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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C0HM55 | FSX1_UNCAX | MRRAALILAFVLFIGLSSATVTSADSITYNSGTSEFFDGDVFAIEVTADQSTDEIDIYLGASELSEKTDGEVNQDLSIEFTHQDSKLKYSTSTSDELRDIVTLTTYYEDGFDTEQDAIDAIKSDCYDLNQNGNGSGRYSRYYSVTSPVYDYEIYCFQKNEKLATPAYIDNPDEIFTAKAELQAGDKTIQSATLSNGDAGDGTVTDLGDSKISWNGNLDLGASEPENSRVIALYSNDFENGWRIGNKQSYEDYKTFIGGGDAYDLLIDWQDGTYTASEVEDELVNTDANQAVEEASSSTTDLVNAKVKDSSLDTGSFVYDTPELLSYPSFTVYVDAGENGYIEVTKPTGDPDIISTSSTEIKEGDEGTVTATVENVGDGEGEFSGRLSSCGEGFSIVDDQNTKNVGAGESVTYSFDVAFSSVSSESKEISGSCTFEVNGVESSDSTSVSVTGIQQSECNPGDQRREKNENDRWEIYTCQDNGLTYEYDVTCAEDEKAVAQGDNQFSCEKQDDDSGGGDNTGSDSGLFSNLFGGSGSGDLLTQVHTALSILAGLVAGFFGYRGARWIHGETDIKGGFKLESRNVSRVKRGSPVAGIVGAVLGFVVGYGVASVFHPVVQIIVVLGIAVGLYYFR | null | null | plasma membrane fusion [GO:0045026] | cell surface [GO:0009986]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872] | null | 2.60.40.10; | HAP2/GCS1 family, Fusexin 1 subfamily | null | SUBCELLULAR LOCATION: Cell surface {ECO:0000255|HAMAP-Rule:MF_00869, ECO:0000269|PubMed:35794124}. Cell membrane {ECO:0000255|HAMAP-Rule:MF_00869, ECO:0000305|PubMed:35794124}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00869}. | null | null | null | null | null | FUNCTION: Exhibits fusogenic activity (PubMed:35794124). Mediates cell-cell fusion in mammalian cells when present in both cells (bilateral fusion) (PubMed:35794124). {ECO:0000255|HAMAP-Rule:MF_00869, ECO:0000269|PubMed:35794124}. | Uncultured archaeon |
C0HM68 | 5BPIA_HETMG | GTPCKCHGYIGVYWFMLAGCGYNLSCPYFLGICCVKK | null | null | null | extracellular region [GO:0005576]; host cell postsynaptic membrane [GO:0035792]; nematocyst [GO:0042151] | acetylcholine receptor activator activity [GO:0030549]; acetylcholine receptor inhibitor activity [GO:0030550]; ion channel inhibitor activity [GO:0008200]; toxin activity [GO:0090729] | PF07936; | 2.20.20.10; | Sea anemone type 3 (BDS) potassium channel toxin family | PTM: Toxin occurs in two forms in the mucus, Hmg 1b-2 which is not oxidized and Hmg 1b-2 MetOx which is oxidized at Met-16. {ECO:0000269|PubMed:36287966}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:36287966}. Nematocyst {ECO:0000305|PubMed:36287966}. Note=Present in the mucus. {ECO:0000269|PubMed:36287966}. | null | null | null | null | null | FUNCTION: The non-oxidized toxin potentiates ACh-elicited current of human alpha-7/CHRNA7 nicotinic acetylcholine receptors (nAChR) (PubMed:36287966). Also able to bind T. californica muscle-type nAChRs (PubMed:36287966). {ECO:0000269|PubMed:36287966}.; FUNCTION: Forms an oxidized toxin derivative (Hmg 1b-2 MetOx) (PubMed:36287966). Able to bind T. californica muscle-type (alpha-1-beta-1-delta-epsilon (CHRNA1-CHRNB1-CHRND-CHRNE)) nAChRs (PubMed:36287966). Weakly and reversibly inhibits rat homomeric ASIC1 (isoform ASIC1a) (IC(50)=4.8 uM), and ASIC3 (By similarity). In vivo, induces an antihyperalgesic effect in the acid-induced muscle pain mice model (By similarity). Molecular modeling interaction with ASIC1a suggests that this peptide hinders the collapse of acidic pockets and stabilizes nonconducting channels state (By similarity). {ECO:0000250|UniProtKB:C0HL52, ECO:0000269|PubMed:36287966}. | Heteractis magnifica (Magnificent sea anemone) (Radianthus magnifica) |
C0K3N1 | TXVE_BITAR | MAAYLLAVAILFCIQGWPSGTVQGEVRPFMEVYQRSVCQPRETLVSILEEYPDKISKIFRPSCVAVLRCGGCCSDESLTCTSVGERTVELQVMQVTPKTLSSKIKVMKFREHTACECRPRSGSRVNIGKHKRSPEEGEREPSSPLTPGSL | null | null | induction of positive chemotaxis [GO:0050930]; positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of mast cell chemotaxis [GO:0060754]; positive regulation of protein phosphorylation [GO:0001934]; response to hypoxia [GO:0001666]; sprouting angiogenesis [GO:0002040]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; vascular endothelial growth factor signaling pathway [GO:0038084] | extracellular space [GO:0005615]; membrane [GO:0016020] | chemoattractant activity [GO:0042056]; growth factor activity [GO:0008083]; toxin activity [GO:0090729]; vascular endothelial growth factor receptor 1 binding [GO:0043183]; vascular endothelial growth factor receptor 2 binding [GO:0043184] | PF00341; | 2.10.90.10; | PDGF/VEGF growth factor family, Snake venom VEGF subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19208624}. | null | null | null | null | null | FUNCTION: Snake venom VEGFs that may contribute to venom dispersion and prey subjugation by inducing vascular permeability and hypotension. This protein induces an increase in capillary permeability after intradermal injection, as well as a drastic hypotensive effect after intravenous injection. The hypotension is mediated by nitric oxide (NO), which is produced by VEGF-activated endothelium NO synthase. Also induces angiogenesis in vitro, probably through VEGF receptor (KDR/VEGFR-2) signaling. {ECO:0000250|UniProtKB:P83942}. | Bitis arietans (African puff adder) |
C0KTJ6 | GATDH_CERSP | MDYRTVFRLDGACAAVTGAGSGIGLEICRAFAASGARLILIDREAAALDRAAQELGAAVAARIVADVTDAEAMTAAAAEAEAVAPVSILVNSAGIARLHDALETDDATWRQVMAVNVDGMFWASRAFGRAMVARGAGAIVNLGSMSGTIVNRPQFASSYMASKGAVHQLTRALAAEWAGRGVRVNALAPGYVATEMTLKMRERPELFETWLDMTPMGRCGEPSEIAAAALFLASPAASYVTGAILAVDGGYTVW | 1.1.1.406 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:7551050}; Note=Can use Mg(2+), Mn(2+), Ni(2+) or Co(2+). {ECO:0000269|PubMed:7551050}; | null | null | metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=galactitol + NAD(+) = H(+) + keto-L-tagatose + NADH; Xref=Rhea:RHEA:51688, ChEBI:CHEBI:15378, ChEBI:CHEBI:16813, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:134275; EC=1.1.1.406; Evidence={ECO:0000269|PubMed:7551050}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=240 mM for galactitol {ECO:0000269|PubMed:7551050}; KM=85 mM for D-threitol {ECO:0000269|PubMed:7551050}; KM=196 mM for (R,S)-1,2-propanediol {ECO:0000269|PubMed:15296184}; KM=49 mM for (R,S)-1,2-butanediol {ECO:0000269|PubMed:15296184}; KM=0.2 mM for 1,2-hexanediol {ECO:0000269|PubMed:7551050}; KM=1.4 mM for (R,S)-1,2-hexanediol {ECO:0000269|PubMed:15296184}; KM=0.5 mM for (R,S)-1,2,6-hexanetriol {ECO:0000269|PubMed:15296184}; KM=12 uM for NAD(+) (in the presence of 100 mM 1,2-hexanediol) {ECO:0000269|PubMed:7551050}; KM=62 mM for acetoin {ECO:0000269|PubMed:7551050}; KM=144 mM for L-erythrulose {ECO:0000269|PubMed:7551050}; KM=202 mM for hydroxyacetone {ECO:0000269|PubMed:15296184}; KM=48 mM for dihydroxyacetone {ECO:0000269|PubMed:7551050}; KM=26 mM for 1-hydroxy-2-butanone {ECO:0000269|PubMed:15296184}; KM=1.4 mM for 2,3-hexanedione {ECO:0000269|PubMed:15296184}; KM=4.2 mM for 3,4-hexanedione {ECO:0000269|PubMed:15296184}; KM=4 uM for NADH (in the presence of 300 mM acetoin) {ECO:0000269|PubMed:7551050}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 10.5 with 1,2-hexanediol as substrate. Optimum pH is 4.0 with acetoin as substrate. {ECO:0000269|PubMed:7551050}; | null | FUNCTION: Catalyzes the interconversion of galactitol to the rare sugar L-tagatose (PubMed:7551050). Shows activity with a wide range of substrates, and catalyzes the oxidation of a variety of polyvalent aliphatic alcohols and polyols to the corresponding ketones and ketoses, respectively, and in the reverse reaction, it reduces ketones with high stereoselectivity yielding the corresponding S-configurated alcohols (PubMed:15296184, PubMed:7551050). Shows high activity with D-threitol, xylitol, 1,2-hexanediol, 1,2-pentanediol, 2-hexanol, L-erythrulose, D-ribulose and acetoin (PubMed:7551050). Specific for NAD(+) (PubMed:7551050). {ECO:0000269|PubMed:15296184, ECO:0000269|PubMed:7551050}. | Cereibacter sphaeroides (Rhodobacter sphaeroides) |
C0L2T8 | VM2C1_CRODO | MIQVLLVTICLAAFPYQGSSIILESGNVNDYEVIYPRKVTALPKGAVQPKYEDTMQYELKVNGQPVVLHLEKNKGLFSKDYSETHYSPDGRKITTNPSVEDHCYYHGRIENDADSTASISACNGLKGHFKLQGEMYIIEPLELSDSEDHAVFKLENVEKEDEAPKMCGVTQNWESNEPIKKASHLNLNPEHQRYVEIVIVVDHGMFTKYNGDSDKIRQRVHQMVNIMKESYRYMYIDISLAGIEIWSNKDLINVQPAAPNTLKSFGEWRETDLPKRKSHDNAQLLTSIDFNGQTIGIANIGAICDPKPSTRVVQDHSKINLRVALTMTHELSHNLGIHHDTGSCSCSGYSCIMSPVISDEPSKYFSDCSYIQCWNFIMNQKPQCILKKPLRTDTVSTPVSGNELLEARIECDCGSIENPCCYATTCKLRPGSQCAEGMCCDQCRFMKKGTVCRVSLVNKNDDTCTGQSADCPRNVLYG | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O93523}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O93523}; | collagen catabolic process [GO:0030574]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | PF00200;PF01562;PF01421; | 3.40.390.10;4.10.70.10; | Venom metalloproteinase (M12B) family, P-II subfamily, P-IIa sub-subfamily | null | SUBCELLULAR LOCATION: [Snake venom metalloproteinase]: Secreted {ECO:0000305|PubMed:19230843}.; SUBCELLULAR LOCATION: [Disintegrin Cdc]: Secreted {ECO:0000269|PubMed:30377432}. | null | null | null | null | null | FUNCTION: [Snake venom metalloproteinase]: Snake venom zinc metalloproteinase that causes hemorrhage by provoking the degradation of the sub-endothelial matrix proteins (fibronectin, laminin, type IV collagen, nidogen, and gelatins). {ECO:0000250|UniProtKB:P34182}.; FUNCTION: [Disintegrin Cdc]: Displays low cytotoxicity. In vitro, inhibits cancer cell migration (human breast cancer cell line MDA-MB-231) with a significant rate after 24 hours of incubation. {ECO:0000269|PubMed:30377432}. | Crotalus durissus collilineatus (Brazilian rattlesnake) |
C0LGE0 | Y1765_ARATH | MIYLHRIYFIIVLFTLIFHGRLGFSDNNKLHEAEVRALKEIGKKLGKKDWDFNKDPCSGEGTWIVTTYTTKGFESNITCDCSFLPQNSSCHVIRIALKSQNLTGIVPPEFSKLRHLKVLDLSRNSLTGSIPKEWASMRLEDLSFMGNRLSGPFPKVLTRLTMLRNLSLEGNQFSGPIPPDIGQLVHLEKLHLPSNAFTGPLTEKLGLLKNLTDMRISDNNFTGPIPDFISNWTRILKLQMHGCGLDGPIPSSISSLTSLTDLRISDLGGKPSSFPPLKNLESIKTLILRKCKIIGPIPKYIGDLKKLKTLDLSFNLLSGEIPSSFENMKKADFIYLTGNKLTGGVPNYFVERNKNVDVSFNNFTDESSIPSHDCNRVTSNLVESFALGNKSHKGSTCFLQRMPCVHPKRYHLYKLYINCGGGEVKVDKEITYQADDEPKGASMYVLGANKRWALSSTGNFMDNDDDADEYTVQNTSRLSVNASSPSFGLYRTARVSPLSLTYYGICLGNGNYTVNLHFAEIIFTDDNTLYSLGKRLFDIYVQDQLVIKNFNIQEAARGSGKPIIKSFLVNVTDHTLKIGLRWAGKGTTGIPIRGVYGPMISAISVEPNFKPPVYYDTKDIILKVGVPVAAATLLLFIIVGVFWKKRRDKNDIDKELRGLDLQTGTFTLRQIKAATDNFDVTRKIGEGGFGSVYKGELSEGKLIAVKQLSAKSRQGNREFVNEIGMISALQHPNLVKLYGCCVEGNQLILVYEYLENNCLSRALFGKDESSRLKLDWSTRKKIFLGIAKGLTFLHEESRIKIVHRDIKASNVLLDKDLNAKISDFGLAKLNDDGNTHISTRIAGTIGYMAPEYAMRGYLTEKADVYSFGVVALEIVSGKSNTNFRPTEDFVYLLDWAYVLQERGSLLELVDPTLASDYSEEEAMLMLNVALMCTNASPTLRPTMSQVVSLIEGKTAMQELLSDPSFSTVNPKLKALRNHFWQNELSRSLSFSTSGPRTASANSLVDAEEKTGLLD | 2.7.11.1 | null | phosphorylation [GO:0016310] | membrane [GO:0016020] | 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;PF11721;PF07714; | 2.60.120.430;3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | 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; 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; | null | null | null | null | null | Arabidopsis thaliana (Mouse-ear cress) |
C0LGF4 | FEI1_ARATH | MMGICEMKSCCSWLLLISLLCSLSNESQAISPDGEALLSFRNAVTRSDSFIHQWRPEDPDPCNWNGVTCDAKTKRVITLNLTYHKIMGPLPPDIGKLDHLRLLMLHNNALYGAIPTALGNCTALEEIHLQSNYFTGPIPAEMGDLPGLQKLDMSSNTLSGPIPASLGQLKKLSNFNVSNNFLVGQIPSDGVLSGFSKNSFIGNLNLCGKHVDVVCQDDSGNPSSHSQSGQNQKKNSGKLLISASATVGALLLVALMCFWGCFLYKKLGKVEIKSLAKDVGGGASIVMFHGDLPYSSKDIIKKLEMLNEEHIIGCGGFGTVYKLAMDDGKVFALKRILKLNEGFDRFFERELEILGSIKHRYLVNLRGYCNSPTSKLLLYDYLPGGSLDEALHERGEQLDWDSRVNIIIGAAKGLSYLHHDCSPRIIHRDIKSSNILLDGNLEARVSDFGLAKLLEDEESHITTIVAGTFGYLAPEYMQSGRATEKTDVYSFGVLVLEVLSGKRPTDASFIEKGLNVVGWLKFLISEKRPRDIVDPNCEGMQMESLDALLSIATQCVSPSPEERPTMHRVVQLLESEVMTPCPSEFYDSSSD | 2.7.11.1 | null | phosphorylation [GO:0016310] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF08263;PF00069; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Autophosphorylated. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19017745}; Single-pass type I membrane protein {ECO:0000269|PubMed:19017745}. | 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; 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; | null | null | null | null | FUNCTION: Involved in the signaling pathway that regulates cell wall function, including cellulose biosynthesis, likely via an 1-aminocyclopropane-1-carboxylic acid (ACC)-mediated signal (a precursor of ethylene). {ECO:0000269|PubMed:19017745}. | Arabidopsis thaliana (Mouse-ear cress) |
C0LGF5 | RGI5_ARATH | MERERSNFFFLFLFCSWVSMAQPTLSLSSDGQALLSLKRPSPSLFSSWDPQDQTPCSWYGITCSADNRVISVSIPDTFLNLSSIPDLSSLSSLQFLNLSSTNLSGPIPPSFGKLTHLRLLDLSSNSLSGPIPSELGRLSTLQFLILNANKLSGSIPSQISNLFALQVLCLQDNLLNGSIPSSFGSLVSLQQFRLGGNTNLGGPIPAQLGFLKNLTTLGFAASGLSGSIPSTFGNLVNLQTLALYDTEISGTIPPQLGLCSELRNLYLHMNKLTGSIPKELGKLQKITSLLLWGNSLSGVIPPEISNCSSLVVFDVSANDLTGDIPGDLGKLVWLEQLQLSDNMFTGQIPWELSNCSSLIALQLDKNKLSGSIPSQIGNLKSLQSFFLWENSISGTIPSSFGNCTDLVALDLSRNKLTGRIPEELFSLKRLSKLLLLGNSLSGGLPKSVAKCQSLVRLRVGENQLSGQIPKEIGELQNLVFLDLYMNHFSGGLPYEISNITVLELLDVHNNYITGDIPAQLGNLVNLEQLDLSRNSFTGNIPLSFGNLSYLNKLILNNNLLTGQIPKSIKNLQKLTLLDLSYNSLSGEIPQELGQVTSLTINLDLSYNTFTGNIPETFSDLTQLQSLDLSSNSLHGDIKVLGSLTSLASLNISCNNFSGPIPSTPFFKTISTTSYLQNTNLCHSLDGITCSSHTGQNNGVKSPKIVALTAVILASITIAILAAWLLILRNNHLYKTSQNSSSSPSTAEDFSYPWTFIPFQKLGITVNNIVTSLTDENVIGKGCSGIVYKAEIPNGDIVAVKKLWKTKDNNEEGESTIDSFAAEIQILGNIRHRNIVKLLGYCSNKSVKLLLYNYFPNGNLQQLLQGNRNLDWETRYKIAIGAAQGLAYLHHDCVPAILHRDVKCNNILLDSKYEAILADFGLAKLMMNSPNYHNAMSRVAGSYGYIAPEYGYTMNITEKSDVYSYGVVLLEILSGRSAVEPQIGDGLHIVEWVKKKMGTFEPALSVLDVKLQGLPDQIVQEMLQTLGIAMFCVNPSPVERPTMKEVVTLLMEVKCSPEEWGKTSQPLIKPSSS | 2.7.11.1 | null | maintenance of meristem identity [GO:0010074]; phosphorylation [GO:0016310]; regulation of root meristem growth [GO:0010082] | membrane [GO:0016020] | ATP binding [GO:0005524]; peptide receptor activity [GO:0001653]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF13855;PF08263;PF00069; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Phosphorylated and ubiquitinated upon interaction with RGF1, thus leading to activation a subsequent degradation. {ECO:0000250|UniProtKB:Q9LHP4}.; PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O22476}. | SUBCELLULAR LOCATION: 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:0000255|PROSITE-ProRule:PRU00159}; 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:0000255|PROSITE-ProRule:PRU00159}; | null | null | null | null | FUNCTION: Together with RGI1, RGI2, RGI3 and RGI4, acts as a receptor of RGF1, a peptide hormone that maintains the postembryonic root stem cell niche by regulating the expression levels and patterns of the transcription factor PLETHORA (PLT) (PubMed:27229311, PubMed:27229312). Links RGF1 signal with its downstream components (PubMed:27229311). {ECO:0000269|PubMed:27229311, ECO:0000269|PubMed:27229312}. | Arabidopsis thaliana (Mouse-ear cress) |
C0LGG6 | Y5189_ARATH | MRFLSFLIFVFAVLGLVQAQDQSGFISLDCGLVPTEITYVEKSTNITYRSDATYIDSGVPGKINEVYRTQFQQQIWALRSFPEGQRNCYNFSLTAKRKYLIRGTFIYGNYDGLNQLPSFDLYIGPNKWTSVSIPGVRNGSVSEMIHVLRQDHLQICLVKTGETTPFISSLELRPLNNNTYVTKSGSLIVVARLYFSPTPPFLRYDEDVHDRIWIPFLDNKNSLLSTELSVDTSNFYNVPQTVAKTAAVPLNATQPLKINWSLDDITSQSYIYMHFAEIENLEANETREFNITYNGGENWFSYFRPPKFRITTVYNPAAVSSLDGNFNFTFSMTGNSTHPPLINGLEIYQVLELPQLDTYQDEVSAMMNIKTIYGLSKRSSWQGDPCAPELYRWEGLNCSYPNFAPPQIISLNLSGSNLSGTITSDISKLTHLRELDLSNNDLSGDIPFVFSDMKNLTLINLSGNKNLNRSVPETLQKRIDNKSLTLIRDETGKNSTNVVAIAASVASVFAVLVILAIVFVVIRKKQRTNEASGPRSFTTGTVKSDARSSSSSIITKERKFTYSEVLKMTKNFERVLGKGGFGTVYHGNLDDTQVAVKMLSHSSAQGYKEFKAEVELLLRVHHRHLVGLVGYCDDGDNLALIYEYMEKGDLRENMSGKHSVNVLSWETRMQIAVEAAQGLEYLHNGCRPPMVHRDVKPTNILLNERSQAKLADFGLSRSFPVDGESHVMTVVAGTPGYLDPEYYRTNWLSEKSDVYSFGVVLLEIVTNQPVMNKNRERPHINEWVMFMLTNGDIKSIVDPKLNEDYDTNGVWKVVELALACVNPSSSRRPTMPHVVMELNECLALEIERKQGSQATYIKESVEFSPSSASDFSPLAR | 2.7.11.1 | null | defense response to bacterium [GO:0042742]; phosphorylation [GO:0016310] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF12819;PF00069; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | 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; 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; | null | null | null | null | null | Arabidopsis thaliana (Mouse-ear cress) |
C0LGG8 | Y5343_ARATH | MGFIFSTEKVVYVLLLIFVCLENFGSNAQLLPEDEVQTLRTIFRKLQNQTVNIERTSCSDQNWNFVVESASNSPTSNITCDCTFNASSVCRVTNIQLKSFSLPGIFPPEFGNLTRLREIDLSRNFLNGTIPTTLSQIPLEILSVIGNRLSGPFPPQLGDITTLTDVNLETNLFTGPLPRNLGNLRSLKELLLSANNFTGQIPESLSNLKNLTEFRIDGNSLSGKIPDFIGNWTLLERLDLQGTSMEGPIPPSISNLTNLTELRITDLRGQAAFSFPDLRNLMKMKRLVLRNCLIRGPIPEYIGSMSELKTLDLSSNMLTGVIPDTFRNLDAFNFMFLNNNSLTGPVPQFIINSKENLDLSDNNFTQPPTLSCNQLDVNLISSYPSVTDNSVQWCLREGLPCPEDAKQSSLFINCGGSRLKIGKDTYTDDLNSRGQSTFSSVSERWGYSSSGVWLGKEDAGYLATDRFNLINGSTPEYYKTARLSPQSLKYYGLCLRRGSYKLQLHFAEIMFSNDQTFNSLGRRIFDIYVQGNLLERDFNIAERAGGVGKPFIRQIDGVQVNGSTLEIHLQWTGKGTNVIPTRGVYGPLISAITITPNFKVDTGKPLSNGAVAGIVIAACAVFGLLVLVILRLTGYLGGKEVDENEELRGLDLQTGSFTLKQIKRATNNFDPENKIGEGGFGPVYKGVLADGMTIAVKQLSSKSKQGNREFVTEIGMISALQHPNLVKLYGCCIEGKELLLVYEYLENNSLARALFGTEKQRLHLDWSTRNKICIGIAKGLAYLHEESRLKIVHRDIKATNVLLDLSLNAKISDFGLAKLNDDENTHISTRIAGTIGYMAPEYAMRGYLTDKADVYSFGVVCLEIVSGKSNTNYRPKEEFVYLLDWAYVLQEQGSLLELVDPDLGTSFSKKEAMRMLNIALLCTNPSPTLRPPMSSVVSMLEGKIKVQPPLVKREADPSGSAAMRFKALELLSQDSESQVSTYARNREQDISSSSMDGPWVDSSFSEPGKDVSLQQQEEGRSSSSSRKLLDDLTDVKIE | 2.7.11.1 | null | phosphorylation [GO:0016310] | membrane [GO:0016020] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF13855;PF11721;PF07714; | 2.60.120.430;3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: 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; 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; | null | null | null | null | null | Arabidopsis thaliana (Mouse-ear cress) |
C0LGH8 | Y1634_ARATH | MRSKYFCSLALVLGLFFVSCDGFASNEVQALRRFKEAIYEDPLLVMSNWNDPNSDPCDWTGIYCSPSKDHVIKINISASSIKGFLAPELGQITYLQELILHGNILIGTIPKEIGNLKNLKILDLGNNHLMGPIPAEIGSLSGIMIINLQSNGLTGKLPAELGNLKYLRELHIDRNRLQGSLLVAGASGYQSKVYSSNSSANIAGLCKSLKVADFSYNFFVGNIPKCLENLPRTSFQGNCMQNKDLKHRSSSQCANAQLVKTHGSPSAAPKHQSAQMVAKHHRASKPKWLLALEIVTGSMVGLLLLVALFSAVHRWNNRSTLIIPWKKSSSEKEKFTVYVDSEMLKDVSRLTRQELEVACEDFSNIIGLSADSQIYKGTLKGGSEIAVISLCVKEEDWTGYLELYFQREVADLARLNHENTAKLLGYCKEISPFTRMLVFEYASNGTLYEHLHYGEAALVSWARRMKIVIGIARGLKYLHMELDPPFTISELSSNAIYLTEDFTPKLVDFECWKTILARSEKNLRNISSQGSICVLPNGMESRYLDVSGNIYAFGILLLEIVSGRPPYCKDKGFLIEWAKEFLEAPEAMSGLVDPELKHFNQEDLETVCEVASQCLNRDPTNNNNNHNKPSVQELCETLESRISLSISAELRSSSLAWAELALDS | 2.7.11.1 | null | phosphorylation [GO:0016310] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF08263;PF07714; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | 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; 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; | null | null | null | null | null | Arabidopsis thaliana (Mouse-ear cress) |
C0LGI5 | Y1699_ARATH | MKTISIFFVIILMSSSHAEDDVLCLKGFKSSLKDPSNQLNTWSFPNSSSSICKLTGVSCWNAKENRILSLQLQSMQLSGQIPESLKLCRSLQSLDLSFNDFSGLIPSQICSWLPYLVTLDLSGNKLSGSIPSQIVDCKFLNSLALNQNKLTGSIPSELTRLNRLQRLSLADNDLSGSIPSELSHYGEDGFRGNGGLCGKPLSNCGSFNGKNLTIIVTAGVIGAVGSLCVGFGMFWWFFIRDRRKMNNYGYGAGKCKDDSDWIGLLRSHKLVQVTLFQKPIVKIKLVDLIEATNGFDSGNIVVSSRSGVSYKADLPDGSTLEVKRLSSCCELSEKQFRSEINKLGQIRHPNLVPLLGFCVVEDEILLVYKHMANGTLYSQLQQWDIDWPTRVRVAVGAARGLAWLHHGCQPLYMHQYISSNVILLDEDFDARVIDYGLGKLVSSQDSKDSSFSNGKFGYVAPEYSSTMVASLSGDVYGFGIVLLEIVTGQKPVLINNGEEGFKESLVEWVSKHLSNGRSKDAIDRRIFGKGYDDEIMQVLRIACSCVVSRPKERPLMIQVYESLKNLGDQHGFFSEYSDEFPLIFNKQEHLK | 2.7.11.1 | null | phosphorylation [GO:0016310] | membrane [GO:0016020] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF13855;PF08263;PF07714; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | 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; 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; | null | null | null | null | null | Arabidopsis thaliana (Mouse-ear cress) |
C0LGJ1 | Y1743_ARATH | MTMVTRVIMTDDDSQSLCFLCFLLFFFITAIAVAGDSLDSDREVLLSLKSYLESRNPQNRGLYTEWKMENQDVVCQWPGIICTPQRSRVTGINLTDSTISGPLFKNFSALTELTYLDLSRNTIEGEIPDDLSRCHNLKHLNLSHNILEGELSLPGLSNLEVLDLSLNRITGDIQSSFPLFCNSLVVANLSTNNFTGRIDDIFNGCRNLKYVDFSSNRFSGEVWTGFGRLVEFSVADNHLSGNISASMFRGNCTLQMLDLSGNAFGGEFPGQVSNCQNLNVLNLWGNKFTGNIPAEIGSISSLKGLYLGNNTFSRDIPETLLNLTNLVFLDLSRNKFGGDIQEIFGRFTQVKYLVLHANSYVGGINSSNILKLPNLSRLDLGYNNFSGQLPTEISQIQSLKFLILAYNNFSGDIPQEYGNMPGLQALDLSFNKLTGSIPASFGKLTSLLWLMLANNSLSGEIPREIGNCTSLLWFNVANNQLSGRFHPELTRMGSNPSPTFEVNRQNKDKIIAGSGECLAMKRWIPAEFPPFNFVYAILTKKSCRSLWDHVLKGYGLFPVCSAGSTVRTLKISAYLQLSGNKFSGEIPASISQMDRLSTLHLGFNEFEGKLPPEIGQLPLAFLNLTRNNFSGEIPQEIGNLKCLQNLDLSFNNFSGNFPTSLNDLNELSKFNISYNPFISGAIPTTGQVATFDKDSFLGNPLLRFPSFFNQSGNNTRKISNQVLGNRPRTLLLIWISLALALAFIACLVVSGIVLMVVKASREAEIDLLDGSKTRHDMTSSSGGSSPWLSGKIKVIRLDKSTFTYADILKATSNFSEERVVGRGGYGTVYRGVLPDGREVAVKKLQREGTEAEKEFRAEMEVLSANAFGDWAHPNLVRLYGWCLDGSEKILVHEYMGGGSLEELITDKTKLQWKKRIDIATDVARGLVFLHHECYPSIVHRDVKASNVLLDKHGNARVTDFGLARLLNVGDSHVSTVIAGTIGYVAPEYGQTWQATTRGDVYSYGVLTMELATGRRAVDGGEECLVEWARRVMTGNMTAKGSPITLSGTKPGNGAEQMTELLKIGVKCTADHPQARPNMKEVLAMLVKISGKAELFNGLSSQGYIEM | 2.7.11.1 | null | defense response to nematode [GO:0002215]; multidimensional cell growth [GO:0009825]; phosphorylation [GO:0016310]; seed germination [GO:0009845] | mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF13855;PF08263;PF00069; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:14671022}; Single-pass type I membrane protein {ECO:0000269|PubMed:14671022}. | 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; 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; | null | null | null | null | null | Arabidopsis thaliana (Mouse-ear cress) |
C0LGJ9 | Y2278_ARATH | MQISLQIHLSSFTFLLLIFLLPVLSESQVASSESQTLLEIQKQLQYPQVLQSWTDTTNFCHIRPSPSLRIICLHGHVTELTVTGNRTSKLSGSFHKLFTLLTQLSSLKTLSLTSLGISGSLSPKIITKLSPSLESLNLSSNFISGKIPEEIVSLKNLKSLVLRDNMFWGFVSDDLRGLSNLQELDLGGNKLGPEVPSLPSKLTTVSLKNNSFRSKIPEQIKKLNNLQSLDLSSNEFTGSIPEFLFSIPSLQILSLDQNLLSGSLPNSSCTSSKIITLDVSHNLLTGKLPSCYSSKSFSNQTVLFSFNCLSLIGTPNAKYQRPLSFCQNQASKAIAVEPIPKAKDKDSARIKLGLVILIIIGVIILAAILVLLVLIALKRRRSRSEDDPFEVNNSNNERHASDKVSVCSTTTASSKSLPDSRRVPQTMRSAVIGLPPYRVFSLEELEEATNDFDAASLFCEQLYRGCLREGIPVTVRVIKLKQKSLPQSLAQQMEVLSKLRHMHLVSVLGHSIASNQDHNQHAGHTIFIVQEYISSGSLRDFLTNCRKKEVLKWPQRMAIAIGVARGIQFLHMGVAPGIFGNNLKIENIMLDETLTVKISGYTIPLPSKVGEERPQAKKPRSNEDREKEDVYQFGVILLQIITGKVVAAGSSEMGSLKLQLENGLRDEPSVLSSLADPSVKGSYAYESLRTTVEFAINCLCEDQSKRPSIEDVVWNLQYTIQVQQGWRPSSGNHESSMKAIYE | 2.7.11.1 | null | phosphorylation [GO:0016310] | membrane [GO:0016020] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF13855;PF07714; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | 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; 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; | null | null | null | null | null | Arabidopsis thaliana (Mouse-ear cress) |
C0LGL4 | Y2289_ARATH | MEGRRQRLLVFIFGALAITHLVQAQPPDQRGFISLDCGLPVNESPYTDPRTGLTFSSDADFILSGLRGEAGDDNTYIYRQYKDLRYFPDGIRNCYNLKVEQGINYLIRAGFGYGNYDGLNVYPKFDLHVGPNMWIAVDLEFGKDREIIYMTTSNLLQICLVKTGSTIPMISTLELRPLRNDSYLTQFGPLDLIYRRAYSSNSTGFIRYPDDIFDRKWDRYNEFETDVNTTLNVRSSSPFQVPEAVSRMGITPENASLPLRFYVSLDDDSDKVNVYFHFAEIQALRGNETREFDIELEEDIIQSAYSPTMLQSDTKYNLSPHKCSSGLCYLKLVRTPRSTLPPLISAIEAFKVVDFPYAETNPNDVAAMKDIEAFYGLKMISWQGDPCVPELLKWEDLKCSYTNKSTPPRIISLDLSSRGLKGVIAPAFQNLTELRKLDLSNNSFTGGVPEFLASMKSLSIINLNWNDLTGPLPKLLLDREKNGLKLTIQGNPKLCNDASCKNNNNQTYIVPVVASVASVLIIIAVLILILVFKKRRPTQVDSLPTVQHGLPNRPSIFTQTKRFTYSEVEALTDNFERVLGEGGFGVVYHGILNGTQPIAVKLLSQSSVQGYKEFKAEVELLLRVHHVNLVSLVGYCDEESNLALLYEYAPNGDLKQHLSGERGGSPLKWSSRLKIVVETAQGLEYLHTGCKPPMVHRDVKTTNILLDEHFQAKLADFGLSRSFPVGGETHVSTAVAGTPGYLDPEYYRTNRLNEKSDVYSFGIVLLEIITSRPVIQQTREKPHIAAWVGYMLTKGDIENVVDPRLNRDYEPTSVWKALEIAMSCVNPSSEKRPTMSQVTNELKQCLTLENSKRGVREDMGSRSSVEMSTSFTTEINPKAR | 2.7.11.1 | null | phosphorylation [GO:0016310] | membrane [GO:0016020] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF13855;PF12819;PF00069; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | 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; 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; | null | null | null | null | null | Arabidopsis thaliana (Mouse-ear cress) |
C0LGL9 | FEI2_ARATH | MGICLMKRCCSWFLLISFLSALTNENEAISPDGEALLSFRNGVLASDGVIGLWRPEDPDPCNWKGVTCDAKTKRVIALSLTYHKLRGPLPPELGKLDQLRLLMLHNNALYQSIPASLGNCTALEGIYLQNNYITGTIPSEIGNLSGLKNLDLSNNNLNGAIPASLGQLKRLTKFNVSNNFLVGKIPSDGLLARLSRDSFNGNRNLCGKQIDIVCNDSGNSTASGSPTGQGGNNPKRLLISASATVGGLLLVALMCFWGCFLYKKLGRVESKSLVIDVGGGASIVMFHGDLPYASKDIIKKLESLNEEHIIGCGGFGTVYKLSMDDGNVFALKRIVKLNEGFDRFFERELEILGSIKHRYLVNLRGYCNSPTSKLLLYDYLPGGSLDEALHKRGEQLDWDSRVNIIIGAAKGLAYLHHDCSPRIIHRDIKSSNILLDGNLEARVSDFGLAKLLEDEESHITTIVAGTFGYLAPEYMQSGRATEKTDVYSFGVLVLEVLSGKLPTDASFIEKGFNIVGWLNFLISENRAKEIVDLSCEGVERESLDALLSIATKCVSSSPDERPTMHRVVQLLESEVMTPCPSDFYDSSSD | 2.7.11.1 | null | mucilage biosynthetic process [GO:0010192]; mucilage biosynthetic process involved in seed coat development [GO:0048354]; phosphorylation [GO:0016310]; plant-type cell wall organization [GO:0009664]; unidimensional cell growth [GO:0009826] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; kinase activity [GO:0016301]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF13855;PF08263;PF00069; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Autophosphorylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19017745}; Single-pass type I membrane protein {ECO:0000269|PubMed:19017745}. | 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; 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; | null | null | null | null | FUNCTION: Involved in the signaling pathway that regulates cell wall function, including cellulose biosynthesis, likely via an 1-aminocyclopropane-1-carboxylic acid (ACC)-mediated signal (a precursor of ethylene). {ECO:0000269|PubMed:19017745}. | Arabidopsis thaliana (Mouse-ear cress) |
C0LGN2 | Y3148_ARATH | MSLNRQLLFTYYFIVSLILFSDFVSSATLPKEEVDALQSVATALKKSNWNFSVDPCDETLSEGGWRNPNAAKGFEDAVTCNCSSVICHVTNIVLKAQDLQGSLPTDLSGLPFLQELDLTRNYLNGSIPPEWGASSLLNISLLGNRISGSIPKELGNLTTLSGLVLEYNQLSGKIPPELGNLPNLKRLLLSSNNLSGEIPSTFAKLTTLTDLRISDNQFTGAIPDFIQNWKGLEKLVIQASGLVGPIPSAIGLLGTLTDLRITDLSGPESPFPPLRNMTSMKYLILRNCNLTGDLPAYLGQNRKLKNLDLSFNKLSGPIPATYSGLSDVDFIYFTSNMLNGQVPSWMVDQGDTIDITYNNFSKDKTEECQQKSVNTFSSTSPLVANNSSNVSCLSKYTCPKTFYGLHINCGGNEITSNETKYDADTWDTPGYYDSKNGWVSSNTGNFLDDDRTNNGKSKWSNSSELKITNSSIDFRLYTQARLSAISLTYQALCLGKGNYTVNLHFAEIMFNEKNMYSNLGRRYFDIYVQGKREVKDFNIVDEAKGVGKAVVKKFPVMVTNGKLEIRLQWAGKGTQAIPVRGVYGPLISAVSVDPDFIPPKEPGTGTGGGSSVGTVVGSVIASTVFLVLLIGGILWWRGCLRPKSQMEKDFKNLDFQISSFSLRQIKVATDNFDPANKIGEGGFGPVHKGIMTDGTVIAVKQLSAKSKQGNREFLNEIAMISALQHPHLVKLYGCCVEGDQLLLVYEYLENNSLARALFGPQETQIPLNWPMRQKICVGIARGLAYLHEESRLKIVHRDIKATNVLLDKELNPKISDFGLAKLDEEENTHISTRVAGTYGYMAPEYAMRGHLTDKADVYSFGVVALEIVHGKSNTSSRSKADTFYLLDWVHVLREQNTLLEVVDPRLGTDYNKQEALMMIQIGMLCTSPAPGDRPSMSTVVSMLEGHSTVNVEKLLEASVNNEKDEESVRAMKRHYATIGEEEITNTTTTDGPFTSSSTSTANANDLYPVKLDSAYWNTRT | 2.7.11.1 | null | jasmonic acid and ethylene-dependent systemic resistance [GO:0009861]; phosphorylation [GO:0016310]; regulation of innate immune response [GO:0045088] | cytosol [GO:0005829]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF11721;PF07714; | 2.60.120.430;3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17644812}; Single-pass type I membrane protein {ECO:0000305|PubMed:17644812}. | 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; 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; | null | null | null | null | null | Arabidopsis thaliana (Mouse-ear cress) |
C0LGP2 | MEE39_ARATH | MKNLCWVFLSLFWFGVFLIIRFAEGQNQEGFISLDCGLPLNEPPYIESETGIQFSSDENFIQSGKTGRIPKNLESENLKQYATLRYFPDGIRNCYDLRVEEGRNYLIRATFFYGNFDGLNVSPEFDMHIGPNKWTTIDLQIVPDGTVKEIIHIPRSNSLQICLVKTGATIPMISALELRPLANDTYIAKSGSLKYYFRMYLSNATVLLRYPKDVYDRSWVPYIQPEWNQISTTSNVSNKNHYDPPQVALKMAATPTNLDAALTMVWRLENPDDQIYLYMHFSEIQVLKANDTREFDIILNGETINTRGVTPKYLEIMTWLTTNPRQCNGGICRMQLTKTQKSTLPPLLNAFEVYSVLQLPQSQTNEIEVVAIKNIRTTYGLSRISWQGDPCVPKQFLWDGLNCNITDISAPPRIISLNLSSSGLSGTIVSNFQNLAHLESLDLSNNSLSGIVPEFLATMKSLLVINLSGNKLSGAIPQALRDREREGLKLNVLGNKELCLSSTCIDKPKKKVAVKVVAPVASIAAIVVVILLFVFKKKMSSRNKPEPWIKTKKKRFTYSEVMEMTKNLQRPLGEGGFGVVYHGDLNGSEQVAVKLLSQTSAQGYKEFKAEVELLLRVHHINLVNLVGYCDEQDHFALIYEYMSNGDLHQHLSGKHGGSVLNWGTRLQIAIEAALGLEYLHTGCKPAMVHRDVKSTNILLDEEFKAKIADFGLSRSFQVGGDQSQVSTVVAGTLGYLDPEYYLTSELSEKSDVYSFGILLLEIITNQRVIDQTRENPNIAEWVTFVIKKGDTSQIVDPKLHGNYDTHSVWRALEVAMSCANPSSVKRPNMSQVIINLKECLASENTRISRNNQNMDSGHSSDQLNVTVTFDTDVKPKAR | 2.7.11.1 | null | embryo development ending in seed dormancy [GO:0009793]; endosperm development [GO:0009960]; phosphorylation [GO:0016310] | membrane [GO:0016020] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF13855;PF12819;PF07714; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | 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; 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; | null | null | null | null | FUNCTION: Receptor-like serine/threonine-kinase required during the endosperm development in seeds. {ECO:0000269|PubMed:15634699}. | Arabidopsis thaliana (Mouse-ear cress) |
C0LGP9 | IMK3_ARATH | MEFITQNQAITSLSMINTDIDQPKASLRSRFLLHLIICLLFFVPPCSSQAWDGVVITQADYQGLQAVKQELIDPRGFLRSWNGSGFSACSGGWAGIKCAQGQVIVIQLPWKSLGGRISEKIGQLQALRKLSLHDNNLGGSIPMSLGLIPNLRGVQLFNNRLTGSIPASLGVSHFLQTLDLSNNLLSEIIPPNLADSSKLLRLNLSFNSLSGQIPVSLSRSSSLQFLALDHNNLSGPILDTWGSKSLNLRVLSLDHNSLSGPFPFSLCNLTQLQDFSFSHNRIRGTLPSELSKLTKLRKMDISGNSVSGHIPETLGNISSLIHLDLSQNKLTGEIPISISDLESLNFFNVSYNNLSGPVPTLLSQKFNSSSFVGNSLLCGYSVSTPCPTLPSPSPEKERKPSHRNLSTKDIILIASGALLIVMLILVCVLCCLLRKKANETKAKGGEAGPGAVAAKTEKGGEAEAGGETGGKLVHFDGPMAFTADDLLCATAEIMGKSTYGTVYKATLEDGSQVAVKRLREKITKSQKEFENEINVLGRIRHPNLLALRAYYLGPKGEKLVVFDYMSRGSLATFLHARGPDVHINWPTRMSLIKGMARGLFYLHTHANIIHGNLTSSNVLLDENITAKISDYGLSRLMTAAAGSSVIATAGALGYRAPELSKLKKANTKTDVYSLGVIILELLTGKSPSEALNGVDLPQWVATAVKEEWTNEVFDLELLNDVNTMGDEILNTLKLALHCVDATPSTRPEAQQVMTQLGEIRPEETTATTSEPLIDVPEASASTSQ | 2.7.11.1 | null | phosphorylation [GO:0016310] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF13855;PF08263;PF07714; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Autophosphorylated. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|Ref.8}; Single-pass type I membrane protein {ECO:0000269|Ref.8}. | 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; 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; | null | null | null | null | FUNCTION: Can phosphorylate AGL24. {ECO:0000269|Ref.9}. | Arabidopsis thaliana (Mouse-ear cress) |
C0LGQ4 | MDIS2_ARATH | MMGCGFHFPWFFFLIIGLQAPLSLSLTSQGSALLKFRARVNSDPHGTLANWNVSGINDLCYWSGVTCVDGKVQILDLSGYSLEGTLAPELSQLSDLRSLILSRNHFSGGIPKEYGSFENLEVLDLRENDLSGQIPPELSNGLSLKHLLLSGNKFSDDMRIKIVRLQSSYEVRLKKSPKLSPLAVLGCINRKLGHCVSRNRIIQVKKVEAIVFRIKATSRRFLKAFPSFLEETDIYKRRELLEETSNLAAEPAPSAPSPSPGIITEASPRSSGSFPAVTNAKKRRPPLVPPVPSPDKGSTSPDISKNQPQDNKQSKGSKHVWLYVVIAVASFVGLLIIVAVIFFCRKRAVKSIGPWKTGLSGQLQKAFVTGVPKLNRSELETACEDFSNIIETFDGYTVYKGTLSSGVEIAVASTAIAESKEWTRAMEMAYRRKIDTLSRINHKNFVNLIGYCEEDDPFNRMMVFEYAPNGTLFEHLHDKETEHLDWSARMRIIMGTAYCLQHMHGMNPPMAHTDFNSSEIYLTDDYAAKVSEIPFNLEARLNPKKHVSGDLEQTSLLLPPEPEANVHSFGVLMLEIISGKLSFSDEYGSIEQWASKYLEKDDLGEMIDPSLKTFKEEELEVICDVIRECLKTEQRQRPSMKDVAEQLKQVINITPEKATPRSSPLWWAELEILSSEAT | 2.7.11.1 | null | phosphorylation [GO:0016310]; root hair cell differentiation [GO:0048765] | endomembrane system [GO:0012505]; membrane [GO:0016020]; pollen tube [GO:0090406] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF08263;PF07714; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:26863186}; Single-pass type I membrane protein {ECO:0000305}. | 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}; 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}; | null | null | null | null | FUNCTION: Involved in the pollen tube perception of the female signal by binding an unidentified female attractant (PubMed:26863186). May be involved in the regulation of root hairs development (PubMed:16367956). {ECO:0000269|PubMed:16367956, ECO:0000269|PubMed:26863186}. | Arabidopsis thaliana (Mouse-ear cress) |
C0LGQ5 | GSO1_ARATH | MQPLVLLLLFILCFSGLGQPGIINNDLQTLLEVKKSLVTNPQEDDPLRQWNSDNINYCSWTGVTCDNTGLFRVIALNLTGLGLTGSISPWFGRFDNLIHLDLSSNNLVGPIPTALSNLTSLESLFLFSNQLTGEIPSQLGSLVNIRSLRIGDNELVGDIPETLGNLVNLQMLALASCRLTGPIPSQLGRLVRVQSLILQDNYLEGPIPAELGNCSDLTVFTAAENMLNGTIPAELGRLENLEILNLANNSLTGEIPSQLGEMSQLQYLSLMANQLQGLIPKSLADLGNLQTLDLSANNLTGEIPEEFWNMSQLLDLVLANNHLSGSLPKSICSNNTNLEQLVLSGTQLSGEIPVELSKCQSLKQLDLSNNSLAGSIPEALFELVELTDLYLHNNTLEGTLSPSISNLTNLQWLVLYHNNLEGKLPKEISALRKLEVLFLYENRFSGEIPQEIGNCTSLKMIDMFGNHFEGEIPPSIGRLKELNLLHLRQNELVGGLPASLGNCHQLNILDLADNQLSGSIPSSFGFLKGLEQLMLYNNSLQGNLPDSLISLRNLTRINLSHNRLNGTIHPLCGSSSYLSFDVTNNGFEDEIPLELGNSQNLDRLRLGKNQLTGKIPWTLGKIRELSLLDMSSNALTGTIPLQLVLCKKLTHIDLNNNFLSGPIPPWLGKLSQLGELKLSSNQFVESLPTELFNCTKLLVLSLDGNSLNGSIPQEIGNLGALNVLNLDKNQFSGSLPQAMGKLSKLYELRLSRNSLTGEIPVEIGQLQDLQSALDLSYNNFTGDIPSTIGTLSKLETLDLSHNQLTGEVPGSVGDMKSLGYLNVSFNNLGGKLKKQFSRWPADSFLGNTGLCGSPLSRCNRVRSNNKQQGLSARSVVIISAISALTAIGLMILVIALFFKQRHDFFKKVGHGSTAYTSSSSSSQATHKPLFRNGASKSDIRWEDIMEATHNLSEEFMIGSGGSGKVYKAELENGETVAVKKILWKDDLMSNKSFSREVKTLGRIRHRHLVKLMGYCSSKSEGLNLLIYEYMKNGSIWDWLHEDKPVLEKKKKLLDWEARLRIAVGLAQGVEYLHHDCVPPIVHRDIKSSNVLLDSNMEAHLGDFGLAKVLTENCDTNTDSNTWFACSYGYIAPEYAYSLKATEKSDVYSMGIVLMEIVTGKMPTDSVFGAEMDMVRWVETHLEVAGSARDKLIDPKLKPLLPFEEDAACQVLEIALQCTKTSPQERPSSRQACDSLLHVYNNRTAGYKKL | 2.7.11.1 | null | Casparian strip assembly [GO:0160073]; endodermal cell differentiation [GO:0035987]; establishment of protein localization [GO:0045184]; phosphorylation [GO:0016310]; potassium ion homeostasis [GO:0055075]; regulation of cell division [GO:0051302]; regulation of cell fate specification [GO:0042659]; regulation of root development [GO:2000280]; regulation of root morphogenesis [GO:2000067]; response to wounding [GO:0009611]; specification of plant organ axis polarity [GO:0090708] | Casparian strip [GO:0048226]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | 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:0000269|PubMed:25233277}; Single-pass type I membrane protein {ECO:0000255}. Note=Localized into a broader band at the endodermal plasma membrane, embedding growing CASP microdomains. In endodermal cells, first observed on all cell sides, but quickly relocated in the transversal and anticlinal sides of the plasma membrane, but excluded from the Casparian strip membrane domain (CSD). {ECO:0000269|PubMed:25233277}. | 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:0000255|PROSITE-ProRule:PRU00159}; 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:0000255|PROSITE-ProRule:PRU00159}; | null | null | null | null | FUNCTION: Together with GSO2, receptor-like serine/threonine-kinase required during the development of the epidermal surface in embryos and cotyledons (PubMed:18088309). In coordination with GSO2, regulates root growth through control of cell division and cell fate specification. Controls seedling root growth by modulating sucrose response after germination (PubMed:24123341). Receptor of the peptide hormones CIF1 and CIF2 required for contiguous Casparian strip diffusion barrier formation in roots (PubMed:28104889). Required for localizing CASP proteins into the Casparian strip following an uninterrupted, ring-like domain, to trigger endodermal differentiation and thus regulate potassium ion (K) homeostasis. Involved in the maintenance of water transport and root pressure. May also be involved in the regulation of suberin accumulation in the endodermis (PubMed:25233277). {ECO:0000269|PubMed:18088309, ECO:0000269|PubMed:24123341, ECO:0000269|PubMed:25233277, ECO:0000269|PubMed:28104889}. | Arabidopsis thaliana (Mouse-ear cress) |
C0LGQ9 | GHR1_ARATH | MNLSRILLLSMFFLSAMGQLPSQDIMALLEFKKGIKHDPTGFVLNSWNDESIDFNGCPSSWNGIVCNGGNVAGVVLDNLGLTADADFSLFSNLTKLVKLSMSNNSLSGVLPNDLGSFKSLQFLDLSDNLFSSSLPKEIGRSVSLRNLSLSGNNFSGEIPESMGGLISLQSLDMSSNSLSGPLPKSLTRLNDLLYLNLSSNGFTGKMPRGFELISSLEVLDLHGNSIDGNLDGEFFLLTNASYVDISGNRLVTTSGKLLPGVSESIKHLNLSHNQLEGSLTSGFQLFQNLKVLDLSYNMLSGELPGFNYVYDLEVLKLSNNRFSGSLPNNLLKGDSLLLTTLDLSGNNLSGPVSSIMSTTLHTLDLSSNSLTGELPLLTGGCVLLDLSNNQFEGNLTRWSKWENIEYLDLSQNHFTGSFPDATPQLLRANHLNLSYNKLTGSLPERIPTHYPKLRVLDISSNSLEGPIPGALLSMPTLEEIHLQNNGMTGNIGPLPSSGSRIRLLDLSHNRFDGDLPGVFGSLTNLQVLNLAANNLSGSLPSSMNDIVSLSSLDVSQNHFTGPLPSNLSSNIMAFNVSYNDLSGTVPENLKNFPPPSFYPGNSKLVLPAGSPGSSASEASKNKSTNKLVKVVIIVSCAVALIILILVAILLFCICKSRRREERSITGKETNRRAQTIPSGSGGGMVVSAEDLVASRKGSSSEILSPDEKLAVATGFSPSKTSNLSWSPGSGDSFPADQQLARLDVRSPDRLVGELHFLDDSIKLTPEELSRAPAEVLGRSSHGTSYRATLDNGVFLTVKWLREGVAKQRKEFAKEVKKFSNIRHPNVVTLRGYYWGPTQHEKLILSDYISPGSLASFLYDRPGRKGPPLAWTQRLKIAVDVARGLNYLHFDRAVPHGNLKATNILLDGAELNARVADYCLHRLMTQAGTVEQILDAGILGYRAPELAASRKPLPSFKSDVYAFGVILLEILTGRCAGDVITGEQEGVDLTDWVRLRVAEGRGAECFDSVLTQEMGSDPVTEKGMKEVLGIALRCIRSVSERPGIKTIYEDLSSI | 2.7.11.1 | null | abscisic acid-activated signaling pathway [GO:0009738]; cellular response to absence of light [GO:0071485]; cellular response to carbon dioxide [GO:0071244]; hydrogen peroxide mediated signaling pathway involved in stomatal movement [GO:1901528]; phosphorylation [GO:0016310]; positive regulation of abscisic acid-activated signaling pathway [GO:0009789]; regulation of stomatal closure [GO:0090333]; response to abscisic acid [GO:0009737]; response to light stimulus [GO:0009416] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF13855;PF08263;PF07714; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Phosphorylated by HT1; this phosphorylation is inhibited by MPK12 and MPK4. {ECO:0000269|PubMed:27694184, ECO:0000269|PubMed:30361234}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22730405, ECO:0000269|PubMed:30361234}; 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:0000269|PubMed:22730405}; 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:0000269|PubMed:22730405}; | null | null | null | null | FUNCTION: Receptor kinase acting as an early component in abscisic acid (ABA) signaling (PubMed:22730405). Required for darkness, ABA, high CO(2) and hydrogen peroxide (H(2)O(2)) induction of S-type anion currents in guard cells leading to stomatal closure, possibly via the phosphorylation and activation of the anion channel SLAC1 and as a scaffolding component (PubMed:22730405, PubMed:27694184, PubMed:30361234). Seems to act in parallel with SRK2E/OST1 in the ABA signaling pathway which regulates stomatal movement (PubMed:22730405). Binds ATP (PubMed:30361234). Involved in the local and/or systemic stomatal responses (e.g. stomatal closure) to light stress (PubMed:29463779). {ECO:0000269|PubMed:22730405, ECO:0000269|PubMed:27694184, ECO:0000269|PubMed:29463779, ECO:0000269|PubMed:30361234}. | Arabidopsis thaliana (Mouse-ear cress) |
C0LGR3 | RGI3_ARATH | MPPNIYRLSFFSSLLCFFFIPCFSLDQQGQALLSWKSQLNISGDAFSSWHVADTSPCNWVGVKCNRRGEVSEIQLKGMDLQGSLPVTSLRSLKSLTSLTLSSLNLTGVIPKEIGDFTELELLDLSDNSLSGDIPVEIFRLKKLKTLSLNTNNLEGHIPMEIGNLSGLVELMLFDNKLSGEIPRSIGELKNLQVLRAGGNKNLRGELPWEIGNCENLVMLGLAETSLSGKLPASIGNLKRVQTIAIYTSLLSGPIPDEIGYCTELQNLYLYQNSISGSIPTTIGGLKKLQSLLLWQNNLVGKIPTELGNCPELWLIDFSENLLTGTIPRSFGKLENLQELQLSVNQISGTIPEELTNCTKLTHLEIDNNLITGEIPSLMSNLRSLTMFFAWQNKLTGNIPQSLSQCRELQAIDLSYNSLSGSIPKEIFGLRNLTKLLLLSNDLSGFIPPDIGNCTNLYRLRLNGNRLAGSIPSEIGNLKNLNFVDISENRLVGSIPPAISGCESLEFLDLHTNSLSGSLLGTTLPKSLKFIDFSDNALSSTLPPGIGLLTELTKLNLAKNRLSGEIPREISTCRSLQLLNLGENDFSGEIPDELGQIPSLAISLNLSCNRFVGEIPSRFSDLKNLGVLDVSHNQLTGNLNVLTDLQNLVSLNISYNDFSGDLPNTPFFRRLPLSDLASNRGLYISNAISTRPDPTTRNSSVVRLTILILVVVTAVLVLMAVYTLVRARAAGKQLLGEEIDSWEVTLYQKLDFSIDDIVKNLTSANVIGTGSSGVVYRITIPSGESLAVKKMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHGAGKGGCVDWEARYDVVLGVAHALAYLHHDCLPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTGIDLAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLPGGAHLVKWVRDHLAEKKDPSRLLDPRLDGRTDSIMHEMLQTLAVAFLCVSNKANERPLMKDVVAMLTEIRHIDVGRSETEKIKAGGCGSKEPQQFMSNEKIINSHGSSNCSFAFSDDSV | 2.7.11.1 | null | maintenance of meristem identity [GO:0010074]; maintenance of root meristem identity [GO:0010078]; phosphorylation [GO:0016310]; regulation of root development [GO:2000280]; regulation of root meristem growth [GO:0010082] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; peptide binding [GO:0042277]; peptide receptor activity [GO:0001653]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF13855;PF08263;PF00069; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Phosphorylated and ubiquitinated upon interaction with RGF1, thus leading to activation a subsequent degradation. {ECO:0000250|UniProtKB:Q9LHP4}.; PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O22476}. | 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:0000255|PROSITE-ProRule:PRU00159}; 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:0000255|PROSITE-ProRule:PRU00159}; | null | null | null | null | FUNCTION: Together with RGI1, RGI2, RGI4 and RGI5, acts as a receptor of RGF peptides (e.g. RGF1, GLV5/CLEL1/RGF2, GLV7/CLEL3/RGF3, GLV3/RGF4, GLV10/CLEL7/RGF5 and RGF10/CLELN), peptide hormones which maintain the postembryonic root stem cell niche by regulating the expression levels and patterns of the transcription factor PLETHORA (PLT, e.g. PLT1 and PLT2) (PubMed:27001831, PubMed:27229311, PubMed:27229312). Links RGF peptides signal with their downstream components (PubMed:27001831, PubMed:27229311). {ECO:0000269|PubMed:27001831, ECO:0000269|PubMed:27229311, ECO:0000269|PubMed:27229312}. | Arabidopsis thaliana (Mouse-ear cress) |
C0LGR6 | Y4291_ARATH | MGAHSVFLILFSVIAIAIVVHGQGQAGFISIDCGSPPNINYVDTDTGISYTWDAPFINAGVNLNVSEEYGYPKNPVLPFPLADVRSFPQGNRNCYTLTPSDGKGNLYLIRASFMYGNYDGKNALPEFDLYVNVNFWTSVKLRNASENVIKEILSFAESDTIYVCLVNKGKGTPFISALELRPMNSSIYGTEFGRNVSLVLYQRWDTGYLNGTGRYQKDTYDRIWSPYSPVSWNTTMTTGYIDIFQSGYRPPDEVIKTAASPKSDDEPLELSWTSSDPDTRFYAYLYFAELENLKRNESREIKIFWNGSPVSGAFNPSPEYSMTVSNSRAFTGKDHWISVQKTAESTRPPILNAIEIFSAQSLDEFYTRIDDVQAIESIKSTYKVNKIWTGDPCSPRLFPWEGIGCSYNTSSYQIKSLNLSSSGLHGPIAFAFRNLSLLESLDLSNNNLKGIVPEFLADLKYLKSLNLKGNNLTGFIPRSLRKRATANGLALSVDEQNICHSRSCRDGNRIMVPIVVSTLVIILIAALAIICIMRRESKIMYSGAYSGPLLPSGKRRFTYSEVSSITNNFNKVIGKGGFGIVYLGSLEDGTEIAVKMINDSSFGKSKGSSSSSSSSQVSKEFQVEAELLLTVHHRNLASFVGYCDDGRSMALIYEYMANGNLQDYLSSENAEDLSWEKRLHIAIDSAQGLEYLHHGCRPPIVHRDVKTANILLNDNLEAKIADFGLSKVFPEDDLSHVVTAVMGTPGYVDPEYYNTFKLNEKSDVYSFGIVLLELITGKRSIMKTDDGEKMNVVHYVEPFLKMGDIDGVVDPRLHGDFSSNSAWKFVEVAMSCVRDRGTNRPNTNQIVSDLKQCLAAELAREPKSNHEKKEVVKEKYTKTKSTVQNYSSNEYNSSSGSVSLSFGDYSTFGPMAR | 2.7.11.1 | null | phosphorylation [GO:0016310] | membrane [GO:0016020] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF13855;PF12819;PF07714; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | 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; 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; | null | null | null | null | null | Arabidopsis thaliana (Mouse-ear cress) |
C0LGR9 | Y4312_ARATH | MTRDDKFPIVYSLLLIVLLFVSPIYGDGDADALLKFKSSLVNASSLGGWDSGEPPCSGDKGSDSKWKGVMCSNGSVFALRLENMSLSGELDVQALGSIRGLKSISFMRNHFEGKIPRGIDGLVSLAHLYLAHNQFTGEIDGDLFSGMKALLKVHLEGNRFSGEIPESLGKLPKLTELNLEDNMFTGKIPAFKQKNLVTVNVANNQLEGRIPLTLGLMNITFFSGNKGLCGAPLLPCRYTRPPFFTVFLLALTILAVVVLITVFLSVCILSRRQGKGQDQIQNHGVGHFHGQVYGQPEQQQHSEKSSQDSKVYRKLANETVQRDSTATSGAISVGGLSPDEDKRGDQRKLHFVRNDQERFTLQDMLRASAEVLGSGGFGSSYKAALSSGRAVVVKRFRFMSNIGREEFYDHMKKIGRLSHPNLLPLIAFYYRKEEKLLVTNYISNGSLANLLHANRTPGQVVLDWPIRLKIVRGVTRGLAYLYRVFPDLNLPHGHLKSSNVLLDPNFEPLLTDYALVPVVNRDQSQQFMVAYKAPEFTQQDRTSRRSDVWSLGILILEILTGKFPANYLRQGKGADDELAAWVESVARTEWTADVFDKEMKAGKEHEAQMLKLLKIGLRCCDWDIEKRIELHEAVDRIEEVDRDAGGGQESVRSSYVTASDGDHRSSRAMTEEFSLM | 2.7.11.1 | null | phosphorylation [GO:0016310] | membrane [GO:0016020] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF08263;PF00069; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | 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; 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; | null | null | null | null | null | Arabidopsis thaliana (Mouse-ear cress) |
C0LGS2 | Y4361_ARATH | MAMDISLFFIFLVIYAPLVSYADESQAEIDALTAFKLNLHDPLGALTSWDPSTPAAPCDWRGVGCTNHRVTEIRLPRLQLSGRISDRISGLRMLRKLSLRSNSFNGTIPTSLAYCTRLLSVFLQYNSLSGKLPPAMRNLTSLEVFNVAGNRLSGEIPVGLPSSLQFLDISSNTFSGQIPSGLANLTQLQLLNLSYNQLTGEIPASLGNLQSLQYLWLDFNLLQGTLPSAISNCSSLVHLSASENEIGGVIPAAYGALPKLEVLSLSNNNFSGTVPFSLFCNTSLTIVQLGFNAFSDIVRPETTANCRTGLQVLDLQENRISGRFPLWLTNILSLKNLDVSGNLFSGEIPPDIGNLKRLEELKLANNSLTGEIPVEIKQCGSLDVLDFEGNSLKGQIPEFLGYMKALKVLSLGRNSFSGYVPSSMVNLQQLERLNLGENNLNGSFPVELMALTSLSELDLSGNRFSGAVPVSISNLSNLSFLNLSGNGFSGEIPASVGNLFKLTALDLSKQNMSGEVPVELSGLPNVQVIALQGNNFSGVVPEGFSSLVSLRYVNLSSNSFSGEIPQTFGFLRLLVSLSLSDNHISGSIPPEIGNCSALEVLELRSNRLMGHIPADLSRLPRLKVLDLGQNNLSGEIPPEISQSSSLNSLSLDHNHLSGVIPGSFSGLSNLTKMDLSVNNLTGEIPASLALISSNLVYFNVSSNNLKGEIPASLGSRINNTSEFSGNTELCGKPLNRRCESSTAEGKKKKRKMILMIVMAAIGAFLLSLFCCFYVYTLLKWRKKLKQQSTTGEKKRSPGRTSAGSRVRSSTSRSSTENGEPKLVMFNNKITLAETIEATRQFDEENVLSRTRYGLLFKANYNDGMVLSIRRLPNGSLLNENLFKKEAEVLGKVKHRNITVLRGYYAGPPDLRLLVYDYMPNGNLSTLLQEASHQDGHVLNWPMRHLIALGIARGLGFLHQSNMVHGDIKPQNVLFDADFEAHISDFGLDRLTIRSPSRSAVTANTIGTLGYVSPEATLSGEITRESDIYSFGIVLLEILTGKRPVMFTQDEDIVKWVKKQLQRGQVTELLEPGLLELDPESSEWEEFLLGIKVGLLCTATDPLDRPTMSDVVFMLEGCRVGPDVPSSADPTSQPSPA | 2.7.11.1 | null | phosphorylation [GO:0016310] | plasma membrane [GO:0005886]; pollen tube [GO:0090406] | ATP binding [GO:0005524]; kinase activity [GO:0016301]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF13855;PF08263;PF07714; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17644812}; Single-pass type I membrane protein {ECO:0000305|PubMed:17644812}. | 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; 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; | null | null | null | null | null | Arabidopsis thaliana (Mouse-ear cress) |
C0LGS3 | Y4372_ARATH | MRMELISVIFFFFCSVLSSSALNSDGLVLMKFKSSVLVDPLSLLQTWNYKHESPCSWRGISCNNDSKVLTLSLPNSQLLGSIPSDLGSLLTLQSLDLSNNSFNGPLPVSFFNARELRFLDLSSNMISGEIPSAIGDLHNLLTLNLSDNALAGKLPTNLASLRNLTVVSLENNYFSGEIPGGWRVVEFLDLSSNLINGSLPPDFGGYSLQYLNVSFNQISGEIPPEIGVNFPRNVTVDLSFNNLTGPIPDSPVFLNQESNFFSGNPGLCGEPTRNPCLIPSSPSIVSEADVPTSTPAIAAIPNTIGSNPVTDPNSQQTDPNPRTGLRPGVIIGIVVGDIAGIGILAVIFLYIYRCKKNKIVDNNNNDKQRTETDTITLSTFSSSSSSPEESRRFRKWSCLRKDPETTPSEEEDEDDEDEESGYNANQRSGDNKLVTVDGEKEMEIETLLKASAYILGATGSSIMYKAVLEDGRVFAVRRLGENGLSQRRFKDFEPHIRAIGKLVHPNLVRLCGFYWGTDEKLVIYDFVPNGSLVNPRYRKGGGSSSPYHLPWETRLKIAKGIARGLAYLHEKKHVHGNLKPSNILLGHDMEPKIGDFGLERLLTGETSYIRAGGSSRIFSSKRYTTSSREFSSIGPTPSPSPSSVGAMSPYCAPESFRSLKPSPKWDVYGFGVILLELLTGKIVSVEEIVLGNGLTVEDGHRAVRMADVAIRGELDGKQEFLLDCFKLGYSCASPVPQKRPTMKESLAVLERFHPNSSVIKSSSFHYGH | 2.7.11.1 | null | phosphorylation [GO:0016310] | membrane [GO:0016020] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF08263;PF00069; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | 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; 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; | null | null | null | null | null | Arabidopsis thaliana (Mouse-ear cress) |
C0LGT1 | Y5129_ARATH | MRMFSLQKMAMAFTLLFFACLCSFVSPDAQGDALFALRISLRALPNQLSDWNQNQVNPCTWSQVICDDKNFVTSLTLSDMNFSGTLSSRVGILENLKTLTLKGNGITGEIPEDFGNLTSLTSLDLEDNQLTGRIPSTIGNLKKLQFLTLSRNKLNGTIPESLTGLPNLLNLLLDSNSLSGQIPQSLFEIPKYNFTSNNLNCGGRQPHPCVSAVAHSGDSSKPKTGIIAGVVAGVTVVLFGILLFLFCKDRHKGYRRDVFVDVAGEVDRRIAFGQLKRFAWRELQLATDNFSEKNVLGQGGFGKVYKGVLPDNTKVAVKRLTDFESPGGDAAFQREVEMISVAVHRNLLRLIGFCTTQTERLLVYPFMQNLSLAHRLREIKAGDPVLDWETRKRIALGAARGFEYLHEHCNPKIIHRDVKAANVLLDEDFEAVVGDFGLAKLVDVRRTNVTTQVRGTMGHIAPEYLSTGKSSERTDVFGYGIMLLELVTGQRAIDFSRLEEEDDVLLLDHVKKLEREKRLGAIVDKNLDGEYIKEEVEMMIQVALLCTQGSPEDRPVMSEVVRMLEGEGLAERWEEWQNVEVTRRHEFERLQRRFDWGEDSMHNQDAIELSGGR | 2.7.11.1 | null | phosphorylation [GO:0016310] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF12799;PF08263;PF07714; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | 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; 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; | null | null | null | null | null | Arabidopsis thaliana (Mouse-ear cress) |
C0LGT6 | EFR_ARATH | MKLSFSLVFNALTLLLQVCIFAQARFSNETDMQALLEFKSQVSENNKREVLASWNHSSPFCNWIGVTCGRRRERVISLNLGGFKLTGVISPSIGNLSFLRLLNLADNSFGSTIPQKVGRLFRLQYLNMSYNLLEGRIPSSLSNCSRLSTVDLSSNHLGHGVPSELGSLSKLAILDLSKNNLTGNFPASLGNLTSLQKLDFAYNQMRGEIPDEVARLTQMVFFQIALNSFSGGFPPALYNISSLESLSLADNSFSGNLRADFGYLLPNLRRLLLGTNQFTGAIPKTLANISSLERFDISSNYLSGSIPLSFGKLRNLWWLGIRNNSLGNNSSSGLEFIGAVANCTQLEYLDVGYNRLGGELPASIANLSTTLTSLFLGQNLISGTIPHDIGNLVSLQELSLETNMLSGELPVSFGKLLNLQVVDLYSNAISGEIPSYFGNMTRLQKLHLNSNSFHGRIPQSLGRCRYLLDLWMDTNRLNGTIPQEILQIPSLAYIDLSNNFLTGHFPEEVGKLELLVGLGASYNKLSGKMPQAIGGCLSMEFLFMQGNSFDGAIPDISRLVSLKNVDFSNNNLSGRIPRYLASLPSLRNLNLSMNKFEGRVPTTGVFRNATAVSVFGNTNICGGVREMQLKPCIVQASPRKRKPLSVRKKVVSGICIGIASLLLIIIVASLCWFMKRKKKNNASDGNPSDSTTLGMFHEKVSYEELHSATSRFSSTNLIGSGNFGNVFKGLLGPENKLVAVKVLNLLKHGATKSFMAECETFKGIRHRNLVKLITVCSSLDSEGNDFRALVYEFMPKGSLDMWLQLEDLERVNDHSRSLTPAEKLNIAIDVASALEYLHVHCHDPVAHCDIKPSNILLDDDLTAHVSDFGLAQLLYKYDRESFLNQFSSAGVRGTIGYAAPEYGMGGQPSIQGDVYSFGILLLEMFSGKKPTDESFAGDYNLHSYTKSILSGCTSSGGSNAIDEGLRLVLQVGIKCSEEYPRDRMRTDEAVRELISIRSKFFSSKTTITESPRDAPQSSPQEWMLNTDMHTM | 2.7.11.1 | null | detection of bacterium [GO:0016045]; immune response-regulating signaling pathway [GO:0002764]; phosphorylation [GO:0016310]; plant-type hypersensitive response [GO:0009626]; regulation of anion channel activity [GO:0010359]; response to molecule of bacterial origin [GO:0002237] | endomembrane system [GO:0012505]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; transmembrane receptor protein kinase activity [GO:0019199] | PF00560;PF13855;PF08263;PF00069; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Autophosphorylated after elicitation with elfl18. Autophosphorylation is inhibited by the binding with avrPto1. Phosphorylation at T-836 is required for immune signaling. {ECO:0000269|PubMed:24625928}.; PTM: Polyubiquitinated at the kinase domain mediated by P.syringae AvrPtoB. {ECO:0000269|PubMed:19062288}. | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endomembrane system; Single-pass type I membrane protein. | 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:0000269|PubMed:18158241, ECO:0000269|PubMed:29649442}; 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:0000269|PubMed:18158241, ECO:0000269|PubMed:29649442}; | null | null | null | null | FUNCTION: Constitutes the pattern-recognition receptor (PPR) that determines the specific perception of elongation factor Tu (EF-Tu), a potent elicitor of the defense response to pathogen-associated molecular patterns (PAMPs); phosphorylates BIK1 upon elicitation to regulate immune responses such as defense hormone expression (e.g. jasmonic acid (JA) and salicylic acid (SA)) (PubMed:29649442). Reduces transformation by Rhizobium radiobacter probably by inducing plant defense during the interaction. Binding to the effector AvrPto1 from P.syringae blocks the downstream plant immune response while interaction with hopD2 decreases the phosphorylation level of EFR upon elf18 treatment. Specific endoplasmic reticulum quality control components (ERD2B, CRT3, UGGT and STT3A) are required for the biogenesis of EFR. {ECO:0000269|PubMed:16713565, ECO:0000269|PubMed:19717464, ECO:0000269|PubMed:19763087, ECO:0000269|PubMed:20410299, ECO:0000269|PubMed:21693696, ECO:0000269|PubMed:24625928, ECO:0000269|PubMed:29649442}. | Arabidopsis thaliana (Mouse-ear cress) |
C0LGU0 | PRK1_ARATH | MPPMQARTLSVYNVMVPLVCLLLFFSTPTHGLSDSEAILKFKESLVVGQENALASWNAKSPPCTWSGVLCNGGSVWRLQMENLELSGSIDIEALSGLTSLRTLSFMNNKFEGPFPDFKKLAALKSLYLSNNQFGGDIPGDAFEGMGWLKKVHLAQNKFTGQIPSSVAKLPKLLELRLDGNQFTGEIPEFEHQLHLLNLSNNALTGPIPESLSMTDPKVFEGNKGLYGKPLETECDSPYIEHPPQSEARPKSSSRGPLVITAIVAALTILIILGVIFLLNRSYKNKKPRLAVETGPSSLQKKTGIREADQSRRDRKKADHRKGSGTTKRMGAAAGVENTKLSFLREDREKFDLQDLLKASAEILGSGCFGASYKAVLSSGQMMVVKRFKQMNNAGRDEFQEHMKRLGRLMHHNLLSIVAYYYRKEEKLLVCDFAERGSLAINLHSNQSLGKPSLDWPTRLKIVKGVAKGLFYLHQDLPSLMAPHGHLKSSNVLLTKTFEPLLTDYGLIPLINQEKAQMHMAAYRSPEYLQHRRITKKTDVWGLGILILEILTGKFPANFSQSSEEDLASWVNSGFHGVWAPSLFDKGMGKTSHCEGQILKLLTIGLNCCEPDVEKRLDIGQAVEKIEELKEREGDDDDFYSTYVSETDGRSSKGESCESISFA | 2.7.11.1 | null | phosphorylation [GO:0016310] | apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF08263;PF00069; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18591430}; Single-pass type I membrane protein {ECO:0000269|PubMed:18591430}. Note=Preferentially localized to the apical region of the pollen tube plasma membrane. | 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}; 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}; | null | null | null | null | FUNCTION: Receptor-like kinase involved in the control of pollen germination and pollen tube polar growth (PubMed:23024212). {ECO:0000269|PubMed:23024212}. | Arabidopsis thaliana (Mouse-ear cress) |
C0LGU5 | Y5457_ARATH | MEISLMKFLFLGIWVYYYSVLDSVSAMDSLLSPKGVNYEVAALMSVKNKMKDEKEVLSGWDINSVDPCTWNMVGCSSEGFVVSLEMASKGLSGILSTSIGELTHLHTLLLQNNQLTGPIPSELGQLSELETLDLSGNRFSGEIPASLGFLTHLNYLRLSRNLLSGQVPHLVAGLSGLSFLDLSFNNLSGPTPNISAKDYRIVGNAFLCGPASQELCSDATPVRNATGLSEKDNSKHHSLVLSFAFGIVVAFIISLMFLFFWVLWHRSRLSRSHVQQDYEFEIGHLKRFSFREIQTATSNFSPKNILGQGGFGMVYKGYLPNGTVVAVKRLKDPIYTGEVQFQTEVEMIGLAVHRNLLRLFGFCMTPEERMLVYPYMPNGSVADRLRDNYGEKPSLDWNRRISIALGAARGLVYLHEQCNPKIIHRDVKAANILLDESFEAIVGDFGLAKLLDQRDSHVTTAVRGTIGHIAPEYLSTGQSSEKTDVFGFGVLILELITGHKMIDQGNGQVRKGMILSWVRTLKAEKRFAEMVDRDLKGEFDDLVLEEVVELALLCTQPHPNLRPRMSQVLKVLEGLVEQCEGGYEARAPSVSRNYSNGHEEQSFIIEAIELSGPR | 2.7.11.1 | null | anther development [GO:0048653]; homeostasis of number of meristem cells [GO:0007639]; phosphorylation [GO:0016310] | membrane [GO:0016020] | ATP binding [GO:0005524]; coreceptor activity [GO:0015026]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF08263;PF07714; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | 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; 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; | null | null | null | null | null | Arabidopsis thaliana (Mouse-ear cress) |
C0LGU7 | MDIS1_ARATH | MGCRWNPIGFQFSCFMFLIITLQSRSSLSLESEGFVLLKFRARVDSDPHGTLANWNVSDHDHFCSWFGVTCVDNKVQMLNLSGCSLGGTLAPELSQLSELRSLILSKNKLSGDIPNEFASFAKLEFLDLRDNNLNGVVPPELNKVLTPENLLLSGNKFAGFMTVKFLRLQSLYKVQMNKNRELSSVSADVLDCVNRKLGYCVSRRSLITRNKAKAFVLRIRATSRHYMVRRESHGKNYVVNYHPSENETSIFKRRELLEETSNLAAMPAPDTPSPSPEIITIVFPRSSGSFPALTNAKKRIPPLIPPSSPPPLPTNNTIASDPPRKFEEKSKGFKDVWLYVVIGVAAFVAMLIIVAVIFFFRKRAVKSIGPWKTGLSGQLQKAFVTGVPKLNRSELETACEDFSNIIEAFDGYTVYKGTLSSGVEIAVASTAILETREWTRAMEMTYRRRIDTMSRVNHKNFINLIGYCEEDEPFNRMMVFEYAPNGTLFEHLHDKEMEHLDWNARTRIIMGTAYCLQYMHELNPPISHTKLVSSAIYLTDDYAAKVGEVPFSGQTGSKPRKPMSGDLDQSLLPLPPEPETNVYSFGVLMLEIISGKLSDSEEEGSILKWASKYLENDNLRDMIDPTLTTYKEEELEAICDVARHCLKLDESQRPKMKYVVQQLKEVINISQEQATPRLSPLWWAELEILSSEAT | 2.7.11.1 | null | phosphorylation [GO:0016310] | endomembrane system [GO:0012505]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF13855;PF08263;PF07714; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Phosphorylated by MIK1. {ECO:0000269|PubMed:26863186}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26863186}; Single-pass type I membrane protein {ECO:0000305}. Endomembrane system {ECO:0000269|PubMed:26863186}. Note=LURE1.2 binding triggers endocytosis in the pollen tube tip. {ECO:0000269|PubMed:26863186}. | 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}; 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}; | null | null | null | null | FUNCTION: Involved in the pollen tube perception of the female signal. {ECO:0000269|PubMed:26863186}. | Arabidopsis thaliana (Mouse-ear cress) |
C0LGV1 | RGI2_ARATH | MSLQMPIPRKKALTVSHFSITLSLFLAFFISSTSASTNEVSALISWLHSSNSPPPSVFSGWNPSDSDPCQWPYITCSSSDNKLVTEINVVSVQLALPFPPNISSFTSLQKLVISNTNLTGAISSEIGDCSELIVIDLSSNSLVGEIPSSLGKLKNLQELCLNSNGLTGKIPPELGDCVSLKNLEIFDNYLSENLPLELGKISTLESIRAGGNSELSGKIPEEIGNCRNLKVLGLAATKISGSLPVSLGQLSKLQSLSVYSTMLSGEIPKELGNCSELINLFLYDNDLSGTLPKELGKLQNLEKMLLWQNNLHGPIPEEIGFMKSLNAIDLSMNYFSGTIPKSFGNLSNLQELMLSSNNITGSIPSILSNCTKLVQFQIDANQISGLIPPEIGLLKELNIFLGWQNKLEGNIPDELAGCQNLQALDLSQNYLTGSLPAGLFQLRNLTKLLLISNAISGVIPLEIGNCTSLVRLRLVNNRITGEIPKGIGFLQNLSFLDLSENNLSGPVPLEISNCRQLQMLNLSNNTLQGYLPLSLSSLTKLQVLDVSSNDLTGKIPDSLGHLISLNRLILSKNSFNGEIPSSLGHCTNLQLLDLSSNNISGTIPEELFDIQDLDIALNLSWNSLDGFIPERISALNRLSVLDISHNMLSGDLSALSGLENLVSLNISHNRFSGYLPDSKVFRQLIGAEMEGNNGLCSKGFRSCFVSNSSQLTTQRGVHSHRLRIAIGLLISVTAVLAVLGVLAVIRAKQMIRDDNDSETGENLWTWQFTPFQKLNFTVEHVLKCLVEGNVIGKGCSGIVYKAEMPNREVIAVKKLWPVTVPNLNEKTKSSGVRDSFSAEVKTLGSIRHKNIVRFLGCCWNKNTRLLMYDYMSNGSLGSLLHERSGVCSLGWEVRYKIILGAAQGLAYLHHDCVPPIVHRDIKANNILIGPDFEPYIGDFGLAKLVDDGDFARSSNTIAGSYGYIAPEYGYSMKITEKSDVYSYGVVVLEVLTGKQPIDPTIPDGLHIVDWVKKIRDIQVIDQGLQARPESEVEEMMQTLGVALLCINPIPEDRPTMKDVAAMLSEICQEREESMKVDGCSGSCNNGRERGKDDSTSSVMQQTAKYLRSSSTSFSASSLLYSSSSSATSNVRPNLK | 2.7.11.1 | null | maintenance of meristem identity [GO:0010074]; maintenance of root meristem identity [GO:0010078]; phosphorylation [GO:0016310]; regulation of root development [GO:2000280]; regulation of root meristem growth [GO:0010082]; root meristem growth [GO:0010449] | membrane [GO:0016020] | ATP binding [GO:0005524]; peptide binding [GO:0042277]; peptide receptor activity [GO:0001653]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF13855;PF08263;PF07714; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Phosphorylated and ubiquitinated upon interaction with RGF1, thus leading to activation a subsequent degradation (By similarity). Stabilized by UBP12 and UBP13-mediated deubiquitination (By similarity). {ECO:0000250|UniProtKB:Q9LHP4}.; PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O22476}. | SUBCELLULAR LOCATION: 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:0000255|PROSITE-ProRule:PRU00159}; 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:0000255|PROSITE-ProRule:PRU00159}; | null | null | null | null | FUNCTION: Together with RGI1, RGI3, RGI4 and RGI5, acts as a receptor of RGF peptides (e.g. RGF1, GLV5/CLEL1/RGF2, GLV7/CLEL3/RGF3, GLV3/RGF4, GLV10/CLEL7/RGF5 and RGF10/CLELN), peptide hormones which maintain the postembryonic root stem cell niche by regulating the expression levels and patterns of the transcription factor PLETHORA (PLT, e.g. PLT1 and PLT2) (PubMed:27001831, PubMed:27229311, PubMed:27229312). Links RGF peptides signal with their downstream components (PubMed:27001831, PubMed:27229311). {ECO:0000269|PubMed:27001831, ECO:0000269|PubMed:27229311, ECO:0000269|PubMed:27229312}. | Arabidopsis thaliana (Mouse-ear cress) |
C0LGW2 | PAM74_ARATH | MDSPCWLLLLLLGAFAIIGCVQAQDQQEFISLDCGLPMTEPSSYTESVTGLRFSSDAEFIQTGESGKIQASMENDYLKPYTRLRYFPEERRNCYSLSVDKNRKYLIRARFIYGNYDGRNSNPIFELHLGPNLWATIDLQKFVNGTMEEILHTPTSNSLNVCLVKTGTTTPLISALELRPLGNNSYLTDGSLNLFVRIYLNKTDGFLRYPDDIYDRRWHNYFMVDDWTQIFTTLEVTNDNNYEPPKKALAAAATPSNASAPLTISWPPDNPGDQYYLYSHFSEIQDLQTNDTREFDILWDGAVVEEGFIPPKLGVTTIHNLSPVTCKGENCIYQLIKTSRSTLPSLLNALEIYTVIQFPRSETNENDVVAVKNIEAAYKLSRIRWQGDPCVPQKYAWDGLNCSNNTDVSKPPRVLSLNLSSSGLTGIIAAAIQNLTHLEKLDLSNNTLTGVVPEFLAQMKSLVIINLSGNNLSGPLPQGLRREGLELLVQGNPRLCLSGSCTEKNSKKKFPVVIVASVASVAIIVAVLVIIFVLSKKKSSTVGALQPPLSMPMVHDNSPEPSIETKKRRFTYSEVIKMTNNFQRVVGEGGFGVVCHGTINGSEQVAVKVLSQSSSQGYKHFKAEVDLLLRVHHTNLVSLVGYCDERDHLALIYEFLPKGDLRQHLSGKSGGSFINWGNRLRIALEAALGLEYLHSGCTPPIVHRDIKTTNILLDEQLKAKLADFGLSRSFPIGGETHISTVVAGTPGYLDPEYYQTTRLGEKSDVYSFGIVLLEIITNQPVIDQSRSKSHISQWVGFELTRGDITKIMDPNLNGDYESRSVWRVLELAMSCANPSSVNRPNMSQVANELKECLVSENLRENMNMDSQNSLKVSMSFDTELFPRAR | 2.7.11.1 | null | phosphorylation [GO:0016310] | membrane [GO:0016020] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF13855;PF12819;PF00069; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | 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; 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; | null | null | null | null | FUNCTION: Required for accurate photosynthesis. {ECO:0000269|Ref.4}. | Arabidopsis thaliana (Mouse-ear cress) |
C0LGW6 | ERL1_ARATH | MKEKMQRMVLSLAMVGFMVFGVASAMNNEGKALMAIKGSFSNLVNMLLDWDDVHNSDLCSWRGVFCDNVSYSVVSLNLSSLNLGGEISPAIGDLRNLQSIDLQGNKLAGQIPDEIGNCASLVYLDLSENLLYGDIPFSISKLKQLETLNLKNNQLTGPVPATLTQIPNLKRLDLAGNHLTGEISRLLYWNEVLQYLGLRGNMLTGTLSSDMCQLTGLWYFDVRGNNLTGTIPESIGNCTSFQILDISYNQITGEIPYNIGFLQVATLSLQGNRLTGRIPEVIGLMQALAVLDLSDNELVGPIPPILGNLSFTGKLYLHGNMLTGPIPSELGNMSRLSYLQLNDNKLVGTIPPELGKLEQLFELNLANNRLVGPIPSNISSCAALNQFNVHGNLLSGSIPLAFRNLGSLTYLNLSSNNFKGKIPVELGHIINLDKLDLSGNNFSGSIPLTLGDLEHLLILNLSRNHLSGQLPAEFGNLRSIQMIDVSFNLLSGVIPTELGQLQNLNSLILNNNKLHGKIPDQLTNCFTLVNLNVSFNNLSGIVPPMKNFSRFAPASFVGNPYLCGNWVGSICGPLPKSRVFSRGALICIVLGVITLLCMIFLAVYKSMQQKKILQGSSKQAEGLTKLVILHMDMAIHTFDDIMRVTENLNEKFIIGYGASSTVYKCALKSSRPIAIKRLYNQYPHNLREFETELETIGSIRHRNIVSLHGYALSPTGNLLFYDYMENGSLWDLLHGSLKKVKLDWETRLKIAVGAAQGLAYLHHDCTPRIIHRDIKSSNILLDENFEAHLSDFGIAKSIPASKTHASTYVLGTIGYIDPEYARTSRINEKSDIYSFGIVLLELLTGKKAVDNEANLHQLILSKADDNTVMEAVDPEVTVTCMDLGHIRKTFQLALLCTKRNPLERPTMLEVSRVLLSLVPSLQVAKKLPSLDHSTKKLQQENEVRNPDAEASQWFVQFREVISKSSI | 2.7.11.1 | null | embryo sac development [GO:0009553]; phosphorylation [GO:0016310]; plant ovule development [GO:0048481]; stomatal complex morphogenesis [GO:0010103] | 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]; signaling receptor binding [GO:0005102] | 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:0000269|PubMed:22241782, ECO:0000303|PubMed:14985254}; Single-pass type I membrane protein {ECO:0000305}. | 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; 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; | null | null | null | null | FUNCTION: Receptor kinase that regulates inflorescence architecture and organ shape as well as stomatal patterning, including density and clustering, together with ER and ERL2. Redundantly involved with ER in procambial development regulation. Forms a functional ligand-receptor pair with EPF1 (AC Q8S8I4) (PubMed:22241782). Forms a constitutive complex with TMM involved in the recognition of the stomatal regulatory peptides EPF1, EPF2 and EPFL9/STOMAGEN (PubMed:28536146). {ECO:0000269|PubMed:14985254, ECO:0000269|PubMed:16002616, ECO:0000269|PubMed:17652352, ECO:0000269|PubMed:22241782, ECO:0000269|PubMed:23881395, ECO:0000269|PubMed:28536146}. | Arabidopsis thaliana (Mouse-ear cress) |
C0LGX3 | HSL2_ARATH | MLTNTNLFFFLSLLLLSCFLQVSSNGDAEILSRVKKTRLFDPDGNLQDWVITGDNRSPCNWTGITCHIRKGSSLAVTTIDLSGYNISGGFPYGFCRIRTLINITLSQNNLNGTIDSAPLSLCSKLQNLILNQNNFSGKLPEFSPEFRKLRVLELESNLFTGEIPQSYGRLTALQVLNLNGNPLSGIVPAFLGYLTELTRLDLAYISFDPSPIPSTLGNLSNLTDLRLTHSNLVGEIPDSIMNLVLLENLDLAMNSLTGEIPESIGRLESVYQIELYDNRLSGKLPESIGNLTELRNFDVSQNNLTGELPEKIAALQLISFNLNDNFFTGGLPDVVALNPNLVEFKIFNNSFTGTLPRNLGKFSEISEFDVSTNRFSGELPPYLCYRRKLQKIITFSNQLSGEIPESYGDCHSLNYIRMADNKLSGEVPARFWELPLTRLELANNNQLQGSIPPSISKARHLSQLEISANNFSGVIPVKLCDLRDLRVIDLSRNSFLGSIPSCINKLKNLERVEMQENMLDGEIPSSVSSCTELTELNLSNNRLRGGIPPELGDLPVLNYLDLSNNQLTGEIPAELLRLKLNQFNVSDNKLYGKIPSGFQQDIFRPSFLGNPNLCAPNLDPIRPCRSKRETRYILPISILCIVALTGALVWLFIKTKPLFKRKPKRTNKITIFQRVGFTEEDIYPQLTEDNIIGSGGSGLVYRVKLKSGQTLAVKKLWGETGQKTESESVFRSEVETLGRVRHGNIVKLLMCCNGEEFRFLVYEFMENGSLGDVLHSEKEHRAVSPLDWTTRFSIAVGAAQGLSYLHHDSVPPIVHRDVKSNNILLDHEMKPRVADFGLAKPLKREDNDGVSDVSMSCVAGSYGYIAPEYGYTSKVNEKSDVYSFGVVLLELITGKRPNDSSFGENKDIVKFAMEAALCYPSPSAEDGAMNQDSLGNYRDLSKLVDPKMKLSTREYEEIEKVLDVALLCTSSFPINRPTMRKVVELLKEKKSLE | 2.7.11.1 | null | defense response to Gram-negative bacterium [GO:0050829]; lateral root morphogenesis [GO:0010102]; leaf abscission [GO:0060866]; phosphorylation [GO:0016310]; regulation of gene expression [GO:0010468] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF12799;PF08263;PF00069; | 3.80.10.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | 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; 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; | null | null | null | null | FUNCTION: Receptor-like serine/threonine-kinase acting on substrates that controls floral organ abscission. Regulated by the 'INFLORESCENCE DEFICIENT IN ABSCISSION' (IDA) family of ligands. {ECO:0000269|PubMed:18809915}. | Arabidopsis thaliana (Mouse-ear cress) |
C0LLJ0 | IMA8_MOUSE | MATSKAPKERLKNYKYRGKEMSLPRQQRIASSLQLRKTRKDEQVLKRRNIDLFSSDMVSQALVKEVNFTLDDIIQAVNSSDPILHFRATRAAREMISQENTPPLNLIIEAGLIPKLVDFLKATPHPKLQFEAAWVLTNIASGTSEQTRAVVKEGAIQPLIELLCSPHLTVSEQAVWALGNIAGDCAEFRDCVISNNAIPHLINLISKGIPITFLRNISWTLSNLCRNKDPYPSESAVRQMLPPLCQLLLHRDNEILADTCWALSYLTKGGKEYIHHVVTTGILPRLVELMTSSELSISIPCLHTIGNIVAGTDEQTQMAIDAGMLKVLGQVLKHPKTSIQVLAAWTMSNVAAGPRHQVEQLLCNLLPILVDLLRNAELKVQKEVVCTVINIATGASQDQLTLLAHSGILEPMLSLLSAPDLEVVIIVLDIISYLLQHIDNLQEKKRLYFQIEKFGGFEKIECLQHHHNISISNSALDIIEKYFCEDGDGDSLPGPGLRV | null | null | blastocyst development [GO:0001824]; epigenetic regulation of gene expression [GO:0040029]; negative regulation of gene expression [GO:0010629]; NLS-bearing protein import into nucleus [GO:0006607]; positive regulation of gene expression [GO:0010628]; protein import into nucleus [GO:0006606] | cytosol [GO:0005829]; female germ cell nucleus [GO:0001674]; NLS-dependent protein nuclear import complex [GO:0042564]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819] | nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139] | PF00514;PF16186;PF01749; | 1.20.5.690;1.25.10.10; | Importin alpha family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20699224}. Note=In MII-stage oocytes, localizes to the spindle. | null | null | null | null | null | FUNCTION: Functions in nuclear protein import. {ECO:0000250|UniProtKB:A9QM74}. | Mus musculus (Mouse) |
C0LNR0 | FABH_LISM4 | MNAGILGVGKYVPEKIVTNFDLEKIMDTSDEWIRTRTGIEERRIARDDEYTHDLAYEAAKVAIKNAGLTPDDIDLFIVATVTQEATFPSVANIIQDRLGAKNAAGMDVEAACAGFTFGVVTAAQFIKTGAYKNIVVVGADKLSKITNWDDRTTAVLFGDGAGAVVMGPVSDDHGLLSFDLGSDGSGGKYLNLDENKKIYMNGREVFRFAVRQMGEASLRVLERAGLEKEDLDLLIPHQANIRIMEASRERLNLPEEKLMKTVHKYGNTSSSSIALALVDAVEEGRIKDNDNVLLVGFGGGLTWGALIIRWGK | 2.3.1.180; 2.3.1.300 | null | fatty acid biosynthetic process [GO:0006633] | cytoplasm [GO:0005737] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; beta-ketoacyl-acyl-carrier-protein synthase III activity [GO:0033818] | PF08545;PF08541; | 3.40.47.10; | Thiolase-like superfamily, FabH family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01815}. | CATALYTIC ACTIVITY: Reaction=(2S)-2-methylbutanoyl-CoA + H(+) + malonyl-[ACP] = (4S)-4-methyl-3-oxohexanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42276, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:17148, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:78449, ChEBI:CHEBI:88166, ChEBI:CHEBI:167462; EC=2.3.1.300; Evidence={ECO:0000269|PubMed:19863661}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42277; Evidence={ECO:0000269|PubMed:19863661}; CATALYTIC ACTIVITY: Reaction=2-methylpropanoyl-CoA + H(+) + malonyl-[ACP] = 4-methyl-3-oxopentanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42268, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9940, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338, ChEBI:CHEBI:78449, ChEBI:CHEBI:78820; EC=2.3.1.300; Evidence={ECO:0000269|PubMed:19863661}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42269; Evidence={ECO:0000269|PubMed:19863661}; CATALYTIC ACTIVITY: Reaction=3-methylbutanoyl-CoA + H(+) + malonyl-[ACP] = 5-methyl-3-oxohexanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42272, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9941, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57345, ChEBI:CHEBI:78449, ChEBI:CHEBI:78822; EC=2.3.1.300; Evidence={ECO:0000269|PubMed:19863661}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42273; Evidence={ECO:0000269|PubMed:19863661}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000269|PubMed:19863661}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12081; Evidence={ECO:0000269|PubMed:19863661}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11 uM for 2-methylbutanoyl-CoA (at 30 degrees Celsius) {ECO:0000269|PubMed:19863661}; KM=6.3 uM for 2-methylbutanoyl-CoA (at 10 degrees Celsius) {ECO:0000269|PubMed:19863661}; KM=24.3 uM for 2-methylpropanoyl-CoA (at 30 degrees Celsius) {ECO:0000269|PubMed:19863661}; KM=30.7 uM for 2-methylpropanoyl-CoA (at 10 degrees Celsius) {ECO:0000269|PubMed:19863661}; KM=5.3 uM for 3-methylbutanoyl-CoA (at 30 degrees Celsius) {ECO:0000269|PubMed:19863661}; KM=16.9 uM for 3-methylbutanoyl-CoA (at 10 degrees Celsius) {ECO:0000269|PubMed:19863661}; KM=98.5 uM for acetyl-CoA (at 30 degrees Celsius) {ECO:0000269|PubMed:19863661}; Vmax=16.5 nmol/min/ng enzyme with 2-methylbutanoyl-CoA as substrate (at 30 degrees Celsius) {ECO:0000269|PubMed:19863661}; Vmax=13 nmol/min/ng enzyme with 2-methylbutanoyl-CoA as substrate (at 10 degrees Celsius) {ECO:0000269|PubMed:19863661}; Vmax=11.4 nmol/min/ng enzyme with 2-methylpropanoyl-CoA as substrate (at 30 degrees Celsius) {ECO:0000269|PubMed:19863661}; Vmax=28.5 nmol/min/ng enzyme with 2-methylpropanoyl-CoA as substrate (at 10 degrees Celsius) {ECO:0000269|PubMed:19863661}; Vmax=4.3 nmol/min/ng enzyme with 3-methylbutanoyl-CoA as substrate (at 30 degrees Celsius) {ECO:0000269|PubMed:19863661}; Vmax=5.1 nmol/min/ng enzyme with 3-methylbutanoyl-CoA as substrate (at 10 degrees Celsius) {ECO:0000269|PubMed:19863661}; Vmax=7.5 nmol/min/ng enzyme with acetyl-CoA as substrate (at 30 degrees Celsius) {ECO:0000269|PubMed:19863661}; Note=kcat is 27.5 min(-1) (at 30 degrees Celsius) and 2.8 min(-1) (at 10 degrees Celsius) with 2-methylbutanoyl-CoA as substrate. kcat is 19.0 min(-1) (at 30 degrees Celsius) and 6.1 min(-1) (at 10 degrees Celsius) with 2-methylpropanoyl-CoA as substrate. kcat is 7.2 min(-1) (at 30 degrees Celsius) and 1.1 min(-1) (at 10 degrees Celsius) with 3-methylbutanoyl-CoA as substrate. kcat is 0.04 min(-1) (at 30 degrees Celsius) with acetyl-CoA as substrate. {ECO:0000269|PubMed:19863661}; | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000305|PubMed:19863661}. | null | null | FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities (PubMed:19863661). Can use branched-chain acyl-CoAs, with a preference for 2-methylbutanoyl-CoA, the precursor of odd-numbered anteiso fatty acids, at 30 degrees Celsius, which is further increased at a low temperature (PubMed:19863661). Shows weak activity with acetyl-CoA (PubMed:19863661). {ECO:0000269|PubMed:19863661}. | Listeria monocytogenes serotype 1/2a (strain 10403S) |
C0LT23 | CERK_ORYSJ | MEGGGEALFLDGVGEVTVAVGDDGLSFQPLHQEVSSSCWSSIIMQPKLESKLKFSDVYAVELLEVGPVCEPWNARATVQGKINTEMNRFVIHTVTRPRKRPSPWVPCEYIFGHKDQQTCKTWVEHIKTCINKEQDRPKSLMVFVHPLCGKGRGCKNWETVAPLFERAKVKTKVIVTQRAGHAYDTLASLSDKDLKKFDGVIAVGGDGLFNEILNGLLSTRHTNSYPPTPEGFGYFRNNMKCQEHRNNDLSNSELTGDDANAISGSSNTPDDHEPLLSTTRSTGLDISSSDSSDEPCNGDQVPLVSFPNNWFRLGIIPSGSTDAIVLSTTGERDPVTSALLIILGRRISLDIAQVVRWKSSPSAEVSPTVRYAASFAGYGFYGEVIRESEKYRWMGPARYDFSGTMVFLKHRSYEAKVAFLENGNTHSLTASAENNANGVQTLQYHQNRHRKTICRTNCLICKGTSTSEQNSEDENPDSSRTACETPKWVWSKGRFLSVGAAVISCRNERAPDGLVADAHLSDGFLHLLLIRDCPLPFYLWHLTQFTKKGSDPLSFKFVEHHKTQAFTFISSHDESVWNLDGELLQACEVSVQAFRGLVNLFASGPEV | 2.7.1.138 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:21483860}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21483860}; | ceramide metabolic process [GO:0006672]; negative regulation of programmed cell death [GO:0043069]; phosphorylation [GO:0016310] | null | ATP binding [GO:0005524]; ceramide kinase activity [GO:0001729]; dihydroceramide kinase activity [GO:0102773]; metal ion binding [GO:0046872] | PF19280;PF00781; | 2.60.200.40; | null | null | null | CATALYTIC ACTIVITY: Reaction=an N-acylsphing-4-enine + ATP = ADP + an N-acylsphing-4-enine 1-phosphate + H(+); Xref=Rhea:RHEA:17929, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674, ChEBI:CHEBI:456216; EC=2.7.1.138; Evidence={ECO:0000269|PubMed:21483860}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.1 uM for C6 ceramide {ECO:0000269|PubMed:21483860}; KM=36.4 uM for ATP {ECO:0000269|PubMed:21483860}; Vmax=4.7 nmol/min/mg enzyme toward C6 ceramide {ECO:0000269|PubMed:21483860}; Vmax=2.6 nmol/min/mg enzyme toward ATP {ECO:0000269|PubMed:21483860}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 (at 40 degrees Celsius). {ECO:0000269|PubMed:21483860}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:21483860}; | FUNCTION: Catalyzes specifically the phosphorylation of ceramide to form ceramide 1-phosphate. Possesses activity on ceramide analog (C6 synthetic ceramide) in vitro. Ceramide is a critical sphingolipid metabolite that induces programmed cell death (PCD) in plants and ceramide-1-phosphate has a PCD suppressive effect. Thus, ceramide phosphorylation plays a role in the modulation of PCD and CERK activity is crucial for the maintenance of cell viability. {ECO:0000269|PubMed:21483860}. | Oryza sativa subsp. japonica (Rice) |
C0LU16 | MED21_ARATH | MDIISQLQEQVNTIAAITFNAFGTLQRDAPPVQLSPNYPEPPATTTVTDDATPFPEQPKQLSAGLVKAAKQFDALVAALPLSEGGEGAQLKRIAELQVENDLVGQELQKQLEAAEKELKQVQELFGQAADNCLNMKKPE | null | null | defense response to fungus [GO:0050832]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357] | mediator complex [GO:0016592]; polar nucleus [GO:0043078] | transcription coregulator activity [GO:0003712] | PF11221; | 6.10.280.10; | Mediator complex subunit 21 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | 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. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Required for embryo development and defense against necrotrophic fungal pathogens. | Arabidopsis thaliana (Mouse-ear cress) |
C0M0V4 | AAH1_SOYBN | MYSATASNTFFLLSCFLLFCLLSAPSCVSMFSGIETGDLEKRDDLFPQILRDEAVARLYELGKVSDASGYLERTFLSPASMKAIDLIRKWMEDAGLRTWVDQMGNVHGRVDGANENAEALLIGSHMDTVVDAGMFDGSLGIVSAISAVKAMHVNGKLQKLKRPVEVIAFSDEEGVRFQTTFLGSGAIAGILPGTTLEISDKREVMIKDFLKENSMDITEESLLKLKYDPKSVWGYVEVHIEQGPVLEQVGFPLGVVKGIAGQTRLKVTVRGSQGHAGTVPMSMRQDPMAAAAEQIVVLESLCKHPEEYLSYDGHCSDSTVKSLSSSLVCTVGEISTWPSASNVIPGQVTYTVDIRAIDDLGREAVIYDLSKQIYQICDKRSVSCIIEHKHDAGAVICDSDLSSQLKSAAYSALKKMEGDIQDEVPTLMSGAGHDAMAISHLTKVGMLFVRCRGGISHSPQEHVLDNDVWAAGLATLSFLENLS | 3.5.3.9 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:18065556}; Note=Binds 2 manganese ions per subunit. {ECO:0000250|UniProtKB:Q8VXY9}; | purine nucleobase metabolic process [GO:0006144] | endoplasmic reticulum [GO:0005783] | allantoate deiminase activity [GO:0047652]; metal ion binding [GO:0046872] | PF07687;PF01546; | 3.30.70.360;3.40.630.10; | Peptidase M20A family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:18065556}. | CATALYTIC ACTIVITY: Reaction=allantoate + 2 H(+) + H2O = (S)-2-ureidoglycine + CO2 + NH4(+); Xref=Rhea:RHEA:27485, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17536, ChEBI:CHEBI:28938, ChEBI:CHEBI:59947; EC=3.5.3.9; Evidence={ECO:0000269|PubMed:18065556, ECO:0000269|PubMed:23940254}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=72 uM for allantoate {ECO:0000269|PubMed:23940254}; Note=kcat is 37 sec(-1) for allantoate. {ECO:0000269|PubMed:23940254}; | null | null | null | FUNCTION: Involved in the catabolism of purine nucleotides. Can use allantoate as substrate. The sequential activity of AAH, UGLYAH and UAH allows a complete purine breakdown without the intermediate generation of urea. {ECO:0000269|PubMed:18065556, ECO:0000269|PubMed:19129162}. | Glycine max (Soybean) (Glycine hispida) |
C0MAL8 | THSA_STRE4 | MFIIKGEVSRKDLIREIEKAIKSDELGAFIGAGLSIPAGFCSWKELLREPAEEIGLDVEKESDLVNLAQYYSNSKKRTSIDDLIKGQFSQLVKPTENHKLLSQLPISTFWTTNYDKLIEKALENNMKKPYVKTKDEQLRGTNHNFDAIVYKLHGDVETPEDAVITRSDYEEFGYNKRKLFREVLEGDLLTKTFLFLGFSFEDPNFNYVIGRLRVLLDEKNTRKHYCIMKRVQDADEDYEYKKARQELQIEDLNRYGIFTYLVNKYDEITEILSTLVDRFRRKTIFISGSAYSYSAYSQKTGENFIHKLSFELSKNGYHIVNGYGKGVGEFVLNGVADYCLTHKSKINDFLTLMPFPQNSSLGIDLDKLYKENREQMIESCGIAIFLFGNKEAEDIASGVMDEYELSKKHGLVCLPIEYTGGASKEIYDQTTQEISDKNTISAIEQANKQCDGDIDMSVKNIVQAVKILNKEEF | 3.2.2.5 | null | defense response to virus [GO:0051607] | null | hydrolase activity [GO:0016787]; nucleotide binding [GO:0000166] | PF13289;PF18185; | null | Soluble Thoeris ThsA family | 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=3.2.2.5; Evidence={ECO:0000269|PubMed:36048923}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence={ECO:0000269|PubMed:36048923}; | null | null | null | null | FUNCTION: NAD(+) hydrolyzing component (NADase) of the Thoeris antiviral defense system, composed of ThsA and ThsB (maybe SEQ_0762). Has a low NADase activity that is strongly activated by 3' cyclic ADP-D-ribose (3'cADPR) and weakly activated by 2'cADPR (PubMed:36048923). Upon activation binds and hydrolyzes NAD(+), leading to cell death and inhibition of phage replication (By similarity). {ECO:0000250|UniProtKB:J8G6Z1, ECO:0000269|PubMed:36048923}. | Streptococcus equi subsp. equi (strain 4047) |
C0MHL9 | POLG_SAFV | MACKHGYPLLCPLCTALDITPDGSFTLLFDNEWYPTDLLTVNLDDDVFYPLDTNMDWTDLPLIQDIVMEPQGNSNSSDKNNSQSSGNEGVIINNYYSNQYQNSIDLSANANGVGKENSKPQGQLMNILGSAADAFKNIAPLLMDQNTEEMTNLSDRVSSDTAGNTATNTQSTVGRLFGFGQRHKGKHPASCADTATDKVLAAERYYTIKLASWTKTQESFDHIRVPLPHALAGENGGVFSSTLRRHYLCKCGWRIQVQCNASQFHAGSLLVFMAPEFDTSNHSTEVEPRADTAFKVDANWQKHAQILTGHAYVNTTTKVNVPLALNHQNFWQWTTYPHQILNLRTNTTCDLEVPYVNVCPTSSWTQHANWTLVIAVLTPLQYSQGSATTIEITASIQPVKPVFNGLRHTVVNPQSPFPVTVREHAGTFFSTTPDTTVPVYGNTISTPFDYMCGEFTDLLSLCKIPTFLGNLDSNKKRIPYFSATNSTPATPLVTYQVTLSCSCMANSMLAAVARNFNQYRGSLNYLFVFTGSAMTKGKFLISYTPPGAGEPKTLDQAMQATYAIWDLGLNSSYNFTVPFISPTHYRQTSYNTPTITSVDGWLTVWQLTPLTYPLGVPNDSHILTLVSGGDDFTLRMPVTFTKYVPQGVDNAEKGKVSDDNASTDFVAEPVKLPENQTRVSFVYDRSTLSSVLQSTSDVSSKFTPSTAKNLQNSILLTPLPSDIVNNSVLPEQERWISFASPTTQKPPYKTKQDWNFIMFSPFTYYKCDLEVTLSKNDRETISSVVRYVPCGAPSDLSDQTMPQTPSLADTRDPHMWVVGQGTTNQISFVIPYTSPLSVLPSVWFNGFSNFDNSSRFGVAPNADFGRLLLQGQGTFSVHYRYKKMRVFCPRPTVFIPWPNPQDTKIKSVRPTPTLELQNPISIYRVDLFINFSDEIIQFTYKVHGRTVCQYEIPGFGLSRSGRLLVCMGEKPCQLPISTPKCFYHIVFTGSRNSFGVSIYKARYRPWKQPLHDELHDYGFSTFTDFFKAVRDYHASYYKQRLQHDIETNPGPVQSVFQLQGGVLTKSQAPMSGLQSMLLRAIGIEADCTEFTRAVNLITDLCNTWESAKTTLSSPEFWTKMVMRIVKMFAASVLYLHNPDLTTTVCLSLMAGIDILTNDSVFNWLSTKLSKFFHTPAPPIVPLLQQQSPIREANDSFNLAKNIEWAIKTIKRIVEWITSWFKQEETSPQAKLDKMLTDFPEHCNSILAMRNGRKAYTDCASAFKYFEQLYNLAVQCKRIPLATLCEKFKNKHDHAVARPEPVVVVLRGNAGQGKSVTSQIIAQAVSKLSFGRQSVYSLPPDSDYLDGYENQYSVIMDDLGQNPDGEDFKVFCQMVSSTNFLPNMAHLEKKGTPFTSNFIIATTNLPKFRPVTVAHYPAVDRRITFDLTVEAGDECVTHNGMLDVEKAFEEIPGKPQLDCFNTDCRLLHKRGVRFVCNRTKNIYNLQQVVKMVKSTIDNKVENLKKMNTLVAQSPGNDMDYVLTCLRQTNAALQDQIDELQEAFNQAQERQNFLSDWLKVSAIVFASIASLSAVCKLVSRFKNLVCPAPVQIQLSEGEQAAYSGGKKGEKQTLQVLDVQGGGKIVAQAGNPVMDYEVNIAKNMVNPITFFYADKAQVTQSCLLIKGHLFVVNRHVAETDWCAFELKGTRHERDSVQMRSVNKSGMEVDLTFVKVVKGPLFKDNSKKFCSKDDDFPARNETVTGIMNTGVPFVFTGKFLIGNQPVNTTTGACFNHCIHYRATTHRGWCGSALICHVNGKKAVYAMHSAGGGGMAAATIITQEMIEAAEKALDCLTPQGAIVEIGIDTVVHVPRKTKLRRTVAHPCFQPKFEPAVLSRYDPRTTKDVDQVAFSKHTTNLEELPSVFSMVAREYATRVFTTIGKENKILTPEQAILGLPGMDPMEKDTSPGLPYTQQGLKRAQLVNFEQGTMVQNLKEAHTKLTEGNYEDILYQSFLKDEIRPIEKIHEAKTRIVDVPPFHHCIWGRQLLGRFASRFQTNPGLDLGSAIGTDPDTDWTAFAFQLLQYKYVYDVDYSNFDASHSTAMFEVLIENFFTTENGFDERIGDYLRSLAVSRHAFEERRVLVRGGLPSGCAATSMLNTIINNIVIRAALHLTYSNFEFDDIKVLSYGDDLLIATNYQINFNLVKQRLAPFNYKITPANKTVEFPEISNLYEVTFLKRKFVRYNSCLFKPQMDTENLKAMVSYCRPGTLKEKLNSIALLAVHSGKSVYDEIFDPFRRIGIIIPEHGTMLYRWLNLFR | 2.7.7.48; 3.4.22.28; 3.6.4.13 | null | DNA-templated transcription [GO:0006351]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:0039522]; symbiont entry into host cell [GO:0046718]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062] | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleolus [GO:0044196]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule activity [GO:0005198] | PF00548;PF00680;PF00073;PF00910;PF08935; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.90.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Leader protein]: Phosphorylated. {ECO:0000250|UniProtKB:Q66765}.; PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (By similarity). The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip from one codon to the next without formation of a peptide bond (By similarity). This process would release the P1-2A peptide from the translational complex (By similarity). {ECO:0000250|UniProtKB:P03304}.; PTM: [Capsid protein VP0]: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and is followed by a conformational change of the particle. {ECO:0000250|UniProtKB:P03300}.; PTM: [VPg]: Uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase. {ECO:0000250|UniProtKB:P12296}.; PTM: [Capsid protein VP4]: Myristoylation is required during RNA encapsidation and formation of the mature virus particle. {ECO:0000250|UniProtKB:Q66282}. | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000269|PubMed:27279624}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000269|PubMed:27279624}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000269|PubMed:27279624}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Protein 2A]: Host nucleus, host nucleolus {ECO:0000250|UniProtKB:Q66765}.; SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles. {ECO:0000305}.; SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles. {ECO:0000305}.; SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P03304}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles. {ECO:0000250|UniProtKB:P03304}.; SUBCELLULAR LOCATION: [VPg]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles. {ECO:0000305}. | 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}; 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=3.6.4.13; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.; EC=3.4.22.28; Evidence={ECO:0000255|PROSITE-ProRule:PRU01222}; | null | null | null | null | FUNCTION: [Leader protein]: Forms a complex with host RAN and probably binds to exportins carrying activated MAPK in order to mediate the hyperphosphorylation of host Phe/Gly containing nuclear pore proteins (Nups) resulting in cessation of active nucleocytoplasmic transport (Probable). Proteins with NLS signals fail to import, cellular mRNAs fail to export, and some proteins small enough for diffusion are not retained anymore (efflux) (By similarity). The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity). {ECO:0000250|UniProtKB:Q66765, ECO:0000305|PubMed:26115166}.; FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. {ECO:0000269|PubMed:27279624}.; FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. {ECO:0000269|PubMed:27279624}.; FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. {ECO:0000269|PubMed:27279624}.; FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid shell (PubMed:27279624). After binding to the host receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP4 is released, capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm. After genome has been released, the channel shrinks (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000269|PubMed:27279624}.; FUNCTION: [Capsid protein VP0]: VP0 precursor is a component of immature procapsids. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 2A]: Involved in host translation shutoff by inhibiting cap-dependent mRNA translation (By similarity). Nuclear localization is required for this function (By similarity). The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity). Inhibits the phosphorylation of the leader protein (PubMed:25210192). {ECO:0000250|UniProtKB:Q66765, ECO:0000269|PubMed:25210192}.; FUNCTION: [Protein 2B]: Affects membrane integrity and causes an increase in membrane permeability. {ECO:0000250}.; FUNCTION: [Protein 2C]: Associates with and induces structural rearrangements of intracellular membranes (By similarity). It displays RNA-binding, nucleotide binding and NTPase activities (By similarity). {ECO:0000250|UniProtKB:P03305, ECO:0000250|UniProtKB:P08545}.; FUNCTION: [Protein 3A]: Serves as membrane anchor via its hydrophobic domain. {ECO:0000250}.; FUNCTION: [VPg]: Forms a primer, VPg-pU, which is utilized by the polymerase for the initiation of RNA chains. {ECO:0000250|UniProtKB:P03304}.; FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral proteins from the precursor polyprotein (By similarity). In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate cooperatively bind to the protease. Cleaves host PABP1, this cleavage is important for viral replication (By similarity). {ECO:0000250|UniProtKB:P03304, ECO:0000250|UniProtKB:P12296}.; FUNCTION: [RNA-directed RNA polymerase]: Replicates the genomic and antigenomic RNAs by recognizing replications specific signals (By similarity). Performs VPg uridylylation (By similarity). {ECO:0000250|UniProtKB:P12296}. | Saffold virus (SafV) (Human TMEV-like virus-Saffold) |
C0NL63 | ARO1_AJECG | MGVPTKISILGRESIVADFGIWRNYVAKDLLSSCSSSTYILISDTNLTPLYLEGFQRSFEDAATNVSPKPRLLTYEIPPGESSKSRETKADIEDWMLARQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSDEKFAALERDAETILAAVKSKNTPERPRFSGIEETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVSIGMVKEAELARHLGILNNVSVSRISKCLASYGLPTSLKDQRIKKLTAGKHCSVEQLIAYMGVDKKNDGPKKKVVLLSAIGRTHEPRASTVSNEEIQIVLAPSIEVSPGVPKGLDVTCTPPGSKSISNRALVLAALGSGTCRLKNLLHSDDTEVMLNALERLGAATFSWEDEGEVLVVSGKGGRMEASPSELYLGNAGTASRFLTTVATLARKSSVDSSVLTGNARMKQRPIGDLVDALAANGASIEYLENLGCLPLKIASSGGFAGGEINLAAKVSSQYVSSLLMCAPYAKTPVTLRLVGGKPISQPYIDMTTAMMRSFGVEVKKSETEEHTYHIPLGFYTNPVEYIVESDASSATYPLAAAAITGTSCTVPNIGSKSLQGDARFAVDVLRPMGCAVDQSDFSTRVTGPPGGILSPLPNIDMEPMTDAFLTASVLAAVARGKGSNHTTRIFGIANQRVKECNRIKAMKDELAEFGVVCREHDDGLEIDGIDRATLHHPSDGVYCYDDHRVAMSFSVLSLVTPEPTLILEKECVGKTWPGWWDSLAQTFKVKLDGKEVGKRTETNPIVHVNKSAASIFIIGMRGAGKTTSGFWVSKALQRPFIDLDDELERTEGMTIPEIIKQRGWGGFREAELSLLRRVMTEKPTGYIFACGGGVVETPEARKLLTQYHKTTGNVILVMRDIKEIMDFLKIDKTRPAYVEDMMSVWLRRKPWYEECSNVQYYSRLTGLDGMTQVSGGFNRFLKVITGEVDSLAKMRRKENTFFVSLTLPDLSLAAHILKEVTLGSDAVELRVDLLKDPQSDNEIPSVDYVAEQISVLRSRTSVPLVFTIRTKGQGGRFPDDAYDAALQLYRLAVRMGSEFVDLEISFPEQLLRTVTEMKGFSKIITSHHDPKGQLSWVNGSWIQFYNKALQYGDVIKLVGVARSIDDNISLKKFKTWAEEKHNVPIIAINMGDKGQLSRMLNGFMTPVSHPSLPFKAAPGQLSAREIRKGLSLIGEIKAKKFAVIGNPVSASRSPAMHNTLFRQMGLPHTYGTLETDNPEVAKEFIRSPGFGGASVTIPLKISIMPLLDEIAPEAMSIGAVNTIVCAPPAPDGKSQTPRLIGHNTDWQGMVRCLSDAGAYAAATPTTASAGLVIGGGGTARAAIFALQNMGYSPIYVLGRSPDKLSSMTSTFHTDHDIRILEDVKALESLPTVAIGTIPGDKPIEPHMREILCRLFDLCEKANSDTEQARGVSTKRILLEMAYKPSVTSLMQLASDSGWTVLPGLEALVAQGVYQCEYWTNITPVYEYARNAVMGVSPSEDIL | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432) (Darling's disease fungus) (Histoplasma capsulatum) |
C0P9J6 | ADH1A_MAIZE | MASPAMVPLRQLFVDGEWRPPAQGRRLPVVNPTTEAHIGEIPAGTAEDVDAAVAAARAALKRNRGRDWARAPGAVRAKYLRAIAAKVIERKPELAKLEALDCGKPYDEAAWDMDDVAGCFEYFADQAEALDKRQNSPVSLPMETFKCHLRREPIGVVGLITPWNYPLLMATWKIAPALAAGCTAVLKPSELASVTCLELADICKEVGLPSGVLNIVTGLGPDAGAPLSAHPDVDKVAFTGSFETGKKIMASAAPMVKPVTLELGGKSPIVVFDDVDIDKAVEWTLFGCFWTNGQICSATSRLLIHTKIAKKFNERMVAWAKNIKVSDPLEEGCRLGPVVSEGQYEKIKKFISNAKSQGATILTGGVRPAHLEKGFFIEPTIITDITTSMEIWREEVFGPVLCVKEFSTEDEAIELANDTQYGLAGAVISGDRERCQRLSEEIDAGCIWVNCSQPCFCQAPWGGNKRSGFGRELGEGGIDNYLSVKQVTEYISDEPWGWYQSPSKL | 1.2.1.-; 1.2.1.19; 1.2.1.47; 1.2.1.54; 1.2.1.8 | null | cellular detoxification of aldehyde [GO:0110095]; glycine betaine biosynthetic process from choline [GO:0019285] | null | 1-pyrroline dehydrogenase activity [GO:0033737]; 4-trimethylammoniobutyraldehyde dehydrogenase activity [GO:0047105]; aminobutyraldehyde dehydrogenase activity [GO:0019145]; betaine-aldehyde dehydrogenase activity [GO:0008802]; gamma-guanidinobutyraldehyde dehydrogenase activity [GO:0047107]; nucleotide binding [GO:0000166]; protein homodimerization activity [GO:0042803]; sodium ion binding [GO:0031402] | PF00171; | null | Aldehyde dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264, ChEBI:CHEBI:59888; EC=1.2.1.19; Evidence={ECO:0000269|PubMed:23408433}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106; Evidence={ECO:0000269|PubMed:23408433}; CATALYTIC ACTIVITY: Reaction=3-aminopropanal + H2O + NAD(+) = beta-alanine + 2 H(+) + NADH; Xref=Rhea:RHEA:30695, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57966, ChEBI:CHEBI:58374; Evidence={ECO:0000269|PubMed:23408433}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30696; Evidence={ECO:0000269|PubMed:23408433}; CATALYTIC ACTIVITY: Reaction=4-(trimethylamino)butanal + H2O + NAD(+) = 4-(trimethylamino)butanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:17985, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16244, ChEBI:CHEBI:18020, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.47; Evidence={ECO:0000269|PubMed:21740525, ECO:0000269|PubMed:23408433}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17986; Evidence={ECO:0000269|PubMed:23408433}; CATALYTIC ACTIVITY: Reaction=4-guanidinobutanal + H2O + NAD(+) = 4-guanidinobutanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:14381, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57486, ChEBI:CHEBI:57540, ChEBI:CHEBI:57854, ChEBI:CHEBI:57945; EC=1.2.1.54; Evidence={ECO:0000269|PubMed:23408433}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14382; Evidence={ECO:0000269|PubMed:23408433}; CATALYTIC ACTIVITY: Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.8; Evidence={ECO:0000269|PubMed:21740525, ECO:0000269|PubMed:23408433}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306; Evidence={ECO:0000269|PubMed:21740525, ECO:0000269|PubMed:23408433}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=28 uM for 4-aminobutanal {ECO:0000269|PubMed:23408433}; KM=9 uM for 3-aminopropanal {ECO:0000269|PubMed:23408433}; KM=6 uM for 4-(trimethylamino)butanal {ECO:0000269|PubMed:23408433}; KM=3 uM for 4-guanidinobutanal {ECO:0000269|PubMed:23408433}; KM=14 uM for betaine aldehyde {ECO:0000269|PubMed:21740525, ECO:0000269|PubMed:23408433}; KM=91 uM for NAD(+) with 3-aminopropanal as substrate {ECO:0000269|PubMed:23408433}; Vmax=11 nmol/sec/mg enzyme with betaine aldehyde as substrate {ECO:0000269|PubMed:21740525}; | PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. {ECO:0000305}. | null | null | FUNCTION: Dehydrogenase that catalyzes the oxidation of several aminoaldehydes (PubMed:23408433). Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively (PubMed:23408433). Catalyzes the oxidation of 4-(trimethylamino)butanal and 4-guanidinobutanal to 4-trimethylammoniobutanoate and 4-guanidinobutanoate, respectively (PubMed:23408433). Catalyzes the oxidation of betaine aldehyde to glycine betaine (PubMed:23408433). {ECO:0000269|PubMed:23408433, ECO:0000305}.; FUNCTION: Dehydrogenase that catalyzes the oxidation of several aminoaldehydes (PubMed:21740525). Catalyzes the oxidation of betaine aldehyde to glycine betaine (PubMed:21740525). Catalyzes the oxidation of 4-(trimethylamino)butanal to 4-trimethylammoniobutanoate (PubMed:21740525). {ECO:0000269|PubMed:21740525}. | Zea mays (Maize) |
C0QRP9 | GPMPP_PERMH | MVIFTDLDGTLLNHEDYSFKDAIPSLERIKKKGIPLVIVTSKTKKEVELIQKELGIEEPFIVENGAAVFFPKGYRGFNIRCDQENRYCIIKLGRDYREIRDFIEKIKDKFKIKGFGDMTVEEIVRLTDLPYDRAELAKERDFTEPFIIEDEKDIKDLEEIAEKEGFKITKGGRFYHLIGKGQDKGRAVQIVKKVFEENYGEVPLTVGLGDSRNDIPMLREVDIPILIPHINKKYESVNLPGIIKAEYPGSKGWNESIWRILNEIERGCC | 3.1.3.70; 3.1.3.85 | COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:17189358}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17189358}; Note=Divalent metal cations. Can use Mg(2+), Co(2+) and, to a lesser extent, Mn(2+) ions. {ECO:0000269|PubMed:17189358}; | mannosylglycerate biosynthetic process [GO:0051479] | cytosol [GO:0005829] | cobalt ion binding [GO:0050897]; magnesium ion binding [GO:0000287]; mannosyl-3-phosphoglycerate phosphatase activity [GO:0050531]; phosphatase activity [GO:0016791] | PF08282; | 3.40.50.1000; | HAD-like hydrolase superfamily, MPGP family | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-2-O-(alpha-D-glucopyranosyl)-3-phospho-glycerate + H2O = (2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + phosphate; Xref=Rhea:RHEA:31343, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:62510, ChEBI:CHEBI:62600; EC=3.1.3.85; Evidence={ECO:0000269|PubMed:17189358}; CATALYTIC ACTIVITY: Reaction=2-O-(alpha-D-mannosyl)-3-phosphoglycerate + H2O = (2R)-2-O-(alpha-D-mannosyl)-glycerate + phosphate; Xref=Rhea:RHEA:19309, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57541, ChEBI:CHEBI:57744; EC=3.1.3.70; Evidence={ECO:0000269|PubMed:17189358}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.36 mM for GPG (at 70 degrees Celsius) {ECO:0000269|PubMed:17189358}; KM=0.41 mM for GPG (at 85 degrees Celsius) {ECO:0000269|PubMed:17189358}; KM=0.53 mM for GPG (at 90 degrees Celsius) {ECO:0000269|PubMed:17189358}; KM=0.19 mM for MPG (at 85 degrees Celsius) {ECO:0000269|PubMed:17189358}; KM=0.21 mM for MPG (at 90 degrees Celsius) {ECO:0000269|PubMed:17189358}; KM=0.43 mM for MPG (at 70 degrees Celsius) {ECO:0000269|PubMed:17189358}; Vmax=97 umol/min/mg enzyme with GPG as substrate (at 70 degrees Celsius) {ECO:0000269|PubMed:17189358}; Vmax=288 umol/min/mg enzyme with GPG as substrate (at 90 degrees Celsius) {ECO:0000269|PubMed:17189358}; Vmax=294 umol/min/mg enzyme with GPG as substrate (at 85 degrees Celsius) {ECO:0000269|PubMed:17189358}; Vmax=17.9 umol/min/mg enzyme with MPG as substrate (at 90 degrees Celsius) {ECO:0000269|PubMed:17189358}; Vmax=15.75 umol/min/mg enzyme with MPG as substrate (at 70 degrees Celsius) {ECO:0000269|PubMed:17189358}; Vmax=19.6 umol/min/mg enzyme with MPG as substrate (at 85 degrees Celsius) {ECO:0000269|PubMed:17189358}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:17189358}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 85 degrees Celsius. {ECO:0000269|PubMed:17189358}; | FUNCTION: Involved in the biosynthesis of glucosylglycerate. Catalyzes the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) and mannosyl-3-phosphoglycerate (MPG) to glucosylglycerate (GG) and mannosylglycerate (MG), respectively. {ECO:0000269|PubMed:17189358}. | Persephonella marina (strain DSM 14350 / EX-H1) |
C0QRQ2 | GPGS_PERMH | MADFFQNGVITTLQNFRNRSLEELEYELELFSKRRNMVLLLPALYSEFEGPAMPKIIQELKDIRYLYKIVLSLDRATEEEFKKVKKIMSEINTEVKVIWHDGPRMQRLYRELEEAGFNVSIPGKGRSVWMSLGYILSDADAYAIALHDCDIVNYSRELPARLLYPVVHPALDFEFSKGYYARVTHKLYGRVTRIFYTPLIRALIRILGCNRFLVYLDSFRYALSGEFAFIRTLARGIRISPTWGLEVSMLSEVYQNTSFNRICQVEVMDTYEHKHQKLVKSTSEGLVKMASDIAKTLFRVLAHDGFVFSEAFFRTLLTTYLQEARYAIEKYNALSLINGLTYDRHAEIEAIEVFVDALKKAEKEFIEDPIGVPLMSAWVRVRAALPEISDKLIRAVEEDNSDD | 2.4.1.266 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17189358}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:17189358}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17189358}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:17189358}; Note=Requires divalent cations for activity in the following order of efficiency: Mn(2+), Co(2+), Mg(2+) and Ni(2+) ions. {ECO:0000269|PubMed:17189358}; | null | null | glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872] | null | null | Glycosyltransferase 2 family | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + an NDP-alpha-D-glucose = (2R)-2-O-(alpha-D-glucopyranosyl)-3-phospho-glycerate + a ribonucleoside 5'-diphosphate + H(+); Xref=Rhea:RHEA:47244, ChEBI:CHEBI:15378, ChEBI:CHEBI:57930, ChEBI:CHEBI:58272, ChEBI:CHEBI:62600, ChEBI:CHEBI:76533; EC=2.4.1.266; Evidence={ECO:0000269|PubMed:17189358}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.09 mM for 3-PGA (at 70 degrees Celsius) {ECO:0000269|PubMed:17189358}; KM=0.25 mM for 3-PGA (at 85 degrees Celsius) {ECO:0000269|PubMed:17189358}; KM=0.3 mM for 3-PGA (at 90 degrees Celsius) {ECO:0000269|PubMed:17189358}; KM=1.47 mM for UDP-glucose (at 70 degrees Celsius) {ECO:0000269|PubMed:17189358}; KM=1.55 mM for UDP-glucose (at 85 degrees Celsius) {ECO:0000269|PubMed:17189358}; KM=1.58 mM for UDP-glucose (at 90 degrees Celsius) {ECO:0000269|PubMed:17189358}; Vmax=51.5 umol/min/mg enzyme with 3-PGA as substrate (at 70 degrees Celsius) {ECO:0000269|PubMed:17189358}; Vmax=110 umol/min/mg enzyme with 3-PGA as substrate (at 85 degrees Celsius) {ECO:0000269|PubMed:17189358}; Vmax=128 umol/min/mg enzyme with 3-PGA as substrate (at 90 degrees Celsius) {ECO:0000269|PubMed:17189358}; Vmax=66 umol/min/mg enzyme with UDP-glucose as substrate (at 70 degrees Celsius) {ECO:0000269|PubMed:17189358}; Vmax=98 umol/min/mg enzyme with UDP-glucose as substrate (at 85 degrees Celsius) {ECO:0000269|PubMed:17189358}; Vmax=106 umol/min/mg enzyme with UDP-glucose as substrate (at 90 degrees Celsius) {ECO:0000269|PubMed:17189358}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:17189358}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 90 degrees Celsius. GpgS is inactive at 40 degrees Celsius, but the activity increases dramatically above 50 degrees Celsius. At 100 degrees Celsius, GpgS retains 33% of the total activity. {ECO:0000269|PubMed:17189358}; | FUNCTION: Involved in the biosynthesis of 6-O-methylglucose lipopolysaccarides (MGLPs). Catalyzes the transfer of a glucose (Glc) moiety from uridine diphosphate (UDP-Glc) to the position 2 of 3-phospho-D-glycerate (3-PGA) to form glucosyl-3-phosphoglycerate (GPG). GpgS is most active with UDP-glucose, followed by GDP-glucose, ADP-glucose, and to a lesser extent, TDP-glucose. 3-PGA is the only acceptor for these glucosyl donors. {ECO:0000269|PubMed:17189358}. | Persephonella marina (strain DSM 14350 / EX-H1) |
C0S433 | ARO1_PARBP | MGVPTKISILGRESIVADFGIWRNYVAKDLLSNCASSTYILISDTNLTPLYLAGFQQSFENAAAGLSPKPRLLTYEIPPGESSKSRETKAEIEDWMLTRQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALENDADVILAAVKSKNTPDRLRFSSIQETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVSIGMVKEAELARHLGILNNVSVARIAKCLASYELPTSLKDERIKRLTAGKHCSVEQIITYMGVDKKNDGPKKKVVLLSAIGRTYEPRASTVSNEDLQVVLAPSIEVYPGFPKSLNVTCTPPGSKSISNRALVLAALGSGTCRIKNLLHSDDTEVMLTALERLGAATFSWESQGEVLVVNGNGGRMVASPKELYLGNAGTASRFLTTVATLAQKGSVASSVLTGNARMKQRPIGDLVDALKSNGADIEYLENPKSLPLKITASGGFAGGEMRLDAKVSSQYVTSLLMCAPYANEPVTLRLVGGKPVSQLYVDMTTAMMRSFGIDVKKSETEEHTYHIPRGVYKNPAEYVVESDASSATYPLAIAAMTGTSCTVPNIGSKSLQGDARFAIEVLRPMGCTVNQTDFSTSVTGTAGGKLKSLPTIDMEPMTDAFLTASVLAAVARGQGSNHTTRICGIANQRVKECNRIKAMKDELAKFGVTCREHDDGLEIDGIDRSTLRHPTEGVFCYDDHRVAMSFSVLALVAPQPTLILEKECVGKTWPGWWNTLAQTFKVKLDGKEVEVEEVEVEERAKTNGVAHLDKSAASIFIIGMRGAGKTTSGVWVSKALQRPFIDLDDELEKSEGMTIPEMIKQRGWEGFRDSELALLRRVMTEKPMGYIFACGGGVVELPEARELLTQYHKTKGNVILAMRDIKEVMDFLKIDKTRPAYVEDMMSVWLRRKPWYQECSNIQYYSRITQPDGMAQVLHGFNRFLKVITGQLDSLAQMRRKENTFFVSLTFPDLTPASNILKEVTLGSDAVELRVDLLKDPQSDSEIPSVDYVAEQISVLRSRVSVPLVFTIRTKSQGGRFPDDAYDAALQLYRLAIRMGSEFVDLELSFPKQLLRTVTEMKGFSKIIASHHDPEGLLSWANGSWIQIYNKALQYGDVIKLVGVAKTLDDNASLKKFKTWAEAKHDVPLIAINMGYKGQLSRILNGFMTPVSHPSLPFKAAPGQLSAREIRKGLSLMGEIKAKKFAVIGKPVSSSRSPAMHNALFKQMGLPHTYGRIETDNVEDVKEFILSPDFGGASVTIPLKLDIMPLLDEIAPEAEMIGAVNTIVSVPAAPGDKFQSSRLIGRNTDWQGMVRCLSDAGAYSAATPTTSSAGLIIGGGGTARAAIFALNSMSYSPIYIVGRSPEKLACMASSFPADYNIRIVDDVKALESLPMVAIGTIPGDKPIELHMREVLCEILSLCEKANVEAERKTGITPKRILLEMAYKPSVTSLMKLASDAGWTVLPGLEVLVAQGVYQSEYWTDITPVYENARKAVMGVSSSDDTIS | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Paracoccidioides brasiliensis (strain Pb03) |
C0SP85 | YUKE_BACSU | MAGLIRVTPEELRAMAKQYGVESQEVLNQVDRLNRMISDLKSMWEGASSEAFADQYEQLKPSFIKMSDLLQDVNQQLDQTANTLESTDQDIANQIRG | null | null | null | extracellular region [GO:0005576] | null | PF06013; | 1.10.287.1060; | WXG100 family, sagEsxA-like subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23861817, ECO:0000269|PubMed:24798022, ECO:0000269|PubMed:24828531}. Note=Secreted via the ESX/ESAT-6-like secretion system (BsEss) / type VII secretion system (T7SS) (PubMed:23861817, PubMed:24798022). Can be secreted as a dimer (PubMed:24828531). {ECO:0000269|PubMed:23861817, ECO:0000269|PubMed:24798022, ECO:0000269|PubMed:24828531}. | null | null | null | null | null | FUNCTION: Required to deliver LXG toxins to target cells. {ECO:0000269|PubMed:34280190}. | Bacillus subtilis (strain 168) |
C0SPC1 | CCRZ_BACSU | MNIDMNWLGQLLGSDWEIFPAGGATGDAYYAKHNGQQLFLKRNSSPFLAVLSAEGIVPKLVWTKRMENGDVITAQHWMTGRELKPKDMSGRPVAELLRKIHTSKALLDMLKRLGKEPLNPGALLSQLKQAVFAVQQSSPLIQEGIKYLEEHLHEVHFGEKVVCHCDVNHNNWLLSEDNQLYLIDWDGAMIADPAMDLGPLLYHYVEKPAWESWLSMYGIELTESLRLRMAWYVLSETITFIAWHKAKGNDKEFHDAMEELHILMKRIVD | 2.7.1.15; 2.7.1.229 | null | cell cycle [GO:0007049]; cell division [GO:0051301]; DNA damage response [GO:0006974]; DNA replication initiation [GO:0006270] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; carbohydrate kinase activity [GO:0019200]; phosphotransferase activity, alcohol group as acceptor [GO:0016773]; ribokinase activity [GO:0004747] | PF01636; | 3.90.1200.10; | Aminoglycoside phosphotransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A0H2ZQL5}. | CATALYTIC ACTIVITY: Reaction=ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+); Xref=Rhea:RHEA:13697, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:47013, ChEBI:CHEBI:78346, ChEBI:CHEBI:456216; EC=2.7.1.15; Evidence={ECO:0000269|PubMed:35576203}; CATALYTIC ACTIVITY: Reaction=2-deoxy-D-ribose + ATP = 2-deoxy-D-ribose 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:30871, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:62877, ChEBI:CHEBI:90761, ChEBI:CHEBI:456216; EC=2.7.1.229; Evidence={ECO:0000269|PubMed:35576203}; | null | null | null | null | FUNCTION: Plays a role in cell cycle regulation and chromosome integrity. Activates DnaA-dependent chromosomal DNA replication initiation ensuring that the chromosome is replicated at the right time during the cell cycle (By similarity). May regulate replication initiation through phosphorylation of a possible second messenger or metabolite, and by interacting with replication initiation proteins. Has ATPase activity with D-ribose and 2-deoxy-D-ribose in vitro, but not with choline. Involved in DNA damage response (PubMed:35576203). {ECO:0000250|UniProtKB:A0A0H2ZQL5, ECO:0000269|PubMed:35576203}. | Bacillus subtilis (strain 168) |
C0SPF7 | C15C1_BOMMO | MLALIVLCFILFFYIISRRHRGLCYPPGPTPLPIVGNLLSVLWESRKFKCHHLIWQSWSQKYGNLLGLRLGSINVVVVTGIELIREVSNREVFEGRPDGFFYTMRSFGKKLGLVFSDGPTWHRTRRFVLKYLKNFGYNSRFMNVYIGDECEALVQLRLADAGEPILVNQMFHITIVNILWRLVAGKRYDLEDQRLKELCSLVMRLFKLVDMSGGFLNFLPFLRHFVPRLIGFTELQEIHNALHQYLREIIKEHQENLQLGAPKDVIDAFLIDMLESQDDKPTLDDLQVVCLDLLEAGMETVTNTAVFMLLHVVRNEDVQRKLHQEIDDIIGRDRNPLLDDRIRMVYTEAVILETLRISTVASMGIPHMALNDAKLGNYIIPKGTFILLSLYELHHGPHWKDPETFRPERFLTKEGNILQDEWLIPFGIGKRRCIGEGLARSELFMFLTHILQKFHLRIPKNEPLPSTEPIDGLSLSAKQFRIIFEPRKTFKSI | 1.14.14.128 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | juvenile hormone biosynthetic process [GO:0006718]; metamorphosis [GO:0007552]; organic acid metabolic process [GO:0006082]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen [GO:0016709]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesoate + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + juvenile hormone III carboxylate + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:43724, 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:83274, ChEBI:CHEBI:83276; EC=1.14.14.128; Evidence={ECO:0000269|PubMed:22412378}; | null | null | null | null | FUNCTION: Catalyzes the conversion of farnesoate to juvenile hormone III acid in juvenile hormone biosynthesis. {ECO:0000269|PubMed:22412378}. | Bombyx mori (Silk moth) |
C0SUT9 | JMJ16_ARATH | MGTELMRICVKEDSDDLPSVPPGFESYATFTLKRVVPATTSDKAKTPAIESVSATEQAKMEVESDEAKAARALRRRPWINHSGCDDDGDCAANNDNAASQNPDQNCDVKPALPKGVVRGCEECKDCQKVTARWHPDEARRPDLEDAPVFYPSEEEFEDTLNYIAKIRPEAEKYGICRIVPPPSWKPPCPLKEKQVWEGSKFTTRVQRVDKLQNRSSMKKISKLPNQMRKKKRKCMKMGMDSVTNGMGDPCSASTGMNELETFGFEPGPGFTLKDFQKYADEFKAQYFKKSETSTDDKCKVDNSIDCWEPALEDVEGEYWRIVDKATEEIEVLYGADLETGVFGSGFPKISSSHNASSSEDKYAKSGWNLNNFPRLPGSLLKYEGSDISGVLVPWLYIGMCFSSFCWHVEDHHLYSLNYMHWGAPKLWYGVGGKDAVKLEEAMRKHLPDLFEEQPDLLHKLVTQLSPSKLKTAGVPVHRCVQHAGEFVLTFPRAYHAGFNSGFNCAEAVNVAPVDWLPHGQIAIELYCQQGRKTSISHDKLLLGAAREVVKADWELNLLRKNTVDNLRWKAFSAKDGILAKTLKARIDMERTRREFLCNSSLALKMHSNFDATNERECCICFFDLHLSAAGCRCSPEKYSCLTHVKELCSCPWVTKYFLFRYDIDELNVLVEAVEGKLSSVYRWARQDLGLALSTDVSGSKMEIDEEGKVHKDPTPQTTALSGKDLQLKVTSKEVSKELEKTSKLSHVNLLLKEKEEQITSSHCMKPVKEETVCDSSDPNVSACQPSEGGIICMTAVKSASGKKNSQSLPNDVILLSDDEYDIPRKRGSVRRDAISSGKKLEIRERPTHVLALEASAKIAAPICQREGDSLRDTRNTISLPTNDQKTMRRDVPSSTSHAEVNAEATGLTQDICNRMATNSHGGGKPTSCKSKNSGGLAIVDVVDGTRSSSGTPSCSQNNSPDRFIRQKGPRIAKVVRRINCNVEPLSYGCVLSGKSWCSRRAIFPKGFRSRVKYINILDPTNMCFYISEILDAGRNSPLFMVYLESNPSEVFVHMSPTRCWEMVRERVNQEITKQHKAGKSDLPPLQPSGSPDGFEMFGYSSPAIVQAIEALDVNRVCTDYWDSRPYSRPQVQFPANPLLREANTSGRSNVGNLQLNPGHHISPTGINSILKVLFKKASMEELSSLQEVLSETNSDMVTELVKEEIQNRR | 1.14.11.- | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q8GUI6}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8GUI6}; | chromatin remodeling [GO:0006338]; developmental growth [GO:0048589]; meiotic chromosome condensation [GO:0010032]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of leaf senescence [GO:1900056]; plant organ development [GO:0099402]; positive regulation of chromosome condensation [GO:1905821]; positive regulation of gene expression [GO:0010628]; reactive oxygen species biosynthetic process [GO:1903409]; regulation of DNA-templated transcription [GO:0006355] | chromatin [GO:0000785]; nucleus [GO:0005634] | histone H3K4me/H3K4me2/H3K4me3 demethylase activity [GO:0034647]; histone H3K9 demethylase activity [GO:0032454]; metal ion binding [GO:0046872]; SUMO binding [GO:0032183] | PF05965;PF05964;PF02373;PF02375;PF02928; | 3.30.160.360;2.60.120.650; | JARID1 histone demethylase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:32572214}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + O2 = CO2 + formaldehyde + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + succinate; Xref=Rhea:RHEA:60212, Rhea:RHEA-COMP:15537, Rhea:RHEA-COMP:15540, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61961, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:30712008, ECO:0000269|PubMed:32572214}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60213; Evidence={ECO:0000269|PubMed:30712008, ECO:0000269|PubMed:32572214}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + O2 = CO2 + formaldehyde + N(6)-methyl-L-lysyl(4)-[histone H3] + succinate; Xref=Rhea:RHEA:60216, Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15543, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:30712008, ECO:0000269|PubMed:32572214}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60217; Evidence={ECO:0000269|PubMed:30712008, ECO:0000269|PubMed:32572214}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(6)-methyl-L-lysyl(4)-[histone H3] + O2 = CO2 + formaldehyde + L-lysyl(4)-[histone H3] + succinate; Xref=Rhea:RHEA:60220, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929; Evidence={ECO:0000269|PubMed:30712008, ECO:0000269|PubMed:32572214}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60221; Evidence={ECO:0000269|PubMed:30712008, ECO:0000269|PubMed:32572214}; | null | null | null | null | FUNCTION: Functions as a histone H3 'Lys-4' (H3K4me) demethylase involved in the negative regulation of gene expression (PubMed:30712008, PubMed:32572214). Active on H3K4me1, H3K4me2 and H3K4me3 (PubMed:30712008, PubMed:32572214). Not active on mono-, di- and trimethylated H3K9, H3K27 and H3K36 in somatic cells (PubMed:30712008, PubMed:32572214). However, also active on H3K9 when in complex with MMD1, a meiocyte-specific histone reader (PubMed:32572214). Together with MMD1, promotes gene expression in male meiocytes in an H3K9me3-dependent manner, and contributes to meiotic chromosome condensation by triggering some condensin promoters (e.g. CAP-D3 and CAP-H) (PubMed:32572214). Together with JMJ14 and JMJ17, required for plant growth and development (PubMed:31038749). Represses leaf senescence in an age-dependent manner by demethylating H3K4me3 activating histone marks at senescence-associated genes (SAGs) loci, including WRKY53 and SAG201, thus preventing their premature expression (PubMed:30712008). {ECO:0000269|PubMed:30712008, ECO:0000269|PubMed:31038749, ECO:0000269|PubMed:32572214}. | Arabidopsis thaliana (Mouse-ear cress) |
C0VHC9 | CAP4_ACIS2 | MSASLLEKQSTGGAIARVGFGYQDAFVLRSLPLWLSQSAFSHIVSEALSDIEVCYFSSEKSLHVMYEAKNHSLTATEFWDEIRRFKSLFDTHPKNFIWFNLVCPSYNTAISPLISKIDRLRGVGSSYDDDSSVSVNGRSEYLDWCVGKKIDFSLAEFALDYVGFITFNSENSESIFLSEIQDTINIELLRSQVKQLKDQFKNLISRSSFGPIYRKDFENFICHALEEDRSQWLLDPIKINLSASSSQYQDLNLDISDFNGPDRAQKTSSDWNSLIKKAVSIGDFIHNSGDRRTLLIDGKQRMSTACMLGYVFSATRNFLLEIEHNGLIYRTDDHKQKEGQFFTKIEAVEPQGETEAIVAIGFPTAIGKDIDSTINEVKSLPRLNLESSHAIDNMETLNLAVREAKSALVSFKSENKLSKLHLFIKAPSVFAMVLGHRLNGICDIQLYDWVDGQYIPTAELNL | 3.1.-.- | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:32544385}; | defense response to virus [GO:0051607] | null | DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166] | PF14130;PF18145; | null | Cap4 nuclease family | null | null | null | null | null | null | null | FUNCTION: Effector DNase of a CBASS antivirus system (PubMed:32544385). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-C(AAAA) CBASS system (PubMed:32839535). {ECO:0000269|PubMed:32544385, ECO:0000303|PubMed:32839535, ECO:0000305|PubMed:32544385}.; FUNCTION: Binds cyclic nucleotide second messengers (synthesized by CdnD, the cognate CD-NTase in the CBASS operon). Ligand binding activates it to endonucleolytically degrade dsDNA to approximately 6 bp length fragments, with a preference for 5'-C or 5'-G cleavage site. The minor product of CdnD is the activating nucleotide; also binds the major product (2',3',3'-cyclic AMP-AMP-AMP) but is not activated by it. Only binds DNA in the presence of ligand. Is not activated by c-di-AMP, c-di-GMP, 3'3'-cyclic GMP-AMP (3'3'-cGAMP) or 3',3',3'-cyclic AMP-AMP-GMP. {ECO:0000269|PubMed:32544385}. | Acinetobacter sp. (strain ATCC 27244 / 9458) |
C0Z2L5 | BZP44_ARATH | MNNKTEMGSSTSGNCSSVSTTGLANSGSESDLRQRDLIDERKRKRKQSNRESARRSRMRKQKHLDDLTAQVTHLRKENAQIVAGIAVTTQHYVTIEAENDILRAQVLELNHRLQSLNEIVDFVESSSSGFGMETGQGLFDGGLFDGVMNPMNLGFYNQPIMASASTAGDVFNC | null | null | positive regulation of DNA-templated transcription [GO:0045893]; seed germination [GO:0009845] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; protein heterodimerization activity [GO:0046982]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976] | PF00170; | 1.20.5.170; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. | null | null | null | null | null | FUNCTION: Transcription factor that binds to the DNA G-box motif 5'-CACGTG-3' of MAN7 promoter. Involved in the positive regulation of seed germination through MAN7 gene activation. MAN7 is required for both, loosening of the micropylar endosperm, and rupture of the seed coat in germinating seeds. {ECO:0000269|PubMed:23461773}. | Arabidopsis thaliana (Mouse-ear cress) |
C1ANR3 | LYSX_MYCBT | MGLHLTVPGLRRDGRGVQSNSHDTSSKTTADISRCPQHTDAGLQRAATPGISRLLGISSRSVTLTKPRSATRGNSRYHWVPAAAGWTVGVIATLSLLASVSPLIRWIIKVPREFINDYLFNFPDTNFAWSFVLALLAAALTARKRIAWLVLLANMVLAAVVNAAEIAAGGNTAAESFGENLGFAVHVVAIVVLVLGYREFWAKVRRGALFRAAAVWLAGAVVGIVASWGLVELFPGSLAPDERLGYAANRVVGFALADPDLFTGRPHVFLNAIFGLFGAFALIGAAIVLFLSQRADNALTGEDESAIRGLLDLYGKDDSLGYFATRRDKSVVFASSGRACITYRVEVGVCLASGDPVGDHRAWPQAVDAWLRLCQTYGWAPGVMGASSQGAQTYREAGLTALELGDEAILRPADFKLSGPEMRGVRQAVTRARRAGLTVRIRRHRDIAEDEMAQTITRADSWRDTETERGFSMALGRLGDPADSDCLLVEAIDPHNQVLAMLSLVPWGTTGVSLDLMRRSPQSPNGTIELMVSELALHAESLGITRISLNFAVFRAAFEQGAQLGAGPVARLWRGLLVFFSRWWQLETLYRSNMKYQPEWVPRYACYEDARVIPRVGVASVIAEGFLVLPFSRRNRVHTGHHPAVPERLAATGLLHHDGSAPDVSGLRQVGLTNGDGVERRLPEQVRVRFDKLEKLRSSGIDAFPVGRPPSHTVAQALAADHQASVSVSGRIMRIRNYGGVLFAQLRDWSGEMQVLLDNSRLDQGCAAEFNAATDLGDLVEMTGHMGASKTGTPSLIVSGWRLIGKCLRPLPNKWKGLLDPEARVRTRYLDLAVNAESRALITARSSVLRAVRETLFAKGFVEVETPILQQLHGGATARPFVTHINTYSMDLFLRIAPELYLKRLCVGGVERVFELGRAFRNEGVDFSHNPEFTLLEAYQAHAGYLEWIDGCRELIQNAAQAANGAPIAMRPRTDKGSDGTRHHLEPVDISGIWPVRTVHDAISEALGERIDADTGLTTLRKLCDAAGVPYRTQWDAGAVVLELYEHLVECRTEQPTFYIDFPTSVSPLTRPHRSKRGVAERWDLVAWGIELGTAYSELTDPVEQRRRLQEQSLLAAGGDPEAMELDEDFLQAMEYAMPPTGGLGMGIDRVVMLITGRSIRETLPFPLAKPH | 2.3.2.3; 6.1.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250}; | diadenosine tetraphosphate biosynthetic process [GO:0015966]; lipid metabolic process [GO:0006629]; lysyl-tRNA aminoacylation [GO:0006430]; positive regulation of macrophage activation [GO:0043032]; response to antibiotic [GO:0046677] | aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytosol [GO:0005829]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | ATP adenylyltransferase activity [GO:0003877]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; lysine-tRNA ligase activity [GO:0004824]; magnesium ion binding [GO:0000287]; phosphatidylglycerol lysyltransferase activity [GO:0050071]; tRNA binding [GO:0000049] | PF09924;PF00152;PF16995;PF01336; | 2.40.50.140; | LPG synthetase family; Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6; CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys); Xref=Rhea:RHEA:10668, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:64716, ChEBI:CHEBI:75792, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529; EC=2.3.2.3; | null | null | null | null | FUNCTION: Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects M.tuberculosis against the CAMPs produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine results in repulsion of the peptides (By similarity). {ECO:0000250}. | Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019) |
C1B7Z5 | LYSX_RHOOB | MSASTETHHASEAAVPTAPRPRPALGSKSGRLHQVPHIAGLILGVFSVLVFLWSISPVLRYYVHVPREYIDTYYFDAPDTSLSWALVVALLAAALASRKRIAWWLLTIYLVLILITNVIVSITDRNVNAMVAAVVQVVLIGILVAARPEFYTRVRRGAGWKALGVLIVGLAIGTLVGWGLVELFPGTLPQGERFLWALNRVTALAAADNEQFSGRPHGFVNTLLGLFGAMALLAAVITLFRAQRSHNALTGNDESALRGLLLQYGADDSLGYFATRRDKAVVFAPSGKAAITYRVELGVCLASGDPIGDPEAWPHAIEAWQTLASQYGWATAVMGASETGATAYNKAGLTVLQLGDEAILRTREFNLSGRDMRQVRQAVTRVRRQGVTVRIRRHRDVPPEEMAEAIRLADAWRDTETERGFSMALGRLGDRLDGDCLLVEAIAEDGEIDGILSLVPWGPTGVSLDLMRRKPTSPNGVVELMVSELATTSDQFGITKVSLNFAVFRSVFEEGSRIGAGPILRIWRSILVFFSRWWQLEALYRSNVKYQPEWVPRFLCFDDNRELLRVGFASAVAEGFVTLPRFGRSGTHDAIEHTGHHAAVPAALVAAEGLHSDGSAPGEGLAPTATGPKRPEQVRVRLDKLTGLAEQGIDPYPVAYPPSHTVTEAVESPEGTTVRIAGRLLRIRDYGGVVFAVVRDWSGDIQVLVDEARVGTDRIRAFAAEFDLGDLVEVAGVIGYSRRGALSLLANEWRMTGKCLHPLPDKWKGLSDPETRVRQRYVDLAINTDARRLLEARSAVVKSLRDSLGGRGFLEVETPILQQVHGGANAAPFLTHINAYNLDLYLRIAPELYLKRLCVAGMEKVFEIGRVFRNEGVDFKHNPEFTILEAYEAHSDYEKMMVLCRELIQTAAVAAYGREIIMRPGPDGTLVEVDISGEWPVKTMHQAVAEKLGVDVSPETPLAELQRLCDEHEIPYQSTWDAGAVAQEMYEHLVEDYTEFPTFYTNFPTSMSPLTRPHPTIPGVAAKWDLVAWGVELGTAYSELTDPVDQRNRLTEQSMLAAGGDEEAMELDEDFLQALEHAMPPTGGLGMGVDRVVMLITGGSIRETLAFPLAKPRQ | 2.3.2.3; 6.1.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250}; | diadenosine tetraphosphate biosynthetic process [GO:0015966]; lipid metabolic process [GO:0006629]; lysyl-tRNA aminoacylation [GO:0006430]; positive regulation of macrophage activation [GO:0043032]; response to antibiotic [GO:0046677] | aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytosol [GO:0005829]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | ATP adenylyltransferase activity [GO:0003877]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; lysine-tRNA ligase activity [GO:0004824]; magnesium ion binding [GO:0000287]; phosphatidylglycerol lysyltransferase activity [GO:0050071]; tRNA binding [GO:0000049] | PF09924;PF00152;PF16995;PF01336; | 2.40.50.140; | LPG synthetase family; Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6; CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys); Xref=Rhea:RHEA:10668, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:64716, ChEBI:CHEBI:75792, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529; EC=2.3.2.3; | null | null | null | null | FUNCTION: Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects M.tuberculosis against the CAMPs produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine results in repulsion of the peptides (By similarity). {ECO:0000250}. | Rhodococcus opacus (strain B4) |
C1CZ84 | IRRE_DEIDV | MTDPAPPPTALAAAKARMRELAASYGAGLPGRDTHSLMHGLDGITLTFMPMGQRDGAYDPEHHVILINSQVRPERQRFTLAHEISHALLLGDDDLLSDLHDEYEGDRLEQVIETLCNVGAAALLMPAELIDDLLTRFGPTGRALAELARRADVSATSALYALAERTAPPVIYAVCALSRQEDEGEGGGAKELTVRASSASAGVKYSLSAGTPVPDDHPAALALDTRLPLAQDSYVPFRSGRRMPAYVDAFPERQRVLVSFALPAGRSEPDADKPEAPGDQS | 3.4.24.- | null | proteolysis [GO:0006508] | null | metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237] | PF06114; | 1.10.10.2910;3.30.450.130;1.10.10.1030; | null | null | null | null | null | null | null | null | FUNCTION: Plays a central regulatory role in DNA repair and protection pathways in response to radiation stress. Acts as a site-specific metalloprotease that cleaves and inactivates the repressor proteins DdrOC and DdrOP3, resulting in induced expression of genes required for DNA repair and cell survival after exposure to radiation. {ECO:0000269|PubMed:25170972}. | Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115) |
C1FYJ9 | ARO1_PARBD | MGVPTKISILGRESIVADFGIWRNYVAKDLLSNCASSTYILISDTNLTPLYLAGFQQSFENAAAGLSPKPRLLTYEIPPGESSKSRETKAEIEDWMLARQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALENDADVILAAVKSKNTPDRLRFSSIQETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVSIGMVKEAELARHLGILNNVSVARIAKCLASYELPTSLKDERIKRLTAGKHCSVEQIITYMGVDKKNDGPKKKVVLLSAIGRTYEPRASTVSNEDLQVVLAPSIEVYPGFPKSLNVTCTPPGSKSISNRALVLAALGSGTCRIKNLLHSDDTEVMLTALERLGAATFSWESQGEVLVVNGNGGRMVASPKELYLGNAGTASRFLTTVATLAQKGSVASSVLTGNARMKQRPIGDLVDALKANGADIEYLENPKSLPLKITASGGFAGGEMRLDAKVSSQYVSSLLMCAPYAKEPVTLRLVGGKPVSQLYVDMTTAMMRSFGIDVKKSETEEHTYHIPRGVYKNPAEYVVESDASSATYPLAIAAMTGTSCTIPNIGSKSLQGDARFAIEVLRPMGCTVNQTDFSTSVTGTAGGKLKSLPTIDMEPMTDAFLTASVLAAVARGQGSNHTTRICGIANQRVKECNRIKAMKDELAKFGVTCREHDDGLEIDGIDRSTLRHPTEGVFCYDDHRVAMSFSVLALVAPQPTLILEKECVGKTWPGWWNTLAQTFKVKLDGKEVEVEERAETNGVAHLDKSAASIFIIGMRGAGKTTSGVWVSKALQRPFIDLDDELEKSEGMTIPEMIKQRGWEGFRDSELALLRRVMTEKPMGYIFACGGGVVELPEARELLTQYHKTKGNVILAMRDIKEVMDFLKIDKTRPAYVEDMMSVWLRRKPWYQECSNIQYYSRITQPDGMAQVLHGFNRFLKVITGQLDSLAQMRRKENTFFVSLTFPDLTPASNILKEVTLGSDAVELRVDLLKDPQSDSEIPSVDYVAEQISVLRSRVSVPLVFTIRTKSQGGRFPDDAYDAALQLYRLAIRMGSEFVDLELSFPEQLLRTVTEMKGFSKIIASHHDPEGLLSWANGSWIQIYNKALQYGDVIKLVGVAKTLDDNASLKKFKTWAEAKHDVPLIAINMGYKGQLSRILNGFMTPVSHPSLPFKAAPGQLSAREIRKGLSLMGEIKAKKFAVIGKPVSSSRSPAMHNALFKQMGLPHTYGRIETDNVEDVKEFILSPDFGGASVTIPLKLDIMPLLDEIAPEAEMIGAVNTIVSVPAAPGDKSQSSRLIGRNTDWQGMVRCLSDAGAYSAATPTTSSAGLIIGGGGTARAAIFALNSMSYSPIYIVGRSPEKLACMASSFPADYNIRIVDDVKALESLPMVAIGTIPGDKPIELHMREVLCEILSLCEKANVEAERKTGITPKRILLEMAYKPSVTSLMKLASDAGWTVLPGLEVLVAQGVYQSEYWTDITPVYENARKAVMGVSSSDDTIS | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Paracoccidioides brasiliensis (strain Pb18) |
C1H8L1 | ARO1_PARBA | MGVPTKISILGRESIVADFGIWRNYVAKDLLSSCASSTYILISDTNLTPLYLAGFQQSFENAAAGLSPKPRLLTYEIPPGESSKSRETKADIEDWMLTRQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALENDADVILAAVKSKNTPERLRFSNIQETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVSIGMVKEAELARHLGILNNVSVARIVKCLASYELPTSLKDERIKRLTAGKHCSVEQIIAYMGVDKKNDGPKKKVVLLSAIGRTYEPRACTVSNEDLQVVLAPSIEVYPGFPKSLNVTCTPPGSKSISNRALVLAALGSGTCRIKNLLHSDDTEVMLTALERLGAATFSWENQGEVLVVNGNGGRMVASPKELYLGNAGTASRFLTTVATLAQNGSVASSVLTGNARMKQRPIGDLVDALKANGADIEYLENPKSLPLKITASGGFAGGEIRLSAKVSSQYVSSLLMCAPYAKEPVTLRLVGGNPVSQLYIDMTTAMMRSFGIDVKKSETEEHTYHIPRGVYKNPAEYVVESDASSATYPLAIAAMTGTSCTVPNIGSKSLQGDARFAIDVLRPMGCTVNQTDFSTSVTGPAGGKLKSIPTIDMEPMTDAFLTASVLAAVARGQGSNHTTRICGIANQRVKECNRIKAMKDELAKFGVTCREHDDGLEIDGIDRSTLCHPPEGVFCYDDHRVAMSFSILALAAEQPTLILEKECVGKTWPGWWDTLAQTFKVKLDGKEVEVEEKAETNGVAHVDKSAASIFIIGMRGAGKTTSGVWVSKALQRPFIDLDDELEKNEGMTIPEMIKQRGWEGFRDSELALLRRVMTEKPMGYIFACGGGVVELPEARELLTQYHKTKGNVILAMRDIKEVMDFLKIDKTRPAYVEDMMSVWLRRKPWYQECSNIQYYSRITQPDGMAQVLHGFNRFLKVITGKLDSLAQMRRKENTFFVSLTFPDLTPASNILKEVTLGSDAVELRVDLLKDPQSDSEIPSVDYVAEQISVLRSRVSVPLVFTIRTKSQGGRFPDDAYDAALRLYCLAIRMGSEFVDLELSFPEQLLRTVTEMKGFSKIIASHHDPEGLLSWANGSWIQIYNKALQYGDVIKLVGVAKTLDDNASLKKFKTWAEAKHDVPLIAINMGYKGQLSRILNGFMTPVSHPGLPFKAAPGQLSAREIRKGLSLMGEIKAKKFAVIGKPVSSSRSPAMHNALFKQMGLPHTYGRIETDNPEDVKEFIRSPDFGGASVTIPLKLDIMPLLDEIAPEAEMIGAVNTIVSVPAAPGDKSQSSRLIGRNTDWQGMVRCLSDAGAYSAATPTTSSAGLIIGGGGTARAAIFALNSMSYSPIYIVGRSPEKLACMASSFPADYNIRIVDDVKALESLPMVAIGTIPGDKPIELHMREVLCEILSLCEKANVEAERRTGITPKRILLEMAYKPSVTSLMKLASDAGWTVLPGLEVLVAQGVYQSEYWTDITPVYENARKAVMGVSSSDDIIS | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides brasiliensis) |
C1I202 | PNPB_PSEWB | MPTKIQIVFYSSYGHIYKMAEAIAAGAREVGDVEVTLLQVPELMPEEVQVKSGIKGYRAAFGSIPYATPEVLAEADAIIFGTPTRFGNMCSQMRNFLDQTGGLWMSGGLIGKVGSVFTSTASQHGGQETTITSFHTTLLHHGMVIVGVPYSEPGLTNMTEISGGTPYGASTLAGADGSRQPSENELQIARFQGKHVATIAKRLANNK | 1.6.5.6 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:19218392}; Note=Binds 1 FMN per monomer. {ECO:0000269|PubMed:19218392}; | 4-nitrophenol catabolic process [GO:0046196]; aromatic compound catabolic process [GO:0019439] | membrane [GO:0016020] | flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; NAD binding [GO:0051287]; NAD(P)H dehydrogenase (quinone) activity [GO:0003955]; NADP binding [GO:0050661]; p-benzoquinone reductase (NADPH) activity [GO:0018541] | PF03358; | 3.40.50.360; | WrbA family | null | null | CATALYTIC ACTIVITY: Reaction=1,4-benzoquinone + H(+) + NADPH = hydroquinone + NADP(+); Xref=Rhea:RHEA:23488, ChEBI:CHEBI:15378, ChEBI:CHEBI:16509, ChEBI:CHEBI:17594, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.5.6; Evidence={ECO:0000269|PubMed:19218392}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.7 uM for p-benzoquinone {ECO:0000269|PubMed:19218392}; KM=181.6 uM for NADPH {ECO:0000269|PubMed:19218392}; | PATHWAY: Xenobiotic degradation; 4-nitrophenol degradation. | null | null | FUNCTION: Involved in the degradation of para-nitrophenol (PNP). Catalyzes the reduction of p-benzoquinone to hydroquinone. {ECO:0000269|PubMed:19218392}. | Pseudomonas sp. (strain WBC-3) |
C1ITJ8 | HMR1_BOVIN | MMLLLPLIIVLMMKLSDARTHSLRYFRLGISEPGYGIPEFISAGYVDSHPITMYNSVSQLKEPRALWMEENLAPDHWERYTQLLRGWQQAFKVELKQLQHHYNHSGFHTYQRMIGCELLEDGSITGFLQYAYDGQDFLIFNKDTLSWMAMDNVADIIRRVWEANRHELQYQKNWLEEECIAWLKRFLEYGKDALQRTEPPKVRVNHKETFPGITTLYCRAYGFYPPEISINWMKNGEEIFQDTDYGGILPSGDGTYQTWVSVELDPQNGDIYSCHVEHGGVHMVLQGFQESETILLVVKAVGFIVLAIALAGVGILAWRKRPRGKNKVICLSTPEH | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; immune response [GO:0006955]; innate immune response [GO:0045087]; positive regulation of T cell mediated cytotoxicity directed against tumor cell target [GO:0002854]; T cell differentiation in thymus [GO:0033077] | early endosome membrane [GO:0031901]; endoplasmic reticulum membrane [GO:0005789]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; MHC class I protein complex [GO:0042612]; plasma membrane [GO:0005886] | beta-2-microglobulin binding [GO:0030881]; T cell receptor binding [GO:0042608] | PF07654;PF00129; | 2.60.40.10;3.30.500.10; | MHC class I family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q95460}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19416870}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q95460}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q95460}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q95460}; Single-pass type I membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q95460}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:Q95460}; Single-pass type I membrane protein {ECO:0000255}. Note=In the absence of antigen remains within the endoplasmic reticulum where it acts as a metabolite sensor. Antigen binding triggers trafficking of the ternary complex to the plasma membrane. After presentation, most of these complexes are rapidly internalized and degraded via endocytosis. A small subset recycles via endosomes back to the plasma membrane and may thus acquire and present new antigens that do not efficiently reach the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q95460}. | null | null | null | null | null | FUNCTION: Antigen-presenting molecule specialized in displaying microbial pyrimidine-based metabolites to alpha-beta T cell receptors (TCR) on innate-type mucosal-associated invariant T (MAIT) cells. In complex with B2M preferentially presents riboflavin-derived metabolites to semi-invariant TCRs on MAIT cells, guiding immune surveillance of the microbial metabolome at mucosal epithelial barriers (By similarity). Signature pyrimidine-based microbial antigens are generated via non-enzymatic condensation of metabolite intermediates of the riboflavin pathway with by-products arising from other metabolic pathways such as glycolysis. Typical potent antigenic metabolites are 5-(2-oxoethylideneamino)-6-D-ribitylaminouracil (5-OE-RU) and 5-(2-oxopropylideneamino)-6-D-ribitylaminouracil (5-OP-RU), products of condensation of 5-amino-6-D-ribityaminouracil (5-A-RU) with glyoxal or methylglyoxal by-products, respectively (By similarity). May present microbial antigens to various MAIT cell subsets, providing for unique recognition of diverse microbes, including pathogens that do not synthesize riboflavin. Upon antigen recognition, elicits rapid innate-type MAIT cell activation to eliminate pathogenic microbes by directly killing infected cells (By similarity). During T cell development, drives thymic selection and post-thymic terminal differentiation of MAIT cells in a process dependent on commensal microflora (By similarity). Acts as an immune sensor of cancer cell metabolome. May present a tumor-specific or -associated metabolite essential for cancer cell survival to a pan-cancer TCR on a non-MAIT CD8-positive T cell clone, triggering T cell-mediated killing of a wide range of cancer cell types (By similarity). {ECO:0000250|UniProtKB:Q8HWB0, ECO:0000250|UniProtKB:Q95460}. | Bos taurus (Bovine) |
C1JCT1 | POL_SINV3 | MSEKTQTFVQNETHVLDMTSDFKSDLSLEKVTSSVEQTDDLVSKIINNNDLDIKDLSFLRNLLLSTLQYLGIAKFVAINITLSILSILMLLINSCAKFTRIVNLSSHILNIITTLGLYFQVSSMEIEEITQTFENEFGTYDDDKILSHYIKICNLPNRKDVYEYISLNDLKYKIKLPDISFYELKNDILSKNKNLHLWIFQKFTDEFLAMWFGVQPYRISNLREMLVISRQGFIPKDLFNEIRKLCNMGVSVIISFIQSKLFDEPFKKRDCTQALKDASVISSPFDTLWNLISKQVCDNSAEERFTQTILDFTSEFDNFLGIPNYKFAKNQKLVNTISKSLDACAKFIRDCPKDKQTEIFPLQGLHTATVKRRNEILTNVMPKFARQEPFVVLFQGPGGIGKTHLVQQLATKCVNSFYQDHEDDYIEISPDDKYWPPLSGQRVAFFDEAGNLNDLTEDLLFRNIKSICSPAYFNCAAADIEHKISPCPFELVFATVNTDLDTLQSKISSTFGQASVFPIWRRCIVVECSWNEKELGPFNYKNPSGHRSDYSHITMNYMSYDDKTQKLALEKEINFDTLFDMIRLRFRKKQQEHDTKISILNNEIQRQSNSKQHFSVCLYGEPGQGKTYNLNKLITTFANATNLKIGSEEKPSIHIFDDYIKDENDENCSKFMDIYNNKLPNNSVIFSATNVYPKTHFFPTFFLTNLIYAFIQPFKQVGLYRRLGFDGYTDIPNSSVNAPIFVQNFKFYERKQHICYFLSLEFLKNIICYIFFFLYFPLKFIKKIDLIEIKDVNKYVYDRYINFLSLSKQIEIVEYPPNLENVEFDFRFNMNKFHRVSFNNPFELDKYIHFNKNSYENLLHFDWKMYLSPRVKHRLALSYEKFFITISEVNKEIIIEELKRYVLLFKQFNIDPNMEINLGEYGSFYYINGKIHLMTINIESNVSEIPVFTDGDYVYISEHKIPVIDLFDNININSKYNLSFDQSIALNSFKTGDSFYSNAKVRKSLSKFVLLNYQTKFKLYLKEAKDKVKNFIETPIGHLLSILLTIFVICYASFKIYSKFSNFFSKDQAIEDQRKGEKKIKKITNYDSDGVQPQRKGEKKIKKVTNYDSDGVQPQSNVKVEEEIKLVFDPTGQKLLFGNDFTSELETLVELEKDDEEFTKSKIDNKSMAGLRREVRRRRYARSKKAQIEKQEVLTLPDVNGFEGGKPYFQIAEEKARKNLCQIYMIANNENCIASKFSDHIVCYGLFVFKKRLASVGHIVEALKCAPGYNLYAGCDQFNGKLYKMNLVRNYRKRELSVWDVDCPNDFVDLTSFFIPKEELYDAENCNTVLGRFGMNKREVYLYGNCEFIQEFFKVDNKGAQEFGYIDWATVDITLTTGGDCGLPYYICERKKFHNKIMGLHFAGNNVNHKTIGMSALIYKEDLVVWKGAERQSKCKFCDVKDIIIAQPDIPKEKYKGYNHEIVWNSLHESSPTTLNEELEHYLNIFPKFTGTIIKHSGDKFYGSVKHSHTQFISKFKTELTVTNGWKLSTAGDCQFESNHISPNTEVMYRVVDVQFNSIFKAFKSQPYIKNFRLIANVYEKDGKQRVTILTIIPVSDFNVKQQTVRQALVPLHLNEDEEVYVTEDVSDIFKTAIKRKQRGILPDVPYETVENETVEILGITHRNMTPEPAQMYKPTPFYKLALKFNLDHKLPVNFNMKDCPQEQKDMMVLDRLGQPNPRITQSLKWAHKDYSPDYELRKYVKEQYMCNIMEYYAGCNLLTEEQILKGYGPNHRLYGALGGMEIDSSIGWTMKELYRVTKKSDVINLDSNGNYSFLNNEAAQYTQELLKISMEQAHNGQRYYTAFNELMKMEKLKPSKNFIPRTFTAQDLNGVLMERWILGEFTARALAWDENCAVGCNPYATFHKFATKFFKFKNFFSCDYKNFDRTIPKCVFEDFRDMLIQANPHMKNEIYACFQTIIDRIQVSGNSILLVHGGMPSGCVPTAPLNSKVNDIMIYTAYVNILRRADRGDITSYRYYRDLVCRLFYGDDVIIAVDDSIADIFNCQTLSEEMKILFGMNMTDGSKSDIIPKFETIETLSFISRFFRPLKHQENFIVGALKKISIQTHFYYATDDTPEHFGQVFKTIQEEAALWEEEYFNKIQSYIQEIIRKFPEISKFFNFESYKSIQKRYIMNGWNEFVKLEKLDLNLNKKKSSKVTGIHSKQYSKFLKFLSRIENEKAALEGNFNKESVNTWYFKMSKAMHLNEIFQKGLISKPLAEFYFNEGQKMWDCNITFRRSKDDLPFTFSGSGTTKACAREQAAEEALVLFSQEDEIVRQINDIQSDCKFCKKMIRYKKLLSGVSIQRQMNVSKITENHVPSAGMMATDPSVAPDSGIATNTQTPSISRVLNPIARALDNPAGTGAPFDKHTYVYNVFTRWPEMSTVVNKSLAAGAEVFKISLDPNKLPKRILQYIQFHKTIIPQIEVQILIGGAAGTVGWLKVGWVPDASTAKKYSLDDLQLVASETINLNSTITMSMIINDSRRNGMFRLTKSDPEPWPGIVCLVEHPITNVQRNDDVNYPVIVSVRLGPDCQLMQPYNDLN | 2.7.7.48; 3.4.22.-; 3.6.4.13 | null | DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; viral RNA genome replication [GO:0039694] | virion component [GO:0044423] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968] | PF00680;PF00910; | 2.60.120.20;3.30.70.270; | null | PTM: [Capsid protein VP1]: N-acetylated. {ECO:0000269|PubMed:24686475}.; PTM: [Polyprotein]: Proteolytic cleavages of the polyprotein yield mature proteins. {ECO:0000305|PubMed:24686475}. | SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000269|PubMed:24686475}. | 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}; 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=3.6.4.13; Evidence={ECO:0000250|UniProtKB:Q6UP17}; | null | null | null | null | FUNCTION: [Capsid protein VP1]: Assembles with VP1-FSD and VP2 to form an icosahedral capsid. VP1 is about 5 time more abundant than VP1-FSD in the virion. {ECO:0000269|PubMed:24686475}.; FUNCTION: [RNA-directed RNA polymerase]: Replicates genomic and antigenomic RNA. {ECO:0000250|UniProtKB:Q6UP17, ECO:0000255|PROSITE-ProRule:PRU00539}. | Solenopsis invicta virus 3 (SINV-3) |
C1JCT2 | POLFS_SINV3 | MSEKTQTFVQNETHVLDMTSDFKSDLSLEKVTSSVEQTDDLVSKIINNNDLDIKDLSFLRNLLLSTLQYLGIAKFVAINITLSILSILMLLINSCAKFTRIVNLSSHILNIITTLGLYFQVSSMEIEEITQTFENEFGTYDDDKILSHYIKICNLPNRKDVYEYISLNDLKYKIKLPDISFYELKNDILSKNKNLHLWIFQKFTDEFLAMWFGVQPYRISNLREMLVISRQGFIPKDLFNEIRKLCNMGVSVIISFIQSKLFDEPFKKRDCTQALKDASVISSPFDTLWNLISKQVCDNSAEERFTQTILDFTSEFDNFLGIPNYKFAKNQKLVNTISKSLDACAKFIRDCPKDKQTEIFPLQGLHTATVKRRNEILTNVMPKFARQEPFVVLFQGPGGIGKTHLVQQLATKCVNSFYQDHEDDYIEISPDDKYWPPLSGQRVAFFDEAGNLNDLTEDLLFRNIKSICSPAYFNCAAADIEHKISPCPFELVFATVNTDLDTLQSKISSTFGQASVFPIWRRCIVVECSWNEKELGPFNYKNPSGHRSDYSHITMNYMSYDDKTQKLALEKEINFDTLFDMIRLRFRKKQQEHDTKISILNNEIQRQSNSKQHFSVCLYGEPGQGKTYNLNKLITTFANATNLKIGSEEKPSIHIFDDYIKDENDENCSKFMDIYNNKLPNNSVIFSATNVYPKTHFFPTFFLTNLIYAFIQPFKQVGLYRRLGFDGYTDIPNSSVNAPIFVQNFKFYERKQHICYFLSLEFLKNIICYIFFFLYFPLKFIKKIDLIEIKDVNKYVYDRYINFLSLSKQIEIVEYPPNLENVEFDFRFNMNKFHRVSFNNPFELDKYIHFNKNSYENLLHFDWKMYLSPRVKHRLALSYEKFFITISEVNKEIIIEELKRYVLLFKQFNIDPNMEINLGEYGSFYYINGKIHLMTINIESNVSEIPVFTDGDYVYISEHKIPVIDLFDNININSKYNLSFDQSIALNSFKTGDSFYSNAKVRKSLSKFVLLNYQTKFKLYLKEAKDKVKNFIETPIGHLLSILLTIFVICYASFKIYSKFSNFFSKDQAIEDQRKGEKKIKKITNYDSDGVQPQRKGEKKIKKVTNYDSDGVQPQSNVKVEEEIKLVFDPTGQKLLFGNDFTSELETLVELEKDDEEFTKSKIDNKSMAGLRREVRRRRYARSKKAQIEKQEVLTLPDVNGFEGGKPYFQIAEEKARKNLCQIYMIANNENCIASKFSDHIVCYGLFVFKKRLASVGHIVEALKCAPGYNLYAGCDQFNGKLYKMNLVRNYRKRELSVWDVDCPNDFVDLTSFFIPKEELYDAENCNTVLGRFGMNKREVYLYGNCEFIQEFFKVDNKGAQEFGYIDWATVDITLTTGGDCGLPYYICERKKFHNKIMGLHFAGNNVNHKTIGMSALIYKEDLVVWKGAERQSKCKFCDVKDIIIAQPDIPKEKYKGYNHEIVWNSLHESSPTTLNEELEHYLNIFPKFTGTIIKHSGDKFYGSVKHSHTQFISKFKTELTVTNGWKLSTAGDCQFESNHISPNTEVMYRVVDVQFNSIFKAFKSQPYIKNFRLIANVYEKDGKQRVTILTIIPVSDFNVKQQTVRQALVPLHLNEDEEVYVTEDVSDIFKTAIKRKQRGILPDVPYETVENETVEILGITHRNMTPEPAQMYKPTPFYKLALKFNLDHKLPVNFNMKDCPQEQKDMMVLDRLGQPNPRITQSLKWAHKDYSPDYELRKYVKEQYMCNIMEYYAGCNLLTEEQILKGYGPNHRLYGALGGMEIDSSIGWTMKELYRVTKKSDVINLDSNGNYSFLNNEAAQYTQELLKISMEQAHNGQRYYTAFNELMKMEKLKPSKNFIPRTFTAQDLNGVLMERWILGEFTARALAWDENCAVGCNPYATFHKFATKFFKFKNFFSCDYKNFDRTIPKCVFEDFRDMLIQANPHMKNEIYACFQTIIDRIQVSGNSILLVHGGMPSGCVPTAPLNSKVNDIMIYTAYVNILRRADRGDITSYRYYRDLVCRLFYGDDVIIAVDDSIADIFNCQTLSEEMKILFGMNMTDGSKSDIIPKFETIETLSFISRFFRPLKHQENFIVGALKKISIQTHFYYATDDTPEHFGQVFKTIQEEAALWEEEYFNKIQSYIQEIIRKFPEISKFFNFESYKSIQKRYIMNGWNEFVKLEKLDLNLNKKKSSKVTGIHSKQYSKFLKFLSRIENEKAALEGNFNKESVNTWYFKMSKAMHLNEIFQKGLISKPLAEFYFNEGQKMWDCNITFRRSKDDLPFTFSGSGTTKACAREQAAEEALVLFSQEDEIVRQINDIQSDCKFCKKMIRYKKLLSGVSIQRQMNVSKITENHVPSAGMMATDPSVAPDSGIATNTQTPSISRVLNPIARALDNPAGTGAPFDKHTYVYNVFTRWPEMSTVVNKSLAAGAEVFKISLDPNKLPKRILQYIQFHKTIIPQIEVQILIGGAAGTVGWLKVGWVPDASTAKKYSLDDLQLVASETINLNSTITMSMIINDSRRNGMFRLTKSDPEPWPGIVCLVEHPITNVQRNDDVNYPVIVSVRLGPDCQLMQPYNDLNLSGGTDPDPDPEPDPDPEPGPDPEPGVDELDLSKYIPNQLIDLLICNSYVPNNVSVDFLSTYPNLNFSIHNITDVVVSSKPYTLALFETESQINSASVWRGDLTQLSVFIQYKFYTRVEAYNKVTTVHTDKWTPNFDGTVYKPVDVKIEHAYGTYELTTMWLTSYGLVMEWSLDESRVFYGTYKTDSNGRRWLIDGNTPIARSDHCFIVSSPDLLSDDKAYYNNPIGAKQGGKLVDGAQIYRIFKTESGGYRSDPFVPETYWPSETPYNADWSGVKMPYQIRKVIQTGNNLAGKHLDGDLKMCAMIRQGSSSTQSTDNYFYPIYVHNFSALLKQMNLILKERKTKYIKFDLQVGGKPFAQMGFGDGAFIGRTTMFRQIRAAITNVILLKNIVGVDDLSGLQALPTSGFADWVVKAQSTNSKFLNDFYNDKISIERQASLGIAAAIGAGQGLFGGLSAQWQWQQQADWSRQMQRERLDMMEKLANINNQARLNQLTQSGAQQRITQQAAYQQQMNALGAGSVSAQNGMYTPSNYTPLPSYKSNTTNYYNNSVYHTDNNITNNPSNTSLTNNINNFNPELFQQQRERMPTPSEAYDNSKGFVPQPGTSKSIATENINPNYKDEEHIYEPIEQQNHEYADIDYNAMNISRENKNSSNFGNVGILDHQYADIDYDAMKIARDQQNSSKFGNVGVLNHQYAELDFSKNNTRKNSQILDNSLYSKTQPSSKMIDNSLYGINPNKMVENQNYEPASMERKNSIYSSNLNSSNNLKFNNIPNFKGPTNLNISGAKPAGFGSGIIQPAINKYTDFSKPN | 2.7.7.48; 3.4.22.-; 3.6.4.13 | null | DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; viral RNA genome replication [GO:0039694] | virion component [GO:0044423] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968] | PF00680;PF00910; | 2.60.120.20;3.30.70.270; | null | PTM: [Capsid protein VP1-FSD]: N-acetylated. {ECO:0000269|PubMed:24686475}.; PTM: [Polyprotein-FSD]: Proteolytic cleavages of the polyprotein yield mature proteins. {ECO:0000305|PubMed:24686475}. | SUBCELLULAR LOCATION: [Capsid protein VP1-FSD]: Virion {ECO:0000269|PubMed:24686475}.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000269|PubMed:24686475}. | 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}; 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=3.6.4.13; Evidence={ECO:0000250|UniProtKB:Q6UP17}; | null | null | null | null | FUNCTION: [Capsid protein VP1-FSD]: Assembles with VP1 and VP2 to form an icosahedral capsid. VP1 is about 5 time more abundant than VP1-FSD in the virion. {ECO:0000269|PubMed:24686475}.; FUNCTION: [Capsid protein VP2]: Assembles with VP1 and VP1-FSD to form an icosahedral capsid. {ECO:0000269|PubMed:24686475}.; FUNCTION: [RNA-directed RNA polymerase]: Replicates genomic and antigenomic RNA. {ECO:0000250|UniProtKB:Q6UP17, ECO:0000255|PROSITE-ProRule:PRU00539}. | Solenopsis invicta virus 3 (SINV-3) |
C1K5M2 | CPT1_SOLLC | MSSLVLQCWKLSSPSLILQQNTSISMGAFKGIHKLQIPNSPLTVSARGLNKISCSLNLQTEKLCYEDNDNDLDEELMPKHIALIMDGNRRWAKDKGLEVYEGHKHIIPKLKEICDISSKLGIQIITAFAFSTENWKRSKEEVDFLLQMFEEIYDEFSRSGVRVSIIGCKSDLPMTLQKCIALTEETTKGNKGLHLVIALNYGGYYDILQATKSIVNKAMNGLLDVEDINKNLFDQELESKCPNPDLLIRTGGEQRVSNFLLWQLAYTEFYFTNTLFPDFGEEDLKEAIMNFQQRHRRFGGHTY | 2.5.1.28 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:23134568}; | plastid membrane organization [GO:0009668]; polyprenol biosynthetic process [GO:0016094]; response to cold [GO:0009409] | chloroplast [GO:0009507]; chloroplast stroma [GO:0009570] | dehydrodolichyl diphosphate synthase activity [GO:0045547]; dimethylallylcistransferase activity [GO:0047863]; magnesium ion binding [GO:0000287]; polyprenyltransferase activity [GO:0002094]; prenyltransferase activity [GO:0004659] | PF01255; | 3.40.1180.10; | UPP synthetase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:23134568}. | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + neryl diphosphate; Xref=Rhea:RHEA:11328, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:57665, ChEBI:CHEBI:128769; EC=2.5.1.28; Evidence={ECO:0000269|PubMed:19487664, ECO:0000269|PubMed:23134568, ECO:0000269|PubMed:23757397}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11329; Evidence={ECO:0000269|PubMed:19487664, ECO:0000269|PubMed:23134568, ECO:0000269|PubMed:23757397}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=152 uM for isopentenyl diphosphate {ECO:0000269|PubMed:19487664}; KM=177 uM for dimethylallyl diphosphate {ECO:0000269|PubMed:19487664}; | null | null | null | FUNCTION: Uses dimethylallyl diphosphate and isopentenyl diphosphate to catalyze the cis-prenyl chain elongation and produce the 10 carbon product neryl diphosphate. {ECO:0000269|PubMed:19487664, ECO:0000269|PubMed:23134568, ECO:0000269|PubMed:23757397}. | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
C1PGW1 | TED7_ZINEL | MASPLSQSVFPHFPPPSPAATPPPAPTTPSTPPPHFISPPPHSVPPPSPPHSVPPPLHPVPPPSPPHPVSPPPHTVPPPSPPHPVSPPPHTVPPPSPPHPVFPPPHTVPPPSPHFVPPPPNMVPPPSPPHANPPPPPPPHSVPPPPHTVPPPPPPPHIIPPPAHALSPPPPHIIPPPPPSPSNHSTTIVVIFVSCGGVFFLAFAMAALWCFLKKKKKKMVQKAENIHFDEHRKVTERIEQGPHGTETAILSVEDDIHIEEDIKKSELENFRKGLHLNYGNTYNIDTGKPSSSFGHHYLHG | null | null | cell wall organization [GO:0071555]; plant-type secondary cell wall biogenesis [GO:0009834]; regulation of secondary cell wall biogenesis [GO:2000652]; tracheary element differentiation [GO:1905177] | extracellular region [GO:0005576]; plant-type cell wall [GO:0009505]; plasma membrane [GO:0005886] | null | null | null | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19383897}; Single-pass membrane protein {ECO:0000255}. Secreted, cell wall {ECO:0000269|PubMed:19383897}. | null | null | null | null | null | FUNCTION: Involved in the secondary cell wall (SCW) formation of vessel elements (e.g. protoxylem and metaxylem), thus promoting tracheary element (TE) differentiation. {ECO:0000269|PubMed:19383897}. | Zinnia elegans (Garden zinnia) (Zinnia violacea) |
C3JXY0 | AK_PSEFS | MALIVQKFGGTSVGSVERIEQVADKVKKFRDAGDDLVVVLSAMSGETNRLIDLAKAISGDQQPLPRELDVIVSTGEQVTIALLAMALNKRGVPAVSYTGSQVRILTDSAHTKARILQIDDQKIRTDLKAGRVVVVAGFQGVDEQGNITTLGRGGSDTTGVALAAALKADECQIYTDVDGVYTTDPRVVSVAQRLDKITFEEMLEMASLGSKVLQIRAVEFAGKYNVPLRVLHSFKEGPGTLITIDEEESMEQPIISGIAFNRDEAKLTIRGVPDTPGVAFKILGPISGANIEVDMIVQNVSHDNTTDFTFTVHRNEYDAAERILQNTAKEIGAREVVGDTKIAKVSIVGVGMRSHAGVASRMFEALAKESINIQMISTSEIKVSVVIEEKYLELAVRALHTAFELDAPARQGE | 2.7.2.4 | null | diaminopimelate biosynthetic process [GO:0019877]; homoserine biosynthetic process [GO:0009090]; lysine biosynthetic process via diaminopimelate [GO:0009089]; methionine biosynthetic process [GO:0009086]; phosphorylation [GO:0016310]; threonine biosynthetic process [GO:0009088] | cytosol [GO:0005829] | aspartate kinase activity [GO:0004072]; ATP binding [GO:0005524] | PF00696;PF01842;PF13840; | 3.40.1160.10;3.30.2130.10; | Aspartokinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP; Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4; Evidence={ECO:0000269|PubMed:4357740, ECO:0000269|PubMed:4357741}; | null | PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3.; PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5. | null | null | FUNCTION: Involved in the biosynthesis of L-aspartate-beta-semialdehyde which is a central intermediate in the biosynthesis of different amino acids (L-lysine, L-methionine, L-threonine). Catalyzes the phosphorylation of the beta-carboxyl group of L-aspartate to yield 4-phospho-L-aspartate. {ECO:0000269|PubMed:4357740, ECO:0000269|PubMed:4357741}. | Pseudomonas fluorescens (strain SBW25) |
C3SBW0 | PNMT_THLFG | METKQTKKEAVANLIKRIEHGEVSDEEIRGMMKIQVQKRLKWGYKPTHEQQLAQLVTFAQSLKGMEMAEEVDTLDAELYEIPLPFLHIMCGKTLKFSPGYFKDESTTLDESEVYMMDLYCERAQIKDGQSILDLGCGHGSLTLHVAQKYRGCKVTGITNSVSQKEFIMDQCKKLDLSNVEIILEDVTKFETEITYDRIFAVALIEHMKNYELFLKKVSTWIAQYGLLFVEHHCHKVFAYQYEPLDEDDWYTEYIFPSGTLVMSSSSILLYFQEDVSVVNHWTLSGKHPSLGFKQWLKRLDDNIDEVKEIFESFYGSKEKAMKFITYWRVFCIAHSQMYSTNNGEEWMLSQVLFKKK | 2.1.1.300 | null | methylation [GO:0032259] | cytoplasm [GO:0005737] | methyltransferase activity [GO:0008168] | PF02353; | 3.40.50.150; | CFA/CMAS family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:19624470}. | CATALYTIC ACTIVITY: Reaction=(+-)-pavine + S-adenosyl-L-methionine = H(+) + N-methylpavine + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:39979, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76921, ChEBI:CHEBI:76922; EC=2.1.1.300; Evidence={ECO:0000269|PubMed:19624470, ECO:0000269|PubMed:27573242}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39980; Evidence={ECO:0000305|PubMed:19624470, ECO:0000305|PubMed:27573242}; CATALYTIC ACTIVITY: Reaction=(S)-reticuline + S-adenosyl-L-methionine = (S)-tembetarine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51520, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:57873, ChEBI:CHEBI:59789, ChEBI:CHEBI:134199; Evidence={ECO:0000269|PubMed:27573242}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51521; Evidence={ECO:0000305|PubMed:27573242}; CATALYTIC ACTIVITY: Reaction=(S)-stylopine + S-adenosyl-L-methionine = (S)-cis-N-methylstylopine + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:75975, ChEBI:CHEBI:444, ChEBI:CHEBI:18285, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; Evidence={ECO:0000269|PubMed:19624470, ECO:0000269|PubMed:27573242}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75976; Evidence={ECO:0000305|PubMed:19624470, ECO:0000305|PubMed:27573242}; CATALYTIC ACTIVITY: Reaction=(S)-scoulerine + S-adenosyl-L-methionine = (S)-cis-N-methylscoulerine + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:76051, ChEBI:CHEBI:17129, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:76923; EC=2.1.1.300; Evidence={ECO:0000269|PubMed:19624470, ECO:0000269|PubMed:27573242}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76052; Evidence={ECO:0000305|PubMed:19624470, ECO:0000305|PubMed:27573242}; CATALYTIC ACTIVITY: Reaction=(S)-tetrahydropapaverine + S-adenosyl-L-methionine = (S)-N-methyltetrahydropapaverine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51548, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:195218, ChEBI:CHEBI:195219; Evidence={ECO:0000269|PubMed:27573242}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51549; Evidence={ECO:0000305|PubMed:27573242}; CATALYTIC ACTIVITY: Reaction=(S)-tetrahydropalmatine + S-adenosyl-L-methionine = (S)-cis-N-methyltetrahydropalmatine + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:76047, ChEBI:CHEBI:16563, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:194514; Evidence={ECO:0000269|PubMed:19624470}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76048; Evidence={ECO:0000305|PubMed:19624470}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=47 uM for (+-)-pavine {ECO:0000269|PubMed:19624470}; KM=16 uM for (R,S)-tetrahydropapaverine {ECO:0000269|PubMed:27573242}; Vmax=0.001 pmol/sec/mg enzyme with (+-)-pavine as substrate {ECO:0000269|PubMed:19624470}; Note=kcat is 0.00005 sec(-1) with (+-)-pavine as substrate (PubMed:19624470). kcat is 0.00079 sec(-1) with (R,S)-tetrahydropapaverine as substrate (PubMed:27573242). {ECO:0000269|PubMed:19624470, ECO:0000269|PubMed:27573242}; | PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:19624470}. | null | null | FUNCTION: N-methyltransferase with a substrate preference for (+-)-pavine and (S)-reticuline, but also active with the protoberberines scoulerine and stylopine and, to a lesser extent, tetrahydropapaverine (THP) and tetrahydropalmatine (PubMed:19624470, PubMed:27573242). Is not active on (R)-reticuline, cryptopine, glaucine, codeine, canadaline, noscapine and berbamine (PubMed:27573242). {ECO:0000269|PubMed:19624470, ECO:0000269|PubMed:27573242}. | Thalictrum flavum subsp. glaucum (Yellow meadow rue) |
C3UVB0 | ACD_DESML | MDFNLSKELQMLQKEVRNFVNKKIVPFADQWDNENHFPYEEAVRPMGELGFFGTVIPEEYGGEGMDQGWLAAMIVTEEIARGSSALRVQLNMEVLGCAYTILTYGSEALKKKYVPKLSSAEFLGGFGITEPDAGSDVMAMSSTAEDKGDHWLLNGSKTWISNAAQADVLIYYAYTDKAAGSRGLSAFVIEPRNFPGIKTSNLEKLGSHASPTGELFLDNVKVPKENILGKPGDGARIVFGSLNHTRLSAAAGGVGLAQACLDAAIKYCNERRQFGKPIGDFQMNQDMIAQMAVEVEAARLLAYKAAAAKDEGRLNNGLDVAMAKYAAGEAVSKCANYAMRILGAYGYSTEYPVARFYRDAPTYYMVEGSANICKMIIALDQLGVRKANR | 1.3.99.32 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:19395484, ECO:0000269|PubMed:20486657}; | aromatic compound catabolic process [GO:0019439]; leucine catabolic process [GO:0006552] | null | flavin adenine dinucleotide binding [GO:0050660]; isovaleryl-CoA dehydrogenase activity [GO:0008470] | PF00441;PF02770;PF02771; | 1.10.540.10;2.40.110.10;1.20.140.10; | Acyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=A + glutaryl-CoA = (2E)-glutaconyl-CoA + AH2; Xref=Rhea:RHEA:47420, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:57353, ChEBI:CHEBI:57378; EC=1.3.99.32; Evidence={ECO:0000269|PubMed:19395484}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25 uM for glutaryl-CoA; Vmax=11 mmol/min/mg enzyme; | PATHWAY: Aromatic compound metabolism; benzoyl-CoA degradation. {ECO:0000269|PubMed:19395484}. | null | null | FUNCTION: Catalyzes the dehydrogenation of Glutaryl-CoA to glutaconyl-CoA. {ECO:0000269|PubMed:19395484}. | Desulfococcus multivorans |
C3VD30 | ZAR1L_MOUSE | MERLFCVPCGYGTTDPLTYPGPWRHCQQQNWPQNMGAPIFLARLRVPANVSQSCMNPYNRAQLQAVSTQMDPNLSLWLRSVHTTEVGVQVSLRVDKSVQCSQGSQTLHSSSLSDRTSSRKPTEAWEVGRRALIRRPQDGEDEESQEELTGPTEASQLLLPTWSRDREEQFPRLKELGEEYAHSPQDRKGKQFLELKYGYFHCKDCKRRWESAYVWCISGTNKVYFKQLCNKCQKSFNPYRVEEIQCQTCLRVCCSCSPKKRHIDVRRPHRQELCGHCKDKKFSCSVFFSLK | null | null | negative regulation of translation [GO:0017148]; oocyte maturation [GO:0001556]; translation [GO:0006412] | cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; intracellular non-membrane-bounded organelle [GO:0043232] | metal ion binding [GO:0046872]; mRNA 3'-UTR binding [GO:0003730] | PF13695; | null | ZAR1 family | null | SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:20014101, ECO:0000269|PubMed:31598710}. | null | null | null | null | null | FUNCTION: mRNA-binding protein required for maternal mRNA storage, translation and degradation during oocyte maturation (PubMed:31598710). Probably promotes formation of some phase-separated membraneless compartment that stores maternal mRNAs in oocytes: acts by undergoing liquid-liquid phase separation upon binding to maternal mRNAs (By similarity). Binds to the 3'-UTR of maternal mRNAs, inhibiting their translation (PubMed:31598710). {ECO:0000250|UniProtKB:Q80SU3, ECO:0000269|PubMed:31598710}. | Mus musculus (Mouse) |
C3VPR6 | NLRC5_MOUSE | MDAESIRLNNENLWAWLVRLLSKNPEWLSAKLRSFLPTMDLDCSYEPSNPEVIHRQLNRLFAQGMATWKSFINDLCFELDVPLDMEIPLVSIWGPRDEFSKQLGAGEESCPGPQLYHGAKRPFQSYGSSPRRKNSKKQQLELAKKYLKLLKTSAQQWHGGVCPGAWLTPHSPQTYIPPVLQWSRATAPLDAQEGATLGDPEAADNIDVSIQDLFSFKAHKGPRVTVLLGKAGMGKTTLAYRLRWRWAQGQLDRFQALFLFEFRQLNMITQLPTLPQLLFDLYLMPESEPDAVFQYLKENAQEVLLIFDGLDEALHADSVGTDNAGSALTLFSELCHGNLLPGCWVMTTSRPGKLPSCVPTEAATVHMWGFDGLRVEKYVTCFFSDLLSQELALKEMRTNARLRGMCAIPALCTVTCFCLRRLLPGSSPGQSAALLPTITQLYLQMVETFSPSETLLDTSILGFGKVALRGLDTGKVVFSVEDISPQLMSFGAVHSLLTSFCIHTRPGHEEIGYAFVHLSLQEFFAALYLMASHTVDKDTLVEYVTLNSHWVLRTKGRLGLSDHLPAFLAGLASHTCHMFLCQLAQQDRAWVGSRQAAVIQVLRKLASRKLTGPKMIELYHCVAETQDLELARFTAQSLPSRLSFHNFPLTHADLAALANILEHRDDPIHLDFDGCPLEPHCPEALVGCGQVENLSFKSRKCGDAFAEALCRSLPTMGSLKTLGLTGSRITAQGISHLIQTLPLCSQLEEVSLHDNQLKDPEVLSLVELLPSLPKLQKLDLSRNSFSRSILLSLVKVAITCPTVRKLQVRELDLIFYLSPVTETATQQSGASDVQGKDSLKEGQSRSLQLRLQKCQLRIRDAEALVELFQKSPQLEEVNLSGNHLEDDGCRLVAEAASQLHIAQKLDLSDNGLSQTGVTYVLKAMSTCGTLEDLHISLLNNTVVLTFAQEPREQEGSCKGRAPLISFVSPVTSELSQRSRRIRLTHCGFLAKHTETLCEALRASCQTHNLDHLDLSDNSLGGKGVILLTELLPGLGPLKSLNLSRNGLSMDAVFSLVQCLSSLQWVFHLDVSLESDCIFLRGAGTSRDALEPKFQTGVQVLELSQRYTSRSFCLQECQLEPTSLTFLCATLEKSPGPLEVQLSCKSLSDDSLKILLQCLPQLPQLSLLQLRHTVLSSRSPFLLADIFNLCPRVRKVTLRSLCHAVLHFDSNEEQEGVCCGFPGCSLSQEHMETLCCALSKCNALSQLDLTDNLLGDIGLRCLLECLPQLPISGWLDLSHNNISQEGILYLLETLPSYPNIQEVSVSLSSEQIFRMCFSKKEGAGTSLRLCECSFSPEQVSKLASSLSQAQQLTELWLTKCHLDLPQLTMLLNLVNRPTGLLGLRLEEPWVDSVSLPALMEVCAQASGCLTELSISEIQRKLWLQLEFPHQEGNSDSMALRLAHCDLETEHSHLMIQLVETYARLQQLSLSQVSFNDNDGTSSKLLQNILLSSCELKSFRLTFSQVSTKSLTHLAFGLGHCHHLEELDFSNNSLREEDTELLMGALQGTCRLKKLHLSFLPLGASSLALLIQGLSRMTLLQDLCLSHNQIGDVGTQCLAAILPKLPELRKFDLSHNQIGDVGTQCLAAILPKLPELRKFNLSHNQIGHVGTQCLAAILPKLPELRKFDLSRNQIGDVGTQCLAAILPKLPELRKFDLSGNRIGPAGGVQLVKSLTHFEHLEEIKLGNNALGEPTALELAQRLPPQLRVLCLPSSHLGPEGALGLAQALEQCPHIEEVSLAENNLAGGVPRFSKRLPLLRQIDLEFCKIEDQAARHLAANLTLFPALEKLLLSGNLLGDEVAAELAQVLPQMGQLKKVNLEWNRITARGAQLLAQGLVQGSCVPVIRLWNNPILNDVAQSLQSQEPRLDFSITDQQTL | null | null | defense response to virus [GO:0051607]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of type I interferon-mediated signaling pathway [GO:0060339]; positive regulation of MHC class I biosynthetic process [GO:0045345]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of type I interferon-mediated signaling pathway [GO:0060340]; positive regulation of type II interferon-mediated signaling pathway [GO:0060335]; response to bacterium [GO:0009617] | centrosome [GO:0005813]; cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF18461;PF13516;PF05729;PF17776; | 1.10.533.20;3.40.50.300;3.80.10.10; | NLRP family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Probable regulator of the NF-kappa-B and type I interferon signaling pathways. May also regulate the type II interferon signaling pathway. Plays a role in homeostatic control of innate immunity and in antiviral defense mechanisms. {ECO:0000269|PubMed:20434986}. | Mus musculus (Mouse) |
C3W4R6 | PA2A1_MACLB | MRTLWIVAVWLMGVEGDLSQFGDMINKKTGTFGLFSYIYYGCYCGWGGKGKPQDATDRCCFVHDCCYGSVNGCDPKLSTYSYSFQNGDIVCGDDDPCLRAVCECDRVAAICFGENMNTYDKKYMLYSLFDCKEESEKC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; 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, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=676 umol/min/mg enzyme {ECO:0000269|PubMed:19467252}; | null | null | null | FUNCTION: Snake venom phospholipase that inhibits ADP- and collagen-induced human platelet aggregation. This inhibition is completely inhibited by abolition of catalytic activity in case of collagen as inducer and partially inhibited in case of ADP as inducer. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:19467252}. | Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
C3W947 | CTSR_GEOSE | MPNISDIIEQYLKQVLNMSDQDIVEIKRSEIANKFRCVPSQINYVINTRFTLERGYIVESKRGGGGYIRIMKVKTKSEAQLIDQLLELIDHRISQSSAEDVIKRLMEEKVISEREAKMMLSVMDRSVLYIDLPERDELRARMLKAMLTSLKYK | null | null | regulation of DNA-templated transcription [GO:0006355] | null | DNA binding [GO:0003677] | PF05848;PF17727; | 1.10.1200.150;3.30.56.130; | CtsR family | PTM: Phosphorylated on Arg-28, Arg-49 and Arg-62 by McsB. {ECO:0000269|PubMed:19498169}. | null | null | null | null | null | null | FUNCTION: Controls the expression of the cellular protein quality control genes clpC, clpE and clpP, as well as mcsA and mcsB, by acting as a repressor of these class III stress genes. After heat shock, CtsR is degraded by the ClpCP and ClpEP proteolytic systems, ensuring the derepression of clpE, clpP and the clpC operon. CtsR negatively autoregulates its own synthesis (By similarity). {ECO:0000250}. | Geobacillus stearothermophilus (Bacillus stearothermophilus) |
C4AMC7 | WASH3_HUMAN | MTPVRMQHSLAGQTYAVPLIQPDLRREEAVQQMADALQYLQKVSGDIFSRISQQVEQSRSQVQAIGEKVSLAQAKIEKIKGSKKAIKVFSSAKYPAPERLQEYGSIFTGAQDPGLQRRPRHRIQSKHRPLDERALQEKDFPVCVSTKPEPEDDAEEGLGGLPSNISSVSSLLLFNTTENLGKKYVFLDPLAGAVTKTHVMLGAETEEKLFDAPLSISKREQLEQQVPENYFYVPDLGQVPEIDVPSYLPDLPGITNDLMYIADLGPGIAPSAPGTIPELPTFHTEVAEPLKVDLQDGVLTPPPPPPPPPPAPEVLASAPPLPPSTAAPVGQGARQDDSSSSASPSVQGAPREVVDPSGGRATLLESIRQAGGIGKAKLRSMKERKLEKKQQKEQEQVRATSQGGHLMSDLFNKLVMRRKGISGKGPGAGEGPGGAFARVSDSIPPLPPPQQPQAEEDEDDWES | null | null | Arp2/3 complex-mediated actin nucleation [GO:0034314]; early endosome to late endosome transport [GO:0045022]; endocytic recycling [GO:0032456]; endosomal transport [GO:0016197]; endosome organization [GO:0007032]; exocytosis [GO:0006887]; protein targeting to lysosome [GO:0006622]; regulation of Arp2/3 complex-mediated actin nucleation [GO:0034315]; retrograde transport, endosome to Golgi [GO:0042147] | autophagosome [GO:0005776]; centriole [GO:0005814]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; filopodium [GO:0030175]; lamellipodium [GO:0030027]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; WASH complex [GO:0071203] | actin binding [GO:0003779]; alpha-tubulin binding [GO:0043014]; gamma-tubulin binding [GO:0043015] | PF11945; | null | WASH1 family | null | SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:20175130, ECO:0000269|PubMed:20498093}. Early endosome membrane {ECO:0000250|UniProtKB:A8K0Z3}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q8VDD8}. Cell projection, lamellipodium {ECO:0000269|PubMed:18159949}. Cell projection, filopodium {ECO:0000269|PubMed:18159949}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q8VDD8}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8VDD8}. Note=Localization to the endosome membrane is mediated via its interaction with WASHC2. Localizes to MMP14-positive late endosomes and transiently to invadipodia (By similarity). Localized to Salmonella typhimurium entry sites (By similarity). {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:Q8VDD8}. | null | null | null | null | null | FUNCTION: Acts as a nucleation-promoting factor at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting (PubMed:18159949, PubMed:20175130). Involved in endocytic trafficking of EGF (PubMed:20175130). Involved in transferrin receptor recycling. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration (By similarity). In T-cells involved in endosome-to-membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL; proposed to be implicated in T cell proliferation and effector function. In dendritic cells involved in endosome-to-membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T-cell activation. Involved in Arp2/3 complex-dependent actin assembly driving Salmonella typhimurium invasion independent of ruffling (By similarity). Involved in the exocytosis of MMP14 leading to matrix remodeling during invasive migration and implicating late endosome-to-plasma membrane tubular connections and cooperation with the exocyst complex (By similarity). Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (By similarity). {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:Q8VDD8, ECO:0000269|PubMed:18159949, ECO:0000269|PubMed:20175130}. | Homo sapiens (Human) |
C4B4E5 | ATG26_GLOLA | MPPPPLSLPLHGPAGAASVTFAGDEDVKKRVGKKLQKKRHEPTTPAVELPERLKEGDDAGEEDLVPTQGPPMFMNMNQSIFGLIAAAGSRVDFHDRFESSDDESADEGPQRDSADRSHSSSTHGLFLHRKQRRRDESDVAKTTVLNKDPYGSGKPEKHKRKISGHKLLRSLPALPRLPRHKSKKESSKLEPPSEEASDGSGFAQSQPVDEAEDDEDDKDHRLAPVMSRMLEAKAEMSARPSFDVERFSSDQLTYSESADSNDTALARRLQDIFEFDQPEAVIEEYPCWLLQSVLLQGYMYITAKHICFYSYLPKKALEVVKSGYLSKSGKRNPKYNRYWFRLKGDVLSYFKDPSNVYFPSGQIDLRYGISASVTDKKDGLNFTVVTHHRTYHFRADSAPSAKEWVKSLQRVIFRSHNEGDSVKISLPIENVIDIEDTQMLNFADTCKIRVIDNDETYAIDEYFFSFFSFGKEAISVLKILIEDASSTAKDAARLKAVQEEEDRQQQQQQQHPMQPPMQASARSSMSGSRRAIAPPKLTTNKLPEAVKATLSPMSAHSPSALSPRASMDAARASFDAFRSFRRRSLDLSTIIRDSSPRRSFSGNRRSMSRNRLDDQRRGPHQQGSTDSYVQSSMEEPSFSGMVASSIEDPSASQILRGSDVFQNPTMRRSGSASRTEVEKQQRRDPRSPPTLATYSGQHAATAGSLNDGDKQPVTPTLQSITKMGAFPLQRVGAFAEYLNNTSSKLGSMLATESMGYVEKVSGMWRGGRKHYDAPPEIKTDDEDLYEDAEGKIQTSMDRFRAHFALPETEKLQATYFGHILRVLPLYGKIYISDKSFCFRSLLPGTRTKLILPLKDIENVDKEKGFRFGYSGLVVVIRGHEEIFFEFGQAEVRDDCAVTLLQSLETTRYLEKIGDLDTEEREDEENAMAERDALKEARQTEEFHDHDVHLPKETSGVSDAPTILFDDPKASFLNFKPPQPLKITCLTIGSRGDVQPYIALCKGLLAEGHKPRIATHGEFKDWIEGHGIEFAKVEGDPGELMRLCIENGTFTWAFLREANSMFRGWLDELLVSAWEACKGSDLLIESPSAMAGIHIAEKLSIPYFRAFTMPWTRTRAYPHAFIMPEYKMGGAYNYMTYVMFDNVFWKATAHQVNRWRNNTLKLPNTSLEKMQPNKVPFLYNFSEYVVAPPLDFSDWIRVTGYWFLDEGSDWVPPQELTDFIAKARADEKKLVYVGFGSIIVNDTAKMTQEVIDAVLKADVRCILSKGWSDRMGKQGEEAVDQPVMPPEIHVIKSAPHDWLFSQIDAAAHHGGSGTTGASLRAGIPTIIRPFFGDQFFFGSRVEDIGVGICLKKWGAISFARALWEATHNDRMIVKARVLGEQIRSENGVDSAIQCIYRDMEYAKSLIKRKAGKNIQVEPDEDEESAEESWTFIGNDEPDPDMTTKKLSEMPTLPGSSDTKPLGTRIMRVSPSQQSVA | 2.4.1.-; 2.4.1.173 | null | autophagy [GO:0006914]; carbohydrate metabolic process [GO:0005975]; lipid glycosylation [GO:0030259]; protein transport [GO:0015031]; sterol metabolic process [GO:0016125] | phagophore assembly site membrane [GO:0034045] | brassicasterol glucosyltransferase activity [GO:0102203]; cholesterol alpha-glucosyltransferase activity [GO:0102205]; ergosterol UDP-glucosyltransferase activity [GO:0051506]; soladodine glucosyltransferase activity [GO:0102202] | PF06722;PF03033;PF02893;PF00169; | 3.40.50.2000;2.30.29.30; | Glycosyltransferase 28 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06321}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q2U0C3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q2U0C3}. | CATALYTIC ACTIVITY: Reaction=a sterol + UDP-alpha-D-glucose = a sterol 3-beta-D-glucoside + H(+) + UDP; Xref=Rhea:RHEA:22724, ChEBI:CHEBI:15378, ChEBI:CHEBI:15889, ChEBI:CHEBI:37424, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.173; Evidence={ECO:0000250|UniProtKB:Q06321}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22725; Evidence={ECO:0000250|UniProtKB:Q06321}; CATALYTIC ACTIVITY: Reaction=ergosterol + UDP-alpha-D-glucose = ergosteryl 3-beta-D-glucoside + H(+) + UDP; Xref=Rhea:RHEA:61836, ChEBI:CHEBI:15378, ChEBI:CHEBI:16933, ChEBI:CHEBI:52973, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; Evidence={ECO:0000250|UniProtKB:Q06321}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61837; Evidence={ECO:0000250|UniProtKB:Q06321}; | null | null | null | null | FUNCTION: Sterol glycosyltransferase responsible for the glycosylation of ergosterol to form ergosterol-glucoside (By similarity). Mediates autophagic degradation of peroxisomes (pexophagy) and is involved in pathogenesis via peroxisome degradation inside appressoria that are developing into the host invasion stage (PubMed:19363139). {ECO:0000250|UniProtKB:Q06321, ECO:0000269|PubMed:19363139}. | Glomerella lagenarium (Anthracnose fungus) (Colletotrichum lagenarium) |
C4B644 | CPVDH_PSEAH | MALTTTGTEQHDLFSGTFWQNPHPAYAALRAEDPVRKLALPDGPVWLLTRYADVREAFVDPRLSKDWRHTLPEDQRADMPATPTPMMILMDPPDHTRLRKLVGRSFTVRRMNELEPRITEIADGLLAGLPTDGPVDLMREYAFQIPVQVICELLGVPAEDRDDFSAWSSVLVDDSPADDKNAAMGKLHGYLSDLLERKRTEPDDALLSSLLAVSDEDGDRLSQEELVAMAMLLLIAGHETTVNLIGNGVLALLTHPDQRKLLAEDPSLISSAVEEFLRFDSPVSQAPIRFTAEDVTYSGVTIPAGEMVMLGLAAANRDADWMPEPDRLDITRDASGGVFFGHGIHFCLGAQLARLEGRVAIGRLFADRPELALAVGLDELVYRESTLVRGLSRMPVTMGPRSA | 1.14.15.15 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P0A512}; | cholesterol catabolic process [GO:0006707] | cytoplasm [GO:0005737] | 3-alpha,7-alpha,12-alpha-trihydroxycholestan-26-al 26-oxidoreductase activity [GO:0047103]; cholest-4-en-3-one 26-monooxygenase activity [GO:0036199]; cholestanetetraol 26-dehydrogenase activity [GO:0047748]; cholestanetriol 26-monooxygenase activity [GO:0047749]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; steroid hydroxylase activity [GO:0008395] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A512}. | CATALYTIC ACTIVITY: Reaction=5beta-cholestane-3alpha,7alpha,12alpha-triol + 5 H(+) + 3 O2 + 6 reduced [adrenodoxin] = (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + 4 H2O + 6 oxidized [adrenodoxin]; Xref=Rhea:RHEA:34631, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16496, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:58734; EC=1.14.15.15; Evidence={ECO:0000269|PubMed:19450562}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13.5 uM for vitamin D(3) {ECO:0000269|PubMed:19450562}; KM=7.1 uM for 25-hydroxyvitamin D(3) {ECO:0000269|PubMed:19450562}; | null | null | null | FUNCTION: Hydroxylates vitamin D(3) into 25-hydroxyvitamin D(3) and 1-alpha,25-dihydroxyvitamin D(3), its physiologically active forms. It first hydroxylates the C-25 position of vitamin D(3) to form 25-hydroxyvitamin D(3), then subsequently hydroxylates the C-1-alpha position to form 1-alpha,25-dihydroxyvitamin D(3). Also displays 25-hydroxylase activity on vitamin D(2) and 7-dehydrocholesterol. May play a role in the biosynthesis of steroid metabolic intermediates. {ECO:0000269|PubMed:19450562}. | Pseudonocardia autotrophica (Amycolata autotrophica) (Nocardia autotrophica) |
C4JYG6 | ARO1_UNCRE | MATPTVIKILGRDSIVADPGIWKRHVAQDLLTNCPSSTYILISDTTLTPLYVPSFQQAFEAAASSVTPKPRLLTYAIPPGEVSKSRQTKAEIEDWMLSRQPPCGRDTVIIALGGGVIGDLIGYVSATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTTHGKNLIGAIWQPEKIYLDMEFLNTLPEREFINGMAETAAISSEEDFAALERNADAILAAVKSENTTERPRFSGIQEILKLTILASARFKADVVSKDEREGGLRNLLNFGHSIGHAIEGILAPQILHGECVAIGMVKEAELARHLGILKSVAVSRLVKCLASYGLPTSLKDSRVRRLSAGKHCSVEQLLAFMAVDKKNAGPMKKVVLLSSIGSTHEQKASVVSNKDIKIVLAPSIEVSPGVPHALEITCVPPGSKSISNRALVLAALGSGTCRIKNLLHSDDTEVMLSALERLGAATFSWEEEGEVLVVHGKGGRLQASPDALYLGNAGTASRFLTTVATLANKSTVDSTILTGNARMKQRPIGALVDSLRTNGAGIKYMETTGCLPLKIDASGGFAGGHISLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGKPISQPYIDMTTAMMRSFGIDVKKSTSEEHTYHIPQGRYMNPTEYIIESDASSATYPLAVAAITGTTCTIPNIGSKSLQGDARFAVDVLRPMGCEVNQSSFSTTVTGPRNGALNALPNVDMEPMTDAFLTASVLAAVATAGSTSTTRIFGIANQRVKECNRIKAMKDELAKFGVTCREHEDGLEIDGIDRSALLRLPHGVYCYDDHRVAMSFSVLSLAASHPTLILEKECVGKTWPAWWDTLAQLFKANLEGVELKSEKKKAEKPAASLFIIGMRGAGKTTSGLWASKVLKRPFIDLDVELESKLGKSIPEIIKEQGWEGFRANELALLRQVLSEKPTGYVFACGGGIVETEEARDLLTQYQKAHGNVLLVMRDINAVMDFLKIDKTRPAYVEDMMGVWLRRKPWFQQCSNIQYYSQQSDPSKMGSALESFSRFLRVVTGEVDHLALMKKKPQSFFVSLTLPDLRPSVDILNDITLGSDAVELRVDLLVDPSSSSEMPSVDYVAEQISILRSRVSVPLVFTIRTKSQGGRFPDDAHNAALDLYRLAIRMGSEFVDLEVTFPEYVLRAVTEMKGVSKIIASHHDVANRLSWRNGSWTQFYNKALQYGDIIKLVGIASQLDDNIALREFKIWAKKAHDIPVIAINMGERGRLSRILNGFMTPVSHPKLPFKAAPGQLSAKEIREGLSLMGEIESKKFAIVGKPISASRSPALHNALFADVGLPHVYGRLETDDVQNVKDLIHAPDFGGASITIPLKLDIMPLLDEIAPEAKVIGAVNTIVPAPREPGDVKKGPRLIGYNTDWQGMVQCLRHGGAVSPSTSNDPAPGLVIGGGGTARAAIHALHSMGYSPIYLVGRSESKLNDMALSFPATYNLQILKDAESLEILPSVAIGTIPGDQPIDPSMREVLCRLFEMAARIDAELKELAPKRVLLEMAYKPTVTPLSQLASDCGWATIPGLEALVGQGVYQFQLWTGITPVFRDARAAVMNADADI | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF18317;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Uncinocarpus reesii (strain UAMH 1704) |
C4LSS0 | ARGI_ENTH1 | MQFEKVTYIAVPQKYGQKKVGVEEGPKFLEKLGFMNVLEQVAKSVNKKTITEPKTPQELGVTNARNLNEVESVNIELRDTIAKEYDVNNLLINIGGDHSIGLGTIAGVVKAMKPNARVGVVWFDAHPDMNTPENSPSGNIHGMPLACAVGLGPQRLTSIMPHYITPKDIMYVGIRSIDVGEQFEIQDKHIDHFTAEDVKRVGMKEVIEAINKKFVDYDVIHLSFDIDGIDPEFILGTGTPVPKGISLEDSLYFMSEMGKMKKLHSVDIVEYNPKIEEEITGKNVLKCISSLFGIKC | 3.5.3.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|RuleBase:RU361159, ECO:0000269|PubMed:29691540}; Note=Binds 2 manganese ions per subunit. {ECO:0000255|RuleBase:RU361159, ECO:0000269|PubMed:29691540, ECO:0000269|PubMed:31199070}; | arginine catabolic process to ornithine [GO:0019547]; urea cycle [GO:0000050] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | arginase activity [GO:0004053]; identical protein binding [GO:0042802]; manganese ion binding [GO:0030145] | PF00491; | 3.40.800.10; | Arginase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682, ChEBI:CHEBI:46911; EC=3.5.3.1; Evidence={ECO:0000255|RuleBase:RU361159, ECO:0000269|PubMed:15053781, ECO:0000269|PubMed:29691540, ECO:0000269|PubMed:31199070}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=137 mM for L-arginine (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:15053781}; | PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1. {ECO:0000305|PubMed:15053781}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5-9. {ECO:0000269|PubMed:29691540}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius (PubMed:29691540). Active up to 70 degrees Celsius (PubMed:29691540). {ECO:0000269|PubMed:29691540}; | FUNCTION: Catalyzes the hydrolysis of L-arginine into urea and L-ornithine, which is a precursor for polyamine biosynthesis (PubMed:15053781, PubMed:29691540, PubMed:31199070). By depleting host L-arginine, a substrate for nitric oxide synthase (NOS), prevents the production of nitric oxide (NO) by host activated macrophages, and thus allows the parasite to evade host immune response (PubMed:15053781). {ECO:0000269|PubMed:15053781, ECO:0000269|PubMed:29691540, ECO:0000269|PubMed:31199070}. | Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM) |
C4LVG4 | ACTP_ENTH1 | MAGIQLADEVTSVYNDFKLSHKYRYIVFKMNDGMTEVVVEKTAEKNATYDDFLKDLPEKSARYAVYDLEYDTPEGLRQKIIFYLWTPEGCKIREKMLYSATKATIKQALVGLSAEIQATDAGELNLDEVIAKVKTISK | null | null | actin filament depolymerization [GO:0030042]; actin filament fragmentation [GO:0030043]; actin filament severing [GO:0051014] | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; phagocytic cup [GO:0001891]; pseudopodium [GO:0031143] | actin filament binding [GO:0051015] | PF00241; | 3.40.20.10; | Actin-binding proteins ADF family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:35281106}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:35281106}. Cell membrane {ECO:0000269|PubMed:35281106}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000269|PubMed:35281106}. Cell projection, phagocytic cup {ECO:0000269|PubMed:35281106}. Cell projection, pseudopodium {ECO:0000269|PubMed:35281106}. Note=During phagocytosis, localizes to the tip of the actin-rich phagocytic cup until the closure of the phagocytic cup. {ECO:0000269|PubMed:35281106}. | null | null | null | null | null | FUNCTION: Actin-binding protein that severs actin filaments. {ECO:0000269|PubMed:35281106}. | Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM) |
C4LZC2 | PFP_ENTH1 | MSLSALHKYRLQYKPVLPKHIADIDNITIEEGAKTQSAVNQKELSELFKHTYGLPICNIVAGKNADIHRVIRCGFILSGGPAAGGHNVVAGLFDGLMKGNKENKLYGFRCGAGGILSNDYIEITAELVDKHRNTGGFDLVGSGRTKIETEEQFATAFKHITALKLNAMVVVGGDDSNTNAALLAEYFAAHGSDCVFVGVPKTIDGDLKNQYIETSFGFDTACKTYSELIGNIQRDAISSRKYWHFIKVMGRSASHIALEAALETQPTYCIISEEVEDKKMTVSQIASEIADIVIERHKKGLNFGVVLIPEGLVEFIPEVKALIKELNNLLAHKKEEYSKITEFSAQKAFVCENISESCAATFKNLPDNIAKQLLLDRDPHGNVNVSAIETESFVSGIVKAEIVKRGIKVPFTPVHHFFGYEGRCAFPSNFDSTYCYALGYTAFILLALKKTGQICCISGLQKPAEEWICGGVPLTIMMNMEQRNGEMKPVIKKALVEIEGKPFKFYQSKRAQWASAEDFVFPGAIQYFGPSEVCDQPTKTLLLEQN | 2.7.1.90 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03185, ECO:0000269|PubMed:178659, ECO:0000269|PubMed:4372217}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_03185, ECO:0000269|PubMed:178659, ECO:0000269|PubMed:4372217}; | fructose 6-phosphate metabolic process [GO:0006002]; photosynthesis [GO:0015979]; response to glucose [GO:0009749] | cytosol [GO:0005829] | 6-phosphofructokinase activity [GO:0003872]; ATP binding [GO:0005524]; diphosphate-fructose-6-phosphate 1-phosphotransferase activity [GO:0047334]; metal ion binding [GO:0046872]; phosphofructokinase activity [GO:0008443] | PF00365; | 3.40.50.450;3.40.50.460; | Phosphofructokinase type A (PFKA) family, PPi-dependent PFK group II subfamily, Clade 'Long' sub-subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03185}. | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613, ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90; Evidence={ECO:0000255|HAMAP-Rule:MF_03185, ECO:0000269|PubMed:178659, ECO:0000269|PubMed:4372217, ECO:0000269|PubMed:9445396}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14 uM for diphosphate {ECO:0000269|PubMed:178659, ECO:0000269|PubMed:4372217, ECO:0000269|PubMed:9445396}; KM=800 uM for phosphate {ECO:0000269|PubMed:178659, ECO:0000269|PubMed:4372217, ECO:0000269|PubMed:9445396}; KM=38 uM for fructose 6-phosphate {ECO:0000269|PubMed:178659, ECO:0000269|PubMed:4372217, ECO:0000269|PubMed:9445396}; KM=18 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:178659, ECO:0000269|PubMed:4372217, ECO:0000269|PubMed:9445396}; | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_03185}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.4-7.2. {ECO:0000269|PubMed:178659, ECO:0000269|PubMed:4372217, ECO:0000269|PubMed:9445396}; | null | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. {ECO:0000255|HAMAP-Rule:MF_03185, ECO:0000269|PubMed:11262402, ECO:0000269|PubMed:178659, ECO:0000269|PubMed:4372217, ECO:0000269|PubMed:9445396}. | Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM) |
C4M1P9 | DBR1_ENTH1 | MATEQIQHIAIVGCVHGKYREMYRQLSEYEKSTGKEISFVICTGDMQTLRYEADLVYLKVPPKYKQMGDFHLYYEGKEKAPYLTLFIGGNHESSNVLLHLYNGGFVCFNMYYLGVCSCININGLRIVGVSGIYKSFDEKKPYTYPPSPNDVVSLFHTRNYVIQMLSNLSQSSQIDISLSHDWPQGIVMKGNYKQLYRFQPGFKKDGASLGSPINKVILNTLKPKYWISGHMHCEYHAEEGPTHFIALGKIGYKNAISYLDLPLKQKTDLEYDKDWVCNLIMTWPAFSNKAQFPDLSYSISELLSKRTKELDKKIIELWEKYIGLKIIYDSDTFDIQFTSRRFYIEKIYNELNIN | 3.1.4.- | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:27930312}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:27930312, ECO:0000269|PubMed:28504306}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:25123664, ECO:0000269|PubMed:28504306}; Note=Binds 2 divalent metal cations per subunit. {ECO:0000269|PubMed:27930312, ECO:0000269|PubMed:28504306}; | mRNA splicing, via spliceosome [GO:0000398]; RNA splicing, via transesterification reactions [GO:0000375] | nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | iron ion binding [GO:0005506]; manganese ion binding [GO:0030145]; RNA binding [GO:0003723]; RNA lariat debranching enzyme activity [GO:0008419]; zinc ion binding [GO:0008270] | PF20890;PF00149; | 3.60.21.10; | Lariat debranching enzyme family | null | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:30023353}. Note=In trophozoites, appears to localize to the cytoplasmic side of the nucleus concentrating on the basal region. {ECO:0000269|PubMed:30023353}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 uM for 10-mer branched RNA AK88 (when bound to Fe(2+) and Zn(2+)) {ECO:0000269|PubMed:27930312}; Note=kcat is 2 sec(-1) with 0-mer branched RNA AK88 as substrate (when bound to Fe(2+) and Zn(2+)). {ECO:0000269|PubMed:27930312}; | null | null | null | FUNCTION: Cleaves the 2'-5' phosphodiester linkage at the branch point of excised lariat intron RNA and converts them into linear molecules that can be subsequently degraded, thereby facilitating ribonucleotide turnover. {ECO:0000269|PubMed:25123664, ECO:0000269|PubMed:27930312, ECO:0000269|PubMed:28504306}. | Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM) |
C4M4P4 | COAA_ENTH1 | MSGFDLSEVAGPVAEVIDDKNEEVEFVVFGVQTQPNKLVVDAKGKGGLEEVKAALKEDALQFAYYRTISGDEESKRVKFVFISWAGEGIKKPKLRAVMSILKGDVKNVINNFHIELHATSLDDLVEDEIAAKIKKAGGADYSFNTTSN | null | null | neuron projection morphogenesis [GO:0048812]; positive regulation of axon extension [GO:0045773]; postsynaptic actin cytoskeleton organization [GO:0098974]; regulation of actin filament polymerization [GO:0030833] | actin filament [GO:0005884]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; lamellipodium [GO:0030027]; phagocytic cup [GO:0001891]; pseudopodium [GO:0031143]; site of polarized growth [GO:0030427] | actin filament binding [GO:0051015] | PF00241; | 3.40.20.10; | Actin-binding proteins ADF family, Coactosin subfamily | PTM: Phosphorylation at Ser-147 appears not to affect its binding to actin; however, it may regulate phagocytosis and motility. {ECO:0000269|PubMed:32753489}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31095644}. Cell projection, phagocytic cup {ECO:0000269|PubMed:31095644}. Cell projection, pseudopodium {ECO:0000269|PubMed:25210743}. Cell membrane {ECO:0000269|PubMed:25210743}; Peripheral membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:25210743}. Note=During phagocytosis, recruited to the phagocytic cup by 14-3-3 protein 3 (PubMed:31095644). Co-localizes with F-actin in pseudopods and in phagocytic cups. Localizes to the site of phagocytosis until scission of the cups occurs (PubMed:25210743). {ECO:0000269|PubMed:25210743, ECO:0000269|PubMed:31095644}. | null | null | null | null | null | FUNCTION: Actin-binding protein which is involved in F-actin stabilization (PubMed:25210743). May play a role during phagocytosis and pseudopod formation by contributing to the maintenance of F-actin (PubMed:25210743). {ECO:0000269|PubMed:25210743}. | Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM) |
C4M4T9 | DPNP_ENTH1 | MSFDKELALALEIVQVSCKITTSVAEHTLTDQTQIKNDKSPVTVGDYSVQAYVNKKIHETFPEDQIVAEEDTKTIPEDIFAKVCKHVQIYSDMKDDEIRKSIDLGNSTGGKGRHWVLDPIDGTLGFLRREQYAVCLAFMIDGDIKVGVLGCPNFEGGLIVAAQKGCGAKMFSVNDIKNGKDIHVSTTPKTSDMCFCESVEVSHTDQSRSKTITERLQVTKPPVRMDSQCKYMAIASGRADVYLRLPRNLSYQEKIWDHAAGYLIVKEAGGKVTDIYGNDLDFSLGRTLCNNHGIVASNGILHEETVNVVKDVLSDLK | 3.1.3.57; 3.1.3.7 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25004978}; Note=Binds 3 Mg(2+) ions per subunit (PubMed:25004978). Active also with Mn(2+) or Co(2+) (PubMed:25004978). {ECO:0000269|PubMed:25004978}; | phosphatidylinositol phosphate biosynthetic process [GO:0046854]; sulfate assimilation [GO:0000103] | cytoplasm [GO:0005737] | 3'(2'),5'-bisphosphate nucleotidase activity [GO:0008441]; inositol-1,4-bisphosphate 1-phosphatase activity [GO:0004441]; magnesium ion binding [GO:0000287]; nucleotide binding [GO:0000166] | PF00459; | 3.40.190.80;3.30.540.10; | Inositol monophosphatase superfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25004978}. | CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate; Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7; Evidence={ECO:0000269|PubMed:25004978}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate; Xref=Rhea:RHEA:15553, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58282, ChEBI:CHEBI:58469; EC=3.1.3.57; Evidence={ECO:0000269|PubMed:25004978}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7 (PubMed:25004978). Active between pH 6-8.5 (PubMed:25004978). {ECO:0000269|PubMed:25004978}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius (PubMed:25004978). Active between 10-60 degrees Celsius (PubMed:25004978). {ECO:0000269|PubMed:25004978}; | FUNCTION: Phosphatase that converts 3'-phosphoadenosine 5'-phosphate (PAP) to AMP (PubMed:25004978). Is also able to hydrolyze inositol 1,4-bisphosphate but with less efficiency (PubMed:25004978). {ECO:0000269|PubMed:25004978}. | Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM) |
C4M633 | INPP_ENTH1 | MQTSLFEFANVLITAVKEASYSISKFKEEVEIKYKSDGSEVTQVDTQSQQIIFSIIKNKYPTINIIGEEDVENGIPDNQLPTITQLSFGSLENKIININDIIIYVDPLDGTDCYTHKQYDSVCVLVGVTYKGKPMIGIVSKPFYNNEITFAIENYISSISLQPLNDKIIFVCSKKNDIQHLIKSFPDPYEVKYKGGSGAKMMAIIHQEADIYYHPLIQSCTWDTLAAQVILEAQGGIVCDIYGNPLCYPSSKKESMRHKKGVLCLSPRAKKYLPYMLSISKTILL | 3.1.3.57; 3.1.3.7 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25372691}; Note=Binds 3 Mg(2+) per subunit. {ECO:0000269|PubMed:25372691}; | 3'-phosphoadenosine 5'-phosphosulfate metabolic process [GO:0050427]; sulfate assimilation [GO:0000103] | cytoplasm [GO:0005737] | 3'(2'),5'-bisphosphate nucleotidase activity [GO:0008441]; inositol-1,4-bisphosphate 1-phosphatase activity [GO:0004441]; magnesium ion binding [GO:0000287] | PF00459; | 3.40.190.80;3.30.540.10; | Inositol monophosphatase superfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25372691}. | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate; Xref=Rhea:RHEA:15553, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58282, ChEBI:CHEBI:58469; EC=3.1.3.57; Evidence={ECO:0000269|PubMed:25372691}; CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate; Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7; Evidence={ECO:0000269|PubMed:25372691}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 (with 3'(2')-phosphoadenosine 5'-phosphate (PAP) as substrate). {ECO:0000269|PubMed:25372691}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius (with 3'(2')-phosphoadenosine 5'-phosphate (PAP) as substrate) (PubMed:25372691). Active between 30 and 80 degrees Celsius (PubMed:25372691). {ECO:0000269|PubMed:25372691}; | FUNCTION: Catalyzes the hydrolysis of the 1-position phosphate from inositol 1,4-bisphosphate (PubMed:25372691). Is also able to convert 3'(2')-phosphoadenosine 5'-phosphate (PAP) to AMP but with less efficiency (PubMed:25372691). {ECO:0000269|PubMed:25372691}. | Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM) |
C4N147 | FABP1_DORPE | MAADLAGKWILESSENFDDYMKAVGVGMVMRKMANAATPTQEIKIDGDSWSIKTSTTFKTTDISFTIGQEFDETTGDGRKIKTTCKIDGNAMIQDQKGSPDSILSREVKDGKMHMILKVNDVVCTRIYKRVD | null | null | fatty acid transport [GO:0015908] | cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634] | fatty acid binding [GO:0005504] | PF00061; | 2.40.128.20; | Calycin superfamily, Fatty-acid binding protein (FABP) family | PTM: Phosphorylated (PubMed:19168028, PubMed:19386360, PubMed:23224877). Phosphorylation may result in the release of the bound fatty acid (PubMed:22948910). {ECO:0000269|PubMed:19168028, ECO:0000269|PubMed:19386360, ECO:0000269|PubMed:22948910, ECO:0000269|PubMed:23224877}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19168028}. Membrane {ECO:0000269|PubMed:24269200}; Peripheral membrane protein {ECO:0000269|PubMed:24269200}. | null | null | null | null | null | FUNCTION: Binds and may transport fatty acids such as palmitoleate (PubMed:22948910). Also binds poly-phosphoinositides including phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), and phosphatidic acid (PubMed:19168028). When phosphorylated, stimulates the activity of optic nerve Na(+)/Ca(2+) exchanger (PubMed:19168028, PubMed:19386360, PubMed:22948910). {ECO:0000269|PubMed:19168028, ECO:0000269|PubMed:19386360, ECO:0000269|PubMed:22948910}. | Doryteuthis pealeii (Longfin inshore squid) (Loligo pealeii) |
C4QX80 | PSD1_KOMPG | MPNRSFGVFPSVIYETRLGLSHQMRRPIGQPLSKLSQVSQPNQILQRNYQYKFPRIPRPKRNVLYYTFKRPQLSSATILRTVPSKIRNFSSRAKSKVKSSGRRRKFMSRWLALSSISVVLYGVVNKIKHKGIQRNSSLEPDENHSVKPNSWTLYAYSTLPLKAISRVWGQFNSFELPIWLRSPSYKFYAYVFGVNLDEVAEPDLSKFRNLGEFFYRTIKPETRPIDIDAEMVSPCDGKVLKFGIIENGEIEQVKGMTYSINALLGQQKLAAPVHRINYQLDDDDVVRRHEEFARLNGISYTIDDIIGGRGENIHHSYMNQGDQSLRKSSASQVYEVSNDIAKKSSFDKQLYFAVIYLAPGDYHRFHSPSNWVTTLRRHFVGELFSVAPFFQKTLQNLFILNERVALLGYWKHGFFSMIPVGATNVGSIKINFDKDLVTNSIYESDSYAQTSFPSSDTSSCREEDESTPLIKRSSSRTKKVIKNSCYEATYANASKILRGQPLSKGQEIGGFKLGSTVVLVFEAPKTFHFTLAENMKLKMGQRIGELR | 4.1.1.65 | COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP-Rule:MF_03208}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-Rule:MF_03208}; | mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; phosphatidylcholine biosynthetic process [GO:0006656]; phosphatidylethanolamine biosynthetic process [GO:0006646]; positive regulation of mitochondrial fusion [GO:0010636]; positive regulation of protein processing [GO:0010954]; protein autoprocessing [GO:0016540] | mitochondrial inner membrane [GO:0005743] | phosphatidylserine decarboxylase activity [GO:0004609] | PF02666; | null | Phosphatidylserine decarboxylase family, PSD-B subfamily, Eukaryotic type I sub-subfamily | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase. {ECO:0000255|HAMAP-Rule:MF_03208}. | SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 beta chain]: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:19656201}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}.; SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 alpha chain]: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:19656201}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}. Note=Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain. {ECO:0000255|HAMAP-Rule:MF_03208}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262, ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP-Rule:MF_03208}; | null | PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2. {ECO:0000255|HAMAP-Rule:MF_03208}. | null | null | FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:19656201}. | Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris) |
C4R4G9 | OXDA_KOMPG | MTDSKYVIIGAGISGLYTAWSLIDKGTGPSDIKVVAEFLPGDQSTLYTSPWAGGNFSLITSTDERSMKFDKFTYTNLHRIQELLGGPECGLDMLPSTEMFEQELDHAKLDSISQYLKEYRPMTKEEMPEGVVSGVKFLTWNFNCPLFLANFQKHLAAIGVTFERSKIDHISSVFSPSVDAVFNCTGIGAASLGGVKDENVFPTRGQVVVVRAPHIRENRFRWRPDSDTYVIPRPFSDGSIVMGGFFQEGNWSGNTYGYETEDILKRGLELYPEIGKRNELKIIREAAGLRPSRKGGVRIEVEHFDQVNGKDRYIVHNYGASGYGYQSGLGMANEATDMYFEAAK | 1.4.3.3 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|PIRSR:PIRSR000189-1}; | aspartate catabolic process [GO:0006533]; D-alanine metabolic process [GO:0046436]; D-amino acid catabolic process [GO:0019478]; D-amino acid metabolic process [GO:0046416]; D-valine metabolic process [GO:1902114]; nitrogen utilization [GO:0019740] | peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777] | D-amino-acid oxidase activity [GO:0003884]; D-aspartate oxidase activity [GO:0008445]; FAD binding [GO:0071949] | PF01266; | 3.30.9.10;3.40.50.720; | DAMOX/DASOX family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:20550580}. | CATALYTIC ACTIVITY: Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59871; EC=1.4.3.3; Evidence={ECO:0000305|PubMed:20550580}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21817; Evidence={ECO:0000305|PubMed:20550580}; CATALYTIC ACTIVITY: Reaction=D-alanine + H2O + O2 = H2O2 + NH4(+) + pyruvate; Xref=Rhea:RHEA:22688, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57416; Evidence={ECO:0000305|PubMed:20550580}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22689; Evidence={ECO:0000305|PubMed:20550580}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.6. {ECO:0000269|PubMed:20550580}; | null | FUNCTION: Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity (PubMed:20550580). Enables the organism to utilize D-amino acids as a source of nutrients (PubMed:20550580). Enables the organism to utilize D-alanine as a source of nitrogen (PubMed:20550580). {ECO:0000269|PubMed:20550580}. | Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris) |
C4R4R8 | ARO1_KOMPG | MSGLIEKVSILRNDSIHVGYNMSSHIVDEILTKKASSTYVLITDSNIVKMGHLQTFVDEFNRLIPSKRPGSRILTYVVPPGEANKNRATKAAIEDYLLEKGCTRDTFILAIGGGVIGDMIGYVAATFMRGVRFVQIPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPDYVFVDVAFLETLPEREFINGMAEVVKTAAIWNEQEFSRLETYSKRFLKVIRDRRVDDSVDLTSLKEHIIKLVLESIKVKAEVVTLDEREGGLRNLLNFGHSIGHAIEAILTPQALHGECVSIGAVLEAELSRYLGILSPVAVSRLYKCFAAYGLPVSIADKLVQKRTNGKKCPVDVLLQKMAIDKKNDGSKKKVVLLSKIGKCYEPKASYVNDEDLRFVLTDEVLVKDFNSAPSTAVVVPPGSKSISNRALILAALGKGECKIKNLLHSDDTEHMLNAVAALKGADISFDDNGETVVVTGNGGNFTATDAEIYLGNAGTASRFLTSVASIVKPDSNTTHVILTGNARMQERPIGPLVDALRTNGSDIEYLNREGSLPLKIKSGNGLKGGRIELAATISSQYVSSVLMCAPYASEPVTLSLVGGKPISLLYVDMTIAMMKSFGIEVTKSTTEPYTYHVPQGHYVNPAEYVIESDASSATYPLAFAAMNGTQVTIPNIGSSSLQGDARFAVDVLKPMGCKVEQTATSTTVQGPTKGTLKPLPLVDMEPMTDAFLTASVVAAIANDTNQSTSIVGISNQRVKECNRIEAMITQLAKFGVRAKELEDGIEVFGIDYHHLKTPSDGVYTYDDHRVAMSLSLLAGLAESPVLIQERHCTGKTWPGWWDILHTTFNVELDGHEAVVETTTAKANEDKSIIVIGMRAAGKSTLSHVIAQTLKGFKVVDLDDVFVEKYGDIREFIKENSWELFREKEAMIAKEAFKNYSKNTVISTGGGIVETEASRKLLKQQMKDGHIVLHLHRDIEETVVFLSQDKTRPAYVDEINQVWERRKNLYKECSNYFFFSPHCQTEREFFTLKKTFSKFINRITGGAVPSIPNGRSAFVCLTYEDLAPVSSKLTRVTNGCDAVELRVDLLKQHDSHFISNQIGILRNQTSVPILFTIRTKSQGGRFPDDSYEDIERLLNLAIKLGVEYVDLELSLPESLLDSVASKRQFTKIIGSHHDFSGTVKWNNVEWENKYLLALKLNVDIIKFVGTATSLNDNWELEHFRSLHTDKPFIGINMGPLGKVSRVFNTILTPVTHKDLPSSAAPGQLTLKEINEYFGQFGGSSRKKFYIVGKPISHSKSPELHKTFYDEFGLSHTFDKFETDDAAKVFNDLVKGNDELGGCAVTIPLKIDMLKYVNELTDSAKSIGALNTIIPIGDGRFIGDNTDWIGIRDSLHQAGCEIAPESSVGLVVGGGGTSRAAVYALHQMGCSKIYMLNRTPSKLSEIKNHFPSNYNIHIVDSLDAIDEDDKLDAAVSTVPGDKPLDDQLISLLKKLLEKKRGHAVLLEAAYKPRETPIMALAFSRGWKVVPGSKMLVNQGIEQFYKWTGYQFSSHIDL | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris) |
C4Y9D5 | ARO1_CLAL4 | MSQVEKVSILGSDSIHVGYGIQDHIVEETLTNLKSSTYVIITDSNMEATAPYQTLSSKFEAGLKEFRPESRLFYYAVSPGENNKSRETKAQVEDFLLQKGCTRDTVIIAVGGGVVGDMIGFVAATFMRGVRVVQVPTTLLAMVDSSIGGKTAVDTPLGKNFVGAFHQPKYVFVDVSFLTTLPTRQFINGMAEVVKTAAIWNEEEFTRLENFAKTFIAVVTSDNIDLATIKDDLVKTVLESIRVKADVVSADEKESSLRNLLNFGHTIGHAIEAIVTPQALHGECVAVGMVKEAELARYWGVLSPVAVARLVNCIAAYNLPTSVGDKIFVQRIGHKRHFIQINTLLEKMAIDKKNDGSKIRTVILEAIGKCYQLKAHEVSKQDLSFVLTDETLVHPFQEETTPKENVVIPPGSKSISNRALILAALGKGTVRIKNLLHSDDTKHMLAAVAALKGAEISTEDNGDTIVVKGNGGNFITCDEQLYLGNAGTASRFLTTVASLVNVNEQSNDYTVLTGNARMQERPVGPLVNALRANGSEIEYLNNEGSLPLKIKAGKGLKGGRVELAATISSQYVSSILMCAPYAEKEVTLALVGGKPISQLYIDMTIAMMKDFGISVTRDPHEEHTYHIPKGVYSNPGVYEVESDASSATYPLAFAAMTGTSCTVPNIGSSSLQGDARFAVDVLKPMGCTVEQTSTSTTVRGPSKGSLKPLTHVDMEPMTDAFLTASVVAAIANSSVPTQITGIANQRVKECNRILAMVDELAKFGVRAEELPDGIEIYGIDYKNLKVPSLENRGVCTYDDHRVAMSFSLLAGMCPEPVLITERSCTGKTWPGWWDVLHTKFGVELEGYEEPKDLNDPALLVNKEVNGDKSIVVIGMRAAGKSTLSRWIADFMGFELIDLDTVFEQTHGDIREYIKANGWGRFRELEAGIMKEYLTKCSSRHVISTGGGIVESEESRDILKSYTKTGGIVLHLHRDLDETIVFLSSDTTRPAYVSEIKDVWARREKWYHECSNYHFYSSHCGTEEEFKKLRHSFVSYLKTITGAGLSPVPKGRSFVLSLACSDLNDIAENLEDIVAGCEAIELRVDLLKDYSPSFVADQTAVLRKFVNLPIIYTIRTKGQGGNFPDEDVQALEQLSYLGIKLGVDYLDVQLSNSEKFVKSIIEKKAFTKIIATHIDLAGLPWTRAEWDNKYNQGISLNADVIQLVGFAHAFQDNIDLEQFRANHTITPLIAFNAGEHGKLSRVLNRTLTPVTSELLSNVSGNGQLTVGEINRCFSEIGGLSRRNFYIVGNPISHSRSPQLHTAGYEKLNLPHRFSKFETDYAQKVYEEVMTKPGFGGLAVTIPLKLDIMKYVSELSESAKIIGAVNTVTPLDGQPGKFYGDNTDWYGITQSFVRHGVPSFGNSSVNGMVVGGGGTSRAAAFALHQMGCKKIYMVNRTTSKLHEIKSSLPSDFNIEVLETVDQVEAADPVSLVVSCVPADKPLDSELLNKVERILYHGKNQEKRSFVPTLLDAAYKPRVTPIMKIAEEKFGWAVVPGVEMLVNQGVLQFKVHTVFTPPYKNVYEAVVDDNV | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF01488;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae) |
C4YMW2 | THI5_CANAW | MSTNKITFLLNWEAAPYHIPVYLANIKGYFKDENLDIAILEPSNPSDVTELVGSGKVDMGLKAMVHTLAAKARGFPVTSIGSLLDEPFTGICYLEGSGITSDFQSLKGKRIGYVGEFGKIQVDELTKHYGMTPDDYVAVRCGMNVAKYILEGTIDCGIGIECIQQVELEEALKEQGKDSNDAKMLRIDKLAELGCCCFCTILYIANDKFIAENPQAVKKFLKAIKRATDYMLAHPREAWAEYGNFKPTMQTDLNTKKFQRCYAYFSESLYNVHRDWRKVNNYGKRLDILPENYVPNYTNEYLSWPEPKEVDDPEKAQDLMLKHQEECKTCGGYKRLVLA | 2.-.-.- | COFACTOR: Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000269|PubMed:22568620}; | thiamine biosynthetic process [GO:0009228]; thiamine diphosphate biosynthetic process [GO:0009229] | null | 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity from histidine and PLP [GO:0106344]; metal ion binding [GO:0046872] | PF09084; | 3.40.190.10; | NMT1/THI5 family | null | null | CATALYTIC ACTIVITY: Reaction=2 Fe(3+) + 4 H2O + L-histidyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase] + N(6)-(pyridoxal phosphate)-L-lysyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase] = (2S)-2-amino-5-hydroxy-4-oxopentanoyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase] + 3-oxopropanoate + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 2 Fe(2+) + 2 H(+) + L-lysyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase]; Xref=Rhea:RHEA:65756, Rhea:RHEA-COMP:16892, Rhea:RHEA-COMP:16893, Rhea:RHEA-COMP:16894, Rhea:RHEA-COMP:16895, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:29969, ChEBI:CHEBI:29979, ChEBI:CHEBI:33190, ChEBI:CHEBI:58354, ChEBI:CHEBI:143915, ChEBI:CHEBI:157692; Evidence={ECO:0000269|PubMed:22568620}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65757; Evidence={ECO:0000269|PubMed:22568620}; | null | PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. {ECO:0000305|PubMed:22568620}. | null | null | FUNCTION: Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. {ECO:0000269|PubMed:22568620}. | Candida albicans (strain WO-1) (Yeast) |
C4ZQN7 | HCHA_ECOBW | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKLLTGDSPFAANALGKLAAQEMLAAYAG | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790]; zinc ion binding [GO:0008270] | null | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. | Escherichia coli (strain K12 / MC4100 / BW2952) |
C5C7X8 | GYRB_MICLC | MVDAMPENPAEEPTAASAAPNPEAVPDAVGQPEAPVKDRKVPGEYGASAITVLEGLEAVRKRPGMYIGSTGPRGLHHLVYEVVDNSVDEALAGYATGIDVTLQADGGVRVADDGRGIPVDLHPTEGRPTVEVVMTILHAGGKFGGGGYAVSGGLHGVGISVVNALSRRVDTEVRRQGHVWRMSFADGGVPQGELVKGEATDATGTVQTFYPDAEIFDSIEFDYETLRARFQQMAFLNKGLRITLTDERVQESNEVVDDEIAGEGAAGEDVAENGLAEDAEQEPQRRSVTYLYENGLLDYVQHLNSAKKVEYVHDDVIAFEAEDFSDGRSMAVEVAMQWTSAYSESVHTYANTINTHEGGTHEEGFRAALTSLVNRYAREKEILKPKEDNLSGEDIREGLTAVISVKLSEPQFEGQTKTKLGNSEARGFVSKAVTDHLGDWFERNPGPAKEIIRKAIMASHARLAARKARDNARRKSPLESFGMPGKLADCSSKDPERCEVYIVEGDSAGGSAKQGRNPETQAILPLRGKILNVERARLDKALGNAEIQSMITAFGTNIGEEFDISKLRYHKIVLMADADVDGQHITTLLLTVLFRYMRPLIEAGHVFLAQPPLYRIKWSNAPHDYVFSDEERDAAVEAGLAKGWRYPKDNGVQRYKGLGEMNYQELWDTTMDPEHRTLLQVTMEDAAAADAVFSMLMGEDVESRRTFIQQNAKDIRFLDV | 5.6.2.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01898, ECO:0000269|PubMed:276855}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+). {ECO:0000255|HAMAP-Rule:MF_01898}; | DNA topological change [GO:0006265]; DNA-templated DNA replication [GO:0006261] | chromosome [GO:0005694]; cytoplasm [GO:0005737] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA negative supercoiling activity [GO:0034335]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]; metal ion binding [GO:0046872] | PF00204;PF00986;PF02518;PF01751; | 3.30.230.10;3.40.50.670;3.30.565.10; | Type II topoisomerase GyrB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01898, ECO:0000269|PubMed:276855}. | CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01898, ECO:0000269|PubMed:153201, ECO:0000269|PubMed:276855}; | null | null | null | null | FUNCTION: A type II topoisomerase that negatively supercoils DNA in an ATP-dependent manner (PubMed:276855). About 140 bp of DNA wraps around gyrase in the presence or absence of ATP, when ATP is added negative supercoils are made (PubMed:153201). {ECO:0000269|PubMed:153201, ECO:0000269|PubMed:276855}.; FUNCTION: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. {ECO:0000255|HAMAP-Rule:MF_01898}. | Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus) |
C5C7X9 | GYRA_MICLC | MSDETTPQTPDEPVEGAPIPGTPQTGLDIEVEHYVLPEGAADKVEPVDLESEMKRSYLDYAMAVIVGRALPDVRDGLKPVHRRVLYAMYDGGYRPDRAFNKSARVVGDVMGNYHPHGDTAIYDALVRLIQDWVQRYPLALGQGNFGSPGNDGAAAQRYTETKMAPLAMEMVRDIDEDTVDMQDNYDGKQQEPVVLPARYPNLLVNGSSGIAVGMATNIPPHNMREVAAGVQWYLEHPEATREELLEALLARVHGPDFPTGAQILGRKGIEEVYRTGRGPITMRAVVNVEEIQGRTCLVVTELPYMTNPDNLAAKIAEMVRDGKISGIADMRDETSGRTGQRLVIVLKRDAVAKVVLNNLYKHTELQSNFSANMLALVDGVPRTLSLDGFVHHWVKHQIDVIVRRTAFRKRKAEERAHILRGLLKALDMLDEVIATIRRSASADVAREALKELLDIDDVQAQAILQMQLRQLAALESQKIQDEYDDLMAKIAEYNRILESPQRQREVISEELAEIVAKHGDDRRTEIMAGFDGDMSIEDLIPEEEMVVSITRGGYVKRTRIDQYRSQARGGKGVRGATLRGDDVVEHFLTVSTHHWLLFFTNFGRVYRIKTYELLEAGRDAKGQHVANLLAFQPDERIAQIQPLVDYGRAPYLVLATRGGLVKKTPLLDYDTNRTAGLIAIKLREGDELVSARVVSPDDDLILISHKGQSLRFTATDEALRPMGRATSGVTGMKFRDDDSLLTMDVVEEDGYVFTVTDGGFAKRTHVDEYRLQNRGGLGIKVAKLVDDRGELAGGLVVREDQEVLVVMASGKVVRSAVAGVPAKGRDTMGVIFAKPDKRDRIVAVTLNNEQEMEAKADAEAEAGPDVPLDADIDPTDPVAAPEDALTQDAGEGADGGEQ | 5.6.2.2 | null | DNA topological change [GO:0006265]; DNA-templated DNA replication [GO:0006261] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex [GO:0009330] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA negative supercoiling activity [GO:0034335]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918] | PF03989;PF00521; | 3.30.1360.40;2.120.10.90;3.90.199.10;1.10.268.10; | Type II topoisomerase GyrA/ParC subunit family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897, ECO:0000269|PubMed:276855}. | CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01897, ECO:0000269|PubMed:153201, ECO:0000269|PubMed:276855}; | null | null | null | null | FUNCTION: A type II topoisomerase that negatively supercoils DNA in an ATP-dependent manner (PubMed:276855). About 140 bp of DNA wraps around gyrase in the presence or absence of ATP, when ATP is added negative supercoils are made (PubMed:153201). {ECO:0000269|PubMed:153201, ECO:0000269|PubMed:276855}.; FUNCTION: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. {ECO:0000255|HAMAP-Rule:MF_01897}. | Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus) |
C5DN02 | ARO1_LACTC | MKVELSKVPILGKDVVHVGFDIADHIVDTIFQSCPSSTYVVINDTNVEKIPHYVDLCGELQAKLKSGSRILQYSVKPGEAHKTREQKAAIEDYLLSEGCTRDTVIIAVGGGVIGDMIGYVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAVDTPLGKNFIGAFWQPQFVFVDIKWLETLPKREFINGIAEVIKTACIWNAEEFARLEENADLFLQVVNGSKTTQVSVQGQVHELSLTNIDAMLEHVYRLVLESIKVKTHVVSSDEREAGLRNLLNFGHTIGHAYEAILTPQALHGECVSIGMIKEAELSRYLNILSPTQVARLTKILAAYGLPISPDQKWFKDLTLNKKTPLDVLLKKMSIDKKNDGSKKKAVLLETIGKCYGTSAHVVSDEDIRFVLTDETLVYPFKTLENGQEKTIVPPGSKSISNRALILAALGEGTCKIKNLLHSDDTKHMLHAVQQLKGATITWEDNGETVVLKGHGGSTLQATAEPLYLGNAGTASRFLTSVAALVNSTSSQKSVVLTGNARMQERPIGPLVDSLRENGISIDYLNKEKSLPLKINTDSNFKGGRIELAATVSSQYVSSILMCAPYAEEPVTLALVGGKPISKLYIDMTIKMMEKFGIYVKASTEEPNTYHIPKGHYVNPPEYVIESDASSATYPLAYAAMTGTTVTVPNIGFESLQGDARFARDVLKPMGCSVTQTETSTTVTGPPVGGLKPLKHVDMEPMTDAFLTACVVAAVAHDGKEGSRNTTTIEGIANQRVKECNRILAMVDELAKFGVEANELPDGIQVHGLSSIDKLKVPEAIHSYDDHRVAMSFSLLAGMVGATKDALSEPVRILERSCTGKTWPGWWDVLHTQLGAKLDGSEPLQSAVKKNSNSSIVIIGMRAAGKTTVSSWCANALGFKFLDLDTVFEEQYKKGSVKEFVAEHGWDAFRATETKIFEESVKKYGEGYVLSTGGGIVEGAASRKSLKQFASQGGIVLHLHRDIDETIKFLNSDPTRPAYNEDIRNVWERREEWYKECANFTFYAPHCTSSTQFNQLRKTFETFIRTISGKREVKIPTNRSSFVCLTFDDLAAHKEKIPDITAGCSAVELRVDQLKSYDLDFVAKQLSILRLASSSLPIIFTIRTKSQGGQFPDDDKSTLGSLLSLALEVGVEFVDMELTLSSELQYSLVNNKRNTKIIGSHHDFDAKFDWNDSEWENRYNQALSLDVDVVKFVGTAKDFEDNLKLEQFRLQHTAKPLIAINMTDVGKMSRVLNTVLTPVTSSLLPSASAPGQLTLSQINEIYTLLGGFSAKNFYVVGSPISHSRSPVLHNTGYKILGLPHKFEKFETSSASEVKDKLLSKCKLGGLAVTIPLKLDIMEFMDELSESAKLIGAVNTVIPLGDGKFKGDNTDWLGIYNSFLANGVPENVRGNSGFVIGAGGTSRAAVYALHQLGCSDIHLVNRTVEKPHDLKKSFPSEYNLHVLEDSQQAEGISGSVALAVSCVPADKPLDDNLLARVRAVLAKAQGTSFKPTLLEAAYKPAVTPMMKTASDEFSWHIIPGSQMLVHQGVAQFQLWTGFRAPFNAIYSAVTEEQA | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF18317;PF01488;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284) (Yeast) (Kluyveromyces thermotolerans) |
C5DRQ1 | MMM1_ZYGRC | MESNYTGMDGNWALNGTVSVGNGTLISVDEFLHNALPMHLQALFQDGNSQGPLLTMEDLEKAIEFKRASQELVNDNVLAPDGLFVELLRQQEKTLPRLISATSNTQGSFSSWSFAQGLIVGQVSVVLVLIFFIKFFIFSDSSTKTNPNPAKNSSSTNSLSGLSSESRSFISPHFFTSIMNRKGNEQAESNDDENERSRQIDDILEKTYYNVDTHPAESLDWFNVLIGQTIQQLREEAWKKDNIVYSLNAFIERKAQELPSYLDSIKITELDIGHDFPIFSNCRIQYSPNSNGRKLEAKIDIDLNDRLAVGIETRLLLNYPKPLTASLPINVTVSIIRFQACLTVSLTKAEEFVPTSPESVDEDDNDGYFLMFSFAPEYRMEFETQSLIGARSKLENIPKIGSLVEYQIKKWFVERCVEPRFQFIKLPSVWPRSKNTREGKADVDESEPGRETHY | null | null | mitochondrial genome maintenance [GO:0000002]; mitochondrion-endoplasmic reticulum membrane tethering [GO:1990456]; phospholipid transport [GO:0015914]; protein insertion into mitochondrial outer membrane [GO:0045040] | endoplasmic reticulum membrane [GO:0005789]; ERMES complex [GO:0032865] | lipid binding [GO:0008289] | PF10296; | null | MMM1 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03103}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_03103}. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids. {ECO:0000255|HAMAP-Rule:MF_03103}. | null | null | null | null | null | FUNCTION: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria (By similarity). Preferentially binds to glycerophospholipids such as phosphatidylcholoine (PC), phosphatidic acid (PA), phosphatidylglycerol (PG), and phosphatidylserine (PS), but not to phosphatidylethanolamine (PE) (PubMed:29078410). The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids (By similarity). {ECO:0000255|HAMAP-Rule:MF_03103, ECO:0000269|PubMed:29078410}. | Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568 / NRRL Y-229) (Candida mogii) |
C5DVG6 | ARO1_ZYGRC | MVKFEKVPILGKESIHVGYDIHTDMVQTIINDCRSSTYVVVNDTNLSKVPYCQDFVQELRSSLPEGSRLLQYAVKPGEANKTRSTKADIEDYLLSKGCTRDTVIIAIGGGIIGDMVGFVAATFMRGVRVVQVPTSLLAMVDSSIGGKTAVDTPLGKNFIGAFWQPQFVLVDVKWLETLPRREFINGMAEVIKTACIWNGLEFERLESNAELFLRVVNGSKVIKVNGLSTGEVNDIHYTNIEAMLEHTFKLVLESIKVKAEVVSSDERESSLRNLLNFGHSVGHAYEAILTPQALHGECVSIGMIKEAELSRYLGILSPTQVSRLTKILAAYGLPISPEEKWFKDLTLQKKTPLDVLLQKMSIDKKNDGSKKKVVILESIGKCYGKSAHYVNDEDLKFVLTDETLVYPFSNIPQEQAKTIVPPGSKSISNRALILAALGKGTCKIKNLLHSDDTKHMLTAVQELKGASITWEDNGETVVLEGHGGETLTASADPLYLGNAGTASRFLTTLAALVNSSSKQDYVVLTGNARMQQRPIGPLVDSLRTNGTKIDYLKSEGSLPLKIYTSTPFKGGRIELAATVSSQYVSSVLMCAPYAENPVTLALVGGKPISQLYVDMTIKMMEKFGIKVEVSTTEPYTYHIPKGQYTNPPEYIIESDASSATYPLAFAAMTGTTVTVPNIGYESLQGDARFAIEVLRPMGCKVEQTANSTTVTGPPTGSLRPLKHVDMEPMTDAFLTASVVAAVAHDNDTDSANVTTIEGIANQRVKECNRIEAMSTELAKFGVATKELPDGIQIHGINSLDLLQLPSNSTGPIGIESYDDHRVAMSLSLLAGMVNYSKSHPAADIKPVRILERRCTGKTWPGWWDVLHTELGAHLDGAEPLGYLSGKKTKRSVVLIGMRAAGKSTLGRWCSQILGYELCDLDVLFEKQYAKGTVKDFVAEHGWDKFREAEANLFKETVEQYGDGGYVFSAGGGLVENEVSREHLKKYASDGGVVLHLHRDIEETIVFLQSDPTRPAYMEEIRDVWERREKWYNECSNFAFLAPHCSNEKEFQHLRKSFANYITