed:22535422, ECO:0000269|PubMed:27378283, ECO:0000269|PubMed:29610307, ECO:0000269|PubMed:29723437}. | Papaver somniferum (Opium poppy) |
I3R634 | NASA_HALMT | MPRNLRFLSVVNHVTKQVPTTCMRCAVGCGHVHLGSENAYGLETVRGDPSHPVNNGLACGRGIRESADPAGEWLTRPLVREDGELVQTSWSDAMARVGATIRTAVATDPDEVAVLGSGQQTNEAAYALGKLARAGIGTRNYDANTTLCMASAVTAYYRAFGSDAPPPTYDDIPNAETHLVWGANPAVAHPVMFRWIRQSATDGRLVVVDPVETKTAAVADDHVSVAPGGDLALARAILRHLVDTDQIDESFVRSNTEGFDDVVSALPSVTDAAARAGVSLDTVEELAALLDAPTLIYWGMGVNQSVRGTATAGALVNLCLASGNLGPGTGPFSLTGQANSMGTRVCSSKGTWSGHRPFEHPDHRRAVAEAWDVPVSRLPDDSGPGPVGILDSSPSVVWTVATNPLAGFPDATAAREVLRDSFLVVQDAFRSDTVELADVVLPAATWGESEGTAMNMERTVSRIRAATETPPGVRQDLDIIADVAARVAPGLLPRPPVSPSAIFDEFAALTEGTDADCSGISYTRLDGERAVRWPAPEPNSDAGYRYYDPSTSRWTFPTPSGKARFSTLDGEPLPEPVDGDYPLTLTTGREADGYNTGVRSRSDTPEEPVARVNPETVDTYHDAVADTDGELRTTVVSRRASVSVTLDRDDAVPPGLVWLSIHHPMTNQLTSPAVDPQSNEPNFKQCAVRFVHPDAPAKADFLAAEVSD | 1.7.7.2 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305|PubMed:11731152}; COFACTOR: Name=Mo-bis(molybdopterin guanine dinucleotide); Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250|UniProtKB:Q57366}; Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit. {ECO:0000250|UniProtKB:Q57366}; | nitrate assimilation [GO:0042128] | cytoplasm [GO:0005737] | 4 iron, 4 sulfur cluster binding [GO:0051539]; ferredoxin-nitrate reductase activity [GO:0047889]; metal ion binding [GO:0046872]; molybdopterin cofactor binding [GO:0043546] | PF04879;PF00384;PF01568; | 2.40.40.20;3.40.50.740;2.20.25.90;3.40.228.10; | Prokaryotic molybdopterin-containing oxidoreductase family, NasA/NapA/NarB subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=H2O + nitrite + 2 oxidized [2Fe-2S]-[ferredoxin] = 2 H(+) + nitrate + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:21828, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.7.7.2; Evidence={ECO:0000269|PubMed:11731152}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.95 mM for nitrate {ECO:0000269|PubMed:11731152}; KM=0.066 mM for methyl viologen {ECO:0000269|PubMed:11731152}; | PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation). {ECO:0000305|PubMed:16182473}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9. {ECO:0000269|PubMed:11731152}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80 degrees Celsius at 2.2 and 3.1 M NaCl, and 60 degrees Celsius at 0.9 and 1.3 M NaCl. {ECO:0000269|PubMed:11731152}; | FUNCTION: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation. Catalyzes the reduction of nitrate to nitrite, using ferredoxin as the electron donor. Can use reduced methyl viologen but neither NADPH nor NADH as electron donors. {ECO:0000269|PubMed:11731152}. | Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei) |
I3R637 | NASD_HALMT | MASKKEQWKSDLYGDAVRDELEAFAEEGFESIPEDERDKWFTRFKFWGVFQQRTGQESYFMMRLTNANGVLEPGQLRTIAEVARDYATGPVDNPEFGNGWVDLTTRQSIQLHWLELEDIPEIWEQLESVGVTSRSAGGDTMRNITGCPVAGKDTHELVESKPLLDRFQSELREDDALSNMPRKFNISVTGCREGCAQDSINDIGLEPARKEVDGEVITGFNVRVGGGLGSRKPRVARSLDVFVADEERAYEVVRGFVELYHDHGNRDVRARARSRFFVDDWGTEKIRDRLESEYLDFELQSAGEDIRDEYTYNAGRPQSAGKSDHVGVHEQSDGRYYVGLSVAVGRLTAADALELADLADKYGSGKIRLTRRQNPIVMDVPAGALDDLLAEPLLSKHTPEPNPFQRGTVACTGTEFCSLALTETKARTARMLRWLRDNVEVPDDVHQLKIHYSGCTADCGQANTADIGLFGMRAQKDGEMVEAMDIGVGGGIGDEPSFVEWIHQRVPADEVPGAIASLVEAFAAHRTAGQTFRQWVEAEGPDAVAEYCEPIETDFEAPYMHDAKQSWYPFADEDEPPKTEQPMTSD | 1.7.7.1 | COFACTOR: Name=siroheme; Xref=ChEBI:CHEBI:60052; Evidence={ECO:0000269|PubMed:11267765}; Note=Binds 1 siroheme per subunit. {ECO:0000250|UniProtKB:P9WJ03}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305|PubMed:11267765}; Note=Binds 1 [4Fe-4S] cluster per subunit.; | nitrate assimilation [GO:0042128] | null | 4 iron, 4 sulfur cluster binding [GO:0051539]; ferredoxin-nitrite reductase activity [GO:0048307]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491] | PF01077;PF03460; | 3.90.480.20;3.30.413.10; | Nitrite and sulfite reductase 4Fe-4S domain family | null | null | CATALYTIC ACTIVITY: Reaction=2 H2O + NH4(+) + 6 oxidized [2Fe-2S]-[ferredoxin] = 8 H(+) + nitrite + 6 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:18041, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:28938, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.7.7.1; Evidence={ECO:0000269|PubMed:11267765}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.6 mM for nitrite {ECO:0000269|PubMed:11267765}; KM=1.9 mM for methyl viologen {ECO:0000269|PubMed:11267765}; Vmax=4.1 umol/min/mg enzyme with nitrite as substrate {ECO:0000269|PubMed:11267765}; Vmax=1.7 umol/min/mg enzyme with methyl viologen as substrate {ECO:0000269|PubMed:11267765}; Note=In the presence of 3.2 M NaCl.; | PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation). {ECO:0000305|PubMed:16182473}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 at 60 degrees Celsius. At 40 degrees Celsius (temperature of the natural environment for H.mediterranei) the optimum pH is 6.5. {ECO:0000269|PubMed:11267765}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:11267765}; | FUNCTION: Catalyzes the reduction of nitrite to ammonium in the nitrate assimilation pathway, using ferredoxin as the electron donor. Can use reduced methyl viologen but neither NADPH nor NADH as electron donors. {ECO:0000269|PubMed:11267765}. | Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei) |
I3R9M8 | NARH_HALMT | MSTDSDAETVDLADGVDHQVAMVMDLNKCIGCQTCTVACKSLWTEGGGRDYMYWNNVETKPGKGYPRNWEESGGGWKSSEHKERKPGQIPDKEDYGDAWEFNHEEIMYNGSDRPLRPDSDPEWGPNWDEDQGTGEYPNSYYFYLPRICNHCTHPSCVEACPRKAIYKREEDGIVLIDQERCRGYRYCVEGCPYKKVYYNATQKTSEKCIFCYPRIEGEGPDGKTFAPACAEDCPPQLRLVGFLDDEQGPIHKLVEEYEVALPLHPEYQTQPNVYYIPPFAPPQHSEDGESVDVDRIPRNYLEELFGERVHDALDTIEREREKVNRGGGSELLDMLTDTNPARKFRLEVFDDD | 1.7.5.1 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P11349}; Note=Binds 3 [4Fe-4S] clusters per subunit. {ECO:0000250|UniProtKB:P11349}; COFACTOR: Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250|UniProtKB:P11349}; Note=Binds 1 [3Fe-4S] cluster per subunit. {ECO:0000250|UniProtKB:P11349}; | anaerobic respiration [GO:0009061]; nitrate assimilation [GO:0042128] | periplasmic space [GO:0042597]; plasma membrane [GO:0005886] | 4 iron, 4 sulfur cluster binding [GO:0051539]; electron transfer activity [GO:0009055]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491] | PF13247; | 3.30.70.20; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15342113, ECO:0000305|PubMed:17888006}; Peripheral membrane protein {ECO:0000269|PubMed:15342113, ECO:0000269|PubMed:17888006}; Extracellular side {ECO:0000269|PubMed:15342113, ECO:0000269|PubMed:17888006}. Note=Proposed to be coexported with the Tat system-dependent alpha subunit. | CATALYTIC ACTIVITY: Reaction=a quinol + nitrate = a quinone + H2O + nitrite; Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.7.5.1; Evidence={ECO:0000269|PubMed:15342113}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.82 mM for nitrate {ECO:0000269|PubMed:15342113}; KM=0.25 mM for methyl viologen {ECO:0000269|PubMed:15342113}; Note=Characterized with purified enzyme corresponding to a dimer of NarG and NarH.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.2. At 40 degrees Celsius (temperature of natural environment) the optimum pH is 7.9. {ECO:0000269|PubMed:15342113}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. {ECO:0000269|PubMed:15342113}; | FUNCTION: The respiratory membrane-bound nitrate reductase enzyme complex plays a role in generation of metabolic energy by using nitrate as a terminal electron acceptor during anaerobic conditions. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. {ECO:0000269|PubMed:15342113}. | Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei) |
I3R9M9 | NARG_HALMT | MSRNDASQLDDGETTAESPPDDQANDAPEVGDPPGDPVDADSGVSRRTFLEGIGVASLLGIGTSAASDDSLFQMGGLKPVDDPIGNYPYRDWEDLYREKWDWDSVSRSTHSVNCTGSCSWNVYVKNGQVWREEQSGDYPRFDESLPDPNPRGCQKGACYTDYVNADQRIKHPLKRVGERGEGKWKRISWDEALTEIAEHVVDEVEAGRYDAISGFTPIPAMSPVSFASGSRLVNLLGGVSHSFYDWYSDLPPGQPITWGTQTDNAESADWYNADYIIAWGSNINVTRIPDAKYFLESGYNGTKRVGVFTDYSQTAIHTDEWLSPDSGTDTALALGMAQTIVDEGLYDEAHLKEQTDMPLLVRQDTGKFLRASDVPSVNTDADRPEWMLLMLDSNGRIREAPGSLGERDGQKDYSKSIELDFDPQLDGETTVQTQSGRVQVRTVWAELRDELANWDPEMVHEETTVGKETYQRIAREFAEADKAKIIQGKGVNDWYHNDLGNRALQLLVTLTGNLGEQGTGLDHYVGQEKIWTFHGWKTLSFPTGKVRGVPTTLWTYYHAGILDNTDPDTAAKIRESIDKGWMPVYPEERDNGSRPDPTTMFVWRGNYFNQAKGNVAVEEQLWPKLDLVVDINFRMDSTAMYSDIVLPTASHYEKHDLSMTDMHTYVHPFTPAVEPLGESKTDWQIFRELAQKIQEVATERGVEPISDRKFDREIDLQSVYDDYVRDWETGEEGALAEDRAACEYILEHSEESNPADSDEQITFADTVEQPQRLLEAGDHWTSDIEDGEAYAPWKDFVQDKNPWPTVTGRQQYYIDHDWFLELGEELPTHKEGPENTGGDYPMEYNTPHGRWAIHSTWRDSEKLLRLQRGEPLLYLHPEDAEERGIEDGDSVEVFNDLAEVELQAKIYPSSQRGTARMYFAWERFQFDSDSNFNSLVPMYMKPTQLVQYPEDSGEHLHFFPNYWGPTGVNSDVRVDVRKAGGGDE | 1.7.5.1 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250}; COFACTOR: Name=Mo-bis(molybdopterin guanine dinucleotide); Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250}; Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit. {ECO:0000250}; | anaerobic respiration [GO:0009061]; nitrate assimilation [GO:0042128] | plasma membrane [GO:0005886] | 4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; molybdopterin cofactor binding [GO:0043546]; oxidoreductase activity [GO:0016491] | PF00384;PF01568; | 3.40.50.12440; | Prokaryotic molybdopterin-containing oxidoreductase family | PTM: Exported by the Tat system. {ECO:0000269|PubMed:17888006}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15342113, ECO:0000305|PubMed:17888006}; Peripheral membrane protein {ECO:0000269|PubMed:15342113, ECO:0000269|PubMed:17888006}; Extracellular side {ECO:0000269|PubMed:15342113, ECO:0000269|PubMed:17888006}. | CATALYTIC ACTIVITY: Reaction=a quinol + nitrate = a quinone + H2O + nitrite; Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.7.5.1; Evidence={ECO:0000269|PubMed:15342113}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.82 mM for nitrate {ECO:0000269|PubMed:15342113}; KM=0.25 mM for methyl viologen {ECO:0000269|PubMed:15342113}; Note=Characterized with purified enzyme corresponding to a dimer of NarG and NarH.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.2. At 40 degrees Celsius (temperature of natural environment) the optimum pH is 7.9. {ECO:0000269|PubMed:15342113}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. {ECO:0000269|PubMed:15342113}; | FUNCTION: The respiratory membrane-bound nitrate reductase enzyme complex plays a role in generation of metabolic energy by using nitrate as a terminal electron acceptor during anaerobic conditions. The alpha chain is the actual site of nitrate reduction. {ECO:0000269|PubMed:15342113}. | Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei) |
I3SL57 | HO1_LOTJA | MASATVVSQIQSLYIIKPRLSPPPPPHRQFRSIYFPTTRLLQQHRFRQMKSVVIVPATAAETARKRYPGESKGFVEEMRFVAMKLHTKDQAKEGEKEVTEPEEKAVTKWEPTVDGYLKFLVDSKVVYDTLEKIVQDATHPSYAEFRNTGLERSASLAKDLEWFKEQGYTIPQPSSPGLNYAQYLRDLSQNDPQAFICHFYNIYFAHSAGGRMIGKKIAGELLNNKGLEFYKWDGDLSQLLQNVRDKLNKVAEQWTREEKNHCLEETEKSFKWSGEILRLILS | 1.14.14.18 | null | biological process involved in interaction with symbiont [GO:0051702]; heme catabolic process [GO:0042167]; heme oxidation [GO:0006788]; nodulation [GO:0009877]; photosynthesis [GO:0015979]; phytochromobilin biosynthetic process [GO:0010024]; response to absence of light [GO:0009646]; response to nitrate [GO:0010167]; response to symbiotic bacterium [GO:0009609] | chloroplast [GO:0009507]; plastid [GO:0009536] | heme oxygenase (decyclizing) activity [GO:0004392] | PF01126; | 1.20.910.10; | Heme oxygenase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. Plastid {ECO:0000269|PubMed:37329247}. Note=Localized to the plastids of uninfected interstitial cells (UC) within root nodules, but absent from infected cells (IC) plastids. {ECO:0000269|PubMed:37329247}. | CATALYTIC ACTIVITY: Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:29033, ChEBI:CHEBI:57618, ChEBI:CHEBI:57991, ChEBI:CHEBI:58210, ChEBI:CHEBI:60344; EC=1.14.14.18; Evidence={ECO:0000269|PubMed:37329247}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21765; Evidence={ECO:0000269|PubMed:37329247}; | null | null | null | null | FUNCTION: Key enzyme in the synthesis of the chromophore of the phytochrome family of plant photoreceptors (By similarity). Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO) (PubMed:37329247). Produces specifically the biliverdin IX-alpha isomer (By similarity). Can form complex with heme, is ferredoxin-dependent and its activity is increased in the presence of ascorbate (By similarity). May affect the plastid-to-nucleus signaling pathway by perturbing tetrapyrrole synthesis (By similarity). The plastid-to-nucleus signal plays an important role in the coordinated expression of both nuclear- and chloroplast-localized genes that encode photosynthesis-related proteins (By similarity). Required for efficient symbiotic nitrogen fixation (SNF) in root nodules (PubMed:37329247). Responsible for heme catabolism in uninfected nodule interstitial cells (UC), preventing superoxide production under stressful conditions (e.g. nitrate exposure and darkness) and catalyzing biliverdin (BV) production in senescing green nodules (PubMed:37329247). {ECO:0000250|UniProtKB:O48782, ECO:0000269|PubMed:37329247}. | Lotus japonicus (Lotus corniculatus var. japonicus) |
I3V6A7 | SOMT1_PAPSO | MATNGEIFNTYGHNRQTATVTKITASNESSNGVCYLSETANLGKLICIPMALRAAMELNVFQLISKFGTDAKVSASEIASKMPNAKNNPEAAMYLDRILRLLGASSILSVSTTKKSINRGGDDVVVHEKLYGLTNSSCCLVPRQEDGVSLVEELLFTSDKVVVDSFFKLKCVVEEKDSVPFEVAHGAKIFEYAATEPRMNQVFNDGMAVFSIVVFEAVFRFYDGFLDMKELLDVGGGIGTSVSKIVAKYPLIRGVNFDLPHVISVAPQYPGVEHVAGDMFEEVPKGQNMLLKWVLHDWGDERCVKLLKNCWNSLPVGGKVLIIEFVLPNELGNNAESFNALIPDLLLMALNPGGKERTISEYDDLGKAAGFIKTIPIPISNGLHVIEFHK | 2.1.1.-; 2.1.1.117; 2.1.1.89 | null | aromatic compound biosynthetic process [GO:0019438]; benzyl isoquinoline alkaloid biosynthetic process [GO:0009708]; methylation [GO:0032259] | null | (S)-scoulerine 9-O-methyltransferase activity [GO:0030777]; methyltransferase activity [GO:0008168]; O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; tetrahydrocolumbamine 2-O-methyltransferase activity [GO:0030762] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family, COMT subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(S)-scoulerine + S-adenosyl-L-methionine = (S)-tetrahydrocolumbamine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:23808, ChEBI:CHEBI:15378, ChEBI:CHEBI:17129, ChEBI:CHEBI:17772, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.117; Evidence={ECO:0000269|PubMed:22535422, ECO:0000269|PubMed:22653730, ECO:0000269|Ref.5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23809; Evidence={ECO:0000305|PubMed:22535422}; CATALYTIC ACTIVITY: Reaction=(S)-tetrahydrocolumbamine + S-adenosyl-L-methionine = (S)-tetrahydropalmatine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:22536, ChEBI:CHEBI:15378, ChEBI:CHEBI:16563, ChEBI:CHEBI:17772, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.89; Evidence={ECO:0000269|PubMed:22535422}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22537; Evidence={ECO:0000305|PubMed:22535422}; CATALYTIC ACTIVITY: Reaction=(S)-norreticuline + S-adenosyl-L-methionine = (S)-norcodamine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:22180, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143271, ChEBI:CHEBI:143273; Evidence={ECO:0000269|PubMed:22535422}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22181; Evidence={ECO:0000305|PubMed:22535422}; CATALYTIC ACTIVITY: Reaction=(S)-reticuline + S-adenosyl-L-methionine = (S)-codamine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:59532, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:57873, ChEBI:CHEBI:59789, ChEBI:CHEBI:143148; Evidence={ECO:0000269|PubMed:22535422}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59533; Evidence={ECO:0000305|PubMed:22535422}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=28.5 uM for (S)-scoulerine {ECO:0000269|PubMed:22535422}; KM=70.3 uM for (S)-reticuline {ECO:0000269|PubMed:22535422}; KM=19 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:22535422}; Vmax=2036 nmol/min/mg enzyme with (S)-scoulerine as substrate {ECO:0000269|PubMed:22535422}; Vmax=184.4 nmol/min/mg enzyme with (S)-reticuline as substrate {ECO:0000269|PubMed:22535422}; Vmax=1290 nmol/min/mg enzyme with S-adenosyl-L-methionine as substrate {ECO:0000269|PubMed:22535422}; | PATHWAY: Alkaloid biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Methyltransferase involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine (PubMed:22535422, PubMed:22653730, PubMed:29610307). Catalyzes the conversion of (S)-scoulerine to (S)-tetrahydrocolumbamine (PubMed:22535422, PubMed:22653730). Can convert (S)-tetrahydrocolumbamine to tetrahydropalmatine (PubMed:22535422). Can convert (S)-norreticuline to (S)-norcodamine (PubMed:22535422). Can convert (S)-reticuline to (S)-codamine (PubMed:22535422). Substrate preference is (S)-scoulerine > (S)-tetrahydrocolumbamine > (S)-norreticuline > (S)-reticuline (PubMed:22535422). {ECO:0000269|PubMed:22535422, ECO:0000269|PubMed:22653730, ECO:0000269|PubMed:29610307}. | Papaver somniferum (Opium poppy) |
I3VE74 | HCMB_AQUTE | MDQTPIRVLLAKVGLDGHDRGVKVVARALRDAGMDVIYSGLHRTPEEVVNTAIQEDVDVLGVSLLSGVQLTVFPKIFKLLDERGAGDLIVIAGGVMPDEDAAAIRKLGVREVLLQDTPPQAIIDSIRSLVAARGAR | 5.4.99.64 | COFACTOR: Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; Evidence={ECO:0000269|PubMed:25720495}; | null | null | cobalamin binding [GO:0031419]; isomerase activity [GO:0016853]; metal ion binding [GO:0046872] | PF02310; | 3.40.50.280; | Acyl-CoA mutase small subunit family | null | null | CATALYTIC ACTIVITY: Reaction=2-hydroxyisobutanoyl-CoA = (3S)-3-hydroxybutanoyl-CoA; Xref=Rhea:RHEA:49592, ChEBI:CHEBI:57316, ChEBI:CHEBI:131780; EC=5.4.99.64; Evidence={ECO:0000269|PubMed:22433853, ECO:0000269|PubMed:25720495}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49593; Evidence={ECO:0000269|PubMed:22433853}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=128 uM for (S)-3-hydroxybutyryl-CoA {ECO:0000269|PubMed:22433853}; KM=104 uM for 2-hydroxyisobutyryl-CoA {ECO:0000269|PubMed:22433853}; KM=1660 uM for (R)-3-hydroxybutyryl-CoA {ECO:0000269|PubMed:22433853}; KM=3340 uM for butyryl-CoA {ECO:0000269|PubMed:22433853}; KM=550 uM for isobutyryl-CoA {ECO:0000269|PubMed:22433853}; KM=374 uM for pivalyl-CoA {ECO:0000269|PubMed:25720495}; KM=288 uM for isovaleryl-CoA {ECO:0000269|PubMed:25720495}; Vmax=140 nmol/min/mg enzyme with (S)-3-hydroxybutyryl-CoA as substrate {ECO:0000269|PubMed:22433853}; Vmax=36 nmol/min/mg enzyme with 2-hydroxyisobutyryl-CoA as substrate {ECO:0000269|PubMed:22433853}; Vmax=2.4 nmol/min/mg enzyme with (R)-3-hydroxybutyryl-CoA as substrate {ECO:0000269|PubMed:22433853}; Vmax=2.4 nmol/min/mg enzyme with butyryl-CoA as substrate {ECO:0000269|PubMed:22433853}; Vmax=0.67 nmol/min/mg enzyme with isobutyryl-CoA as substrate {ECO:0000269|PubMed:22433853}; Vmax=11.8 nmol/min/mg enzyme with pivalyl-CoA as substrate {ECO:0000269|PubMed:25720495}; Vmax=8.2 nmol/min/mg enzyme with isovaleryl-CoA as substrate {ECO:0000269|PubMed:25720495}; Note=kcat is 12 min(-1) with (S)-3-hydroxybutyryl-CoA as substrate. kcat is 3.0 min(-1) with 2-hydroxyisobutyryl-CoA as substrate. kcat is 0.20 min(-1) with (R)-3-hydroxybutyryl-CoA as substrate. kcat is 0.20 min(-1) with butyryl-CoA as substrate. kcat is 0.06 min(-1) with isobutyryl-CoA as substrate (PubMed:22433853). kcat is 0.98 min(-1) with pivalyl-CoA as substrate. kcat is 0.68 min(-1) with isovaleryl-CoA as substrate (PubMed:25720495). {ECO:0000269|PubMed:22433853, ECO:0000269|PubMed:25720495}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.6. {ECO:0000269|PubMed:22433853}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:22433853}; | FUNCTION: Together with HcmA, catalyzes the isomerization of 2-hydroxyisobutyryl-CoA and 3-hydroxybutyryl-CoA. Is specific for 2-hydroxyisobutyryl-CoA and (S)-3-hydroxybutyryl-CoA, and shows only very low activity with (R)-3-hydroxybutyryl-CoA, isobutyryl-CoA and butyryl-CoA (PubMed:22433853, PubMed:25720495). In vitro, can isomerize pivalyl-CoA and isovaleryl-CoA, with much lower efficiency (PubMed:25720495). Plays a central role in the degradation of substrates bearing a tert-butyl moiety, such as the fuel oxygenate methyl tert-butyl ether (MTBE) and its metabolites (PubMed:22433853). {ECO:0000269|PubMed:22433853, ECO:0000269|PubMed:25720495}. | Aquincola tertiaricarbonis |
I3VE77 | HCMA_AQUTE | MTWLEPQIKSQLQSERKDWEANEVGAFLKKAPERKEQFHTIGDFPVQRTYTAADIADTPLEDIGLPGRYPFTRGPYPTMYRSRTWTMRQIAGFGTGEDTNKRFKYLIAQGQTGISTDFDMPTLMGYDSDHPMSDGEVGREGVAIDTLADMEALLADIDLEKISVSFTINPSAWILLAMYVALGEKRGYDLNKLSGTVQADILKEYMAQKEYIYPIAPSVRIVRDIITYSAKNLKRYNPINISGYHISEAGSSPLQEAAFTLANLITYVNEVTKTGMHVDEFAPRLAFFFVSQGDFFEEVAKFRALRRCYAKIMKERFGARNPESMRLRFHCQTAAATLTKPQYMVNVVRTSLQALSAVLGGAQSLHTNGYDEAFAIPTEDAMKMALRTQQIIAEESGVADVIDPLGGSYYVEALTTEYEKKIFEILEEVEKRGGTIKLIEQGWFQKQIADFAYETALRKQSGQKPVIGVNRFVENEEDVKIEIHPYDNTTAERQISRTRRVRAERDEAKVQAMLDQLVAVAKDESQNLMPLTIELVKAGATMGDIVEKLKGIWGTYRETPVF | 5.4.99.64 | null | null | null | cobalamin binding [GO:0031419]; methylmalonyl-CoA mutase activity [GO:0004494] | PF01642; | 3.20.20.240; | Acyl-CoA mutase large subunit family | null | null | CATALYTIC ACTIVITY: Reaction=2-hydroxyisobutanoyl-CoA = (3S)-3-hydroxybutanoyl-CoA; Xref=Rhea:RHEA:49592, ChEBI:CHEBI:57316, ChEBI:CHEBI:131780; EC=5.4.99.64; Evidence={ECO:0000269|PubMed:22433853, ECO:0000269|PubMed:25720495}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49593; Evidence={ECO:0000269|PubMed:22433853}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=128 uM for (S)-3-hydroxybutyryl-CoA {ECO:0000269|PubMed:22433853}; KM=104 uM for 2-hydroxyisobutyryl-CoA {ECO:0000269|PubMed:22433853}; KM=1660 uM for (R)-3-hydroxybutyryl-CoA {ECO:0000269|PubMed:22433853}; KM=3340 uM for butyryl-CoA {ECO:0000269|PubMed:22433853}; KM=550 uM for isobutyryl-CoA {ECO:0000269|PubMed:22433853}; KM=374 uM for pivalyl-CoA {ECO:0000269|PubMed:25720495}; KM=288 uM for isovaleryl-CoA {ECO:0000269|PubMed:25720495}; Vmax=140 nmol/min/mg enzyme with (S)-3-hydroxybutyryl-CoA as substrate {ECO:0000269|PubMed:22433853}; Vmax=36 nmol/min/mg enzyme with 2-hydroxyisobutyryl-CoA as substrate {ECO:0000269|PubMed:22433853}; Vmax=2.4 nmol/min/mg enzyme with (R)-3-hydroxybutyryl-CoA as substrate {ECO:0000269|PubMed:22433853}; Vmax=2.4 nmol/min/mg enzyme with butyryl-CoA as substrate {ECO:0000269|PubMed:22433853}; Vmax=0.67 nmol/min/mg enzyme with isobutyryl-CoA as substrate {ECO:0000269|PubMed:22433853}; Vmax=11.8 nmol/min/mg enzyme with pivalyl-CoA as substrate {ECO:0000269|PubMed:25720495}; Vmax=8.2 nmol/min/mg enzyme with isovaleryl-CoA as substrate {ECO:0000269|PubMed:25720495}; Note=kcat is 12 min(-1) with (S)-3-hydroxybutyryl-CoA as substrate. kcat is 3.0 min(-1) with 2-hydroxyisobutyryl-CoA as substrate. kcat is 0.20 min(-1) with (R)-3-hydroxybutyryl-CoA as substrate. kcat is 0.20 min(-1) with butyryl-CoA as substrate. kcat is 0.06 min(-1) with isobutyryl-CoA as substrate (PubMed:22433853). kcat is 0.98 min(-1) with pivalyl-CoA as substrate. kcat is 0.68 min(-1) with isovaleryl-CoA as substrate (PubMed:25720495). {ECO:0000269|PubMed:22433853, ECO:0000269|PubMed:25720495}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.6. {ECO:0000269|PubMed:22433853}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:22433853}; | FUNCTION: Together with HcmB, catalyzes the isomerization of 2-hydroxyisobutyryl-CoA and 3-hydroxybutyryl-CoA. Is specific for 2-hydroxyisobutyryl-CoA and (S)-3-hydroxybutyryl-CoA, and shows only very low activity with (R)-3-hydroxybutyryl-CoA, isobutyryl-CoA and butyryl-CoA (PubMed:22433853, PubMed:25720495). In vitro, can isomerize pivalyl-CoA and isovaleryl-CoA, with much lower efficiency (PubMed:25720495). Plays a central role in the degradation of substrates bearing a tert-butyl moiety, such as the fuel oxygenate methyl tert-butyl ether (MTBE) and its metabolites (PubMed:22433853). {ECO:0000269|PubMed:22433853, ECO:0000269|PubMed:25720495}. | Aquincola tertiaricarbonis |
I4AY86 | NOTF_ASPVE | MTAPELRAPAGHPQEPPARSSPAQALSSYHHFPTSDQERWYQETGSLCSRFLEAGQYGLHQQYQFMFFFMHHLIPALGPYPQKWRSTISRSGLPIEFSLNFQKGSHRLLRIGFEPVNFLSGSSQDPFNRIPIADLLAQLARLQLRGFDTQCFQQLLTRFQLSLDEVRQLPPDDQPLKSQGAFGFDFNPDGAILVKGYVFPYLKAKAAGVPVATLIAESVRAIDADRNQFMHAFSLINDYMQESTGYNEYTFLSCDLVEMSRQRVKIYGAHTEVTWAKIAEMWTLGGRLIEEPEIMEGLARLKQIWSLLQIGEGSRAFKGGFDYGKASATDQIPSPIIWNYEISPGSSFPVPKFYLPVHGENDLRVARSLAQFWDSLGWSEHACAYPDMLQQLYPDLDVSRTSRLQSWISYSYTAKKGVYMSVYFHSQSTYLWEED | 2.5.1.109 | null | alkaloid metabolic process [GO:0009820] | null | prenyltransferase activity [GO:0004659] | PF11991; | null | Tryptophan dimethylallyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=brevianamide F + dimethylallyl diphosphate = deoxybrevianamide E + diphosphate; Xref=Rhea:RHEA:35943, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:64530, ChEBI:CHEBI:72948; EC=2.5.1.109; Evidence={ECO:0000269|PubMed:22660767}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35944; Evidence={ECO:0000269|PubMed:22660767}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=32 uM for brevianamide F {ECO:0000269|PubMed:22660767}; KM=98 uM for Dimethylallyl diphosphate (DMAPP) {ECO:0000269|PubMed:22660767}; KM=32 uM for cyclo-L-Trp-L-Pro {ECO:0000269|PubMed:22660767}; KM=82 uM for cyclo-L-Trp-D-Pro {ECO:0000269|PubMed:22660767}; KM=709 uM for cyclo-D-Trp-D-Pro {ECO:0000269|PubMed:22660767}; KM=2906 uM for cyclo-D-Trp-L-Pro {ECO:0000269|PubMed:22660767}; KM=942 uM for cyclo-L-Trp-L-Ala {ECO:0000269|PubMed:22660767}; KM=793 uM for cyclo-L-Trp-D-Ala {ECO:0000269|PubMed:22660767}; KM=1318 uM for cyclo-D-Trp-D-Ala {ECO:0000269|PubMed:22660767}; KM=139 uM for cyclo-D-Trp-L-Ala {ECO:0000269|PubMed:22660767}; KM=1300 uM for cyclo-L-Trp-Gly {ECO:0000269|PubMed:22660767}; KM=106 uM for cyclo-L-Trp-L-Leu {ECO:0000269|PubMed:22660767}; KM=94 uM for cyclo-L-Trp-L-Phe {ECO:0000269|PubMed:22660767}; KM=2148 uM for cyclo-L-Trp-L-Tyr {ECO:0000269|PubMed:22660767}; | PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:22660767}. | null | null | FUNCTION: Deoxybrevianamide E synthase; part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core (PubMed:23213353). The first step of notoamide biosynthesis involves coupling of L-proline and L-tryptophan by the bimodular NRPS notE', to produce cyclo-L-tryptophan-L-proline called brevianamide F (Probable). The reverse prenyltransferase notF' then acts as a deoxybrevianamide E synthase and converts brevianamide F to deoxybrevianamide E via reverse prenylation at C-2 of the indole ring leading to the bicyclo[2.2.2]diazaoctane core (PubMed:22660767). Deoxybrevianamide E is further hydroxylated at C-6 of the indole ring, likely catalyzed by the cytochrome P450 monooxygenase notG', to yield 6-hydroxy-deoxybrevianamide E (Probable). 6-hydroxy-deoxybrevianamide E is a specific substrate of the prenyltransferase notC' for normal prenylation at C-7 to produce 6-hydroxy-7-prenyl-deoxybrevianamide, also called notoamide S (Probable). As the proposed pivotal branching point in notoamide biosynthesis, notoamide S can be diverted to notoamide E through an oxidative pyran ring closure putatively catalyzed by either notH' cytochrome P450 monooxygenase or the notD' FAD-linked oxidoreductase (Probable). This step would be followed by an indole 2,3-epoxidation-initiated pinacol-like rearrangement catalyzed by the notB' FAD-dependent monooxygenase leading to the formation of notoamide C and notoamide D (Probable). On the other hand notoamide S is converted to notoamide T by notH' (or notD'), a bifunctional oxidase that also functions as the intramolecular Diels-Alderase responsible for generation of (-)-notoamide T (Probable). To generate antipodal (+)-notoaminide T, notH (or notD) in Aspergillus strain MF297-2 is expected to catalyze a Diels-Alder reaction leading to the opposite stereochemistry (Probable). The remaining oxidoreductase notD' (or notH') likely catalyzes the oxidative pyran ring formation to yield (-)-stephacidin A (Probable). The FAD-dependent monooxygenase notI' is highly similar to notB' and is predicted to catalyze a similar conversion from (-)-stephacidin A to (+)-notoamide B via the 2,3-epoxidation of (-)-stephacidin A followed by a pinacol-type rearrangement (Probable). Finally, it remains unclear which enzyme could be responsible for the final hydroxylation steps leading to notoamide A and sclerotiamide (Probable). {ECO:0000269|PubMed:22660767, ECO:0000269|PubMed:23213353, ECO:0000305|PubMed:23213353}. | Aspergillus versicolor |
I4CHP3 | VSPI_GLOHA | IIGGDECNINEHRFLVALYTSRSRTLFCGGTLINQEWVLTAAHCDRKNFRIKLGMHSKKVPNEDEQTRVPKEKFFCLSSKNYTLWDKDIMLIRLDSPVKNSKHIAPFSLPSSPPSVGSVCRIMGWGRISPTEGTYPDVPHCVNINLLEYEMCRAPYPEFELPATSRTLCAGILEGGKDTCKGDSGGPLICNGQFQGIASWGDDPCAQPHKPAAYTKVFDHLDWIENIIAGNTDASCPP | 3.4.21.- | null | proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | PTM: N-glycosylated at Asn-81 by a disaccharide composed of two N-acetylglucosamine (NAG). The presence of this N-glycan deforms the enzyme and Removing the carbohydrate moiety increases the esterase activity, but induces a complete loss of contractile response on mouse thoracic aorta. {ECO:0000269|PubMed:23052203}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23052203}. | null | null | null | null | null | FUNCTION: Thrombin-like enzyme that shows fibrinogenolytic activity against both the Aalpha (FGA) and Bbeta (FGB) chains of bovine fibrinogen. This enzyme has poor esterolytic activity upon BAEE substrate. It induces mouse thoracic aortic ring contraction with EC(50)=147 nmol/L. It shows vasoconstrictor effects that are independent of the enzymatic activity, but related to the release of calcium ions form the calcium store, potentially through the activation of ryanodine receptors. {ECO:0000269|PubMed:23052203}. | Gloydius halys (Chinese water mocassin) (Agkistrodon halys) |
I4DST8 | TCEA1_TULGE | MSVASFFSSLPARPFGYKDGRGRTGMVPTTDIGRRMVKPPVLACRPIESNTYHGSVTSVFLTKSSRSPSPSLSPTPTALDDEIVLDLKPFLIIYKSGRIERFLGTTVIPACPEVATKDVVIDPATGVSVRLYLPNVVDLPSKKLPVLVYFHGGGFVIENTGSPNYHNYLTLLAAKAGVLIVSINYRLAPEYPLPASYDDCMAGFNWVVSHSAGPALEPWLAQHGDFSQILLSGDSAGGNVTHYVAMRADAGVIEGVAIVHPYFLGSEPVGNEINDPANIEFHDKLWRLAAPDTEGLDDPLINPVAPGAPSLAGLKCKRAVVFVAGNDFLVERGRMYYEALVKSGWRGEAELVQHEGVGHVFHLSDYSGDISVAMMTKLIAFLKGE | 4.2.99.22 | null | defense response [GO:0006952] | chloroplast [GO:0009507] | hydrolase activity [GO:0016787]; lyase activity [GO:0016829] | PF07859; | 3.40.50.1820; | AB hydrolase superfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:22474185}. | CATALYTIC ACTIVITY: Reaction=6-tuliposide A = D-glucose + tulipalin A; Xref=Rhea:RHEA:36071, ChEBI:CHEBI:4167, ChEBI:CHEBI:72781, ChEBI:CHEBI:104120; EC=4.2.99.22; Evidence={ECO:0000269|PubMed:22474185}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18 mM for 6-tuliposide A {ECO:0000269|PubMed:22474185}; KM=71 mM for 6-tuliposide B {ECO:0000269|PubMed:22474185}; Note=kcat is 2800 sec(-1) with 6-tuliposide A as substrate. kcat is 510 sec(-1) with 6-tuliposide B as substrate.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:22474185}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35-45 degrees Celsius. {ECO:0000269|PubMed:22474185}; | FUNCTION: Lactone-forming carboxylesterases, specifically catalyzing intramolecular transesterification, but not hydrolysis. Involved in the biosynthesis of tulipalins, defensive chemicals that show antimicrobial activities against a broad range of strains of bacteria and fungi. Substrates are 6-tuliposide A > 6-tuliposide B. {ECO:0000269|PubMed:22474185}. | Tulipa gesneriana (Garden tulip) |
I4DST9 | TCEA2_TULGE | MSVASFFSSLPARPFGYKDGRGRTGMVSTTDIGRRMVKPPVLACRPIESNTYHGSVFLTKSSRSPSPSLSPTPTALDDEIVLDLKPFLIIYKSGRIERFLGTTVIPACPEVATKDVVIDPATGVSVRLYLPNVVDLPSKKLPVLVYFHGGGFVIENTGSPNYHNYLTLLAAKAGVLIVSINYRLAPEYPLPASYDDCMAGFNWVVSHSAGPALEPWLAQHGDFSQILLSGDSAGGNVTHYVAMRADAGVIEGVAIVHPYFLGSEPVGNEINDPANIEFHDKLWRLAAPDTEGLDDPLINPVAPGAPILAGLKCKRAVVFVAGNDFLVERGRMYYEALVKSGWGGEAELVQHEGVGHVFHLSDYSGDISVAMMTKLIAFLKGE | 4.2.99.22 | null | defense response [GO:0006952] | chloroplast [GO:0009507] | hydrolase activity [GO:0016787]; lyase activity [GO:0016829] | PF07859; | 3.40.50.1820; | AB hydrolase superfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=6-tuliposide A = D-glucose + tulipalin A; Xref=Rhea:RHEA:36071, ChEBI:CHEBI:4167, ChEBI:CHEBI:72781, ChEBI:CHEBI:104120; EC=4.2.99.22; Evidence={ECO:0000269|PubMed:22474185}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14 mM for 6-tuliposide A {ECO:0000269|PubMed:22474185}; KM=72 mM for 6-tuliposide B {ECO:0000269|PubMed:22474185}; Note=kcat is 2400 sec(-1) with 6-tuliposide A as substrate. kcat is 480 sec(-1) with 6-tuliposide B as substrate.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:22474185}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35-45 degrees Celsius. {ECO:0000269|PubMed:22474185}; | FUNCTION: Lactone-forming carboxylesterases, specifically catalyzing intramolecular transesterification, but not hydrolysis. Involved in the biosynthesis of tulipalins, defensive chemicals that show antimicrobial activities against a broad range of strains of bacteria and fungi. Substrates are 6-tuliposide A > 6-tuliposide B. {ECO:0000269|PubMed:22474185}. | Tulipa gesneriana (Garden tulip) |
I6L8L6 | PA2H1_BOTBZ | SLFQLGKMILQETGKNPAASYGAYGCNCGVLGRGKPKDATDRCCYVHKCCKKKLTGCDPKKDRYSYSWKDKTIVCGENNPCLKELCECDKAVAICLRENLNTYNKKYRYHLKPFCKKADPC | null | null | arachidonic acid secretion [GO:0050482]; defense response to bacterium [GO:0042742]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, K49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18602430}. | null | null | null | null | null | FUNCTION: Snake venom phospholipase A2 homolog that lacks enzymatic activity. Is myotoxic and displays edema-inducing activities in mouse paw (PubMed:18602430). Also displays cytotoxic activity against some cell lines, and antimicrobial activities against E.coli, C.albicans and Leishmania (PubMed:18602430). A model of myotoxic mechanism has been proposed: an apo Lys49-PLA2 is activated by the entrance of a hydrophobic molecule (e.g. fatty acid) at the hydrophobic channel of the protein leading to a reorientation of a monomer (PubMed:24145104). This reorientation causes a transition between 'inactive' to 'active' states, causing alignment of C-terminal and membrane-docking sites (MDoS) side-by-side and putting the membrane-disruption sites (MDiS) in the same plane, exposed to solvent and in a symmetric position for both monomers (PubMed:24145104). The MDoS region stabilizes the toxin on membrane by the interaction of charged residues with phospholipid head groups (PubMed:24145104). Subsequently, the MDiS region destabilizes the membrane with penetration of hydrophobic residues (PubMed:24145104). This insertion causes a disorganization of the membrane, allowing an uncontrolled influx of ions (i.e. calcium and sodium), and eventually triggering irreversible intracellular alterations and cell death (PubMed:24145104). {ECO:0000269|PubMed:18602430, ECO:0000305|PubMed:24145104}. | Bothrops brazili (Brazil's lancehead) |
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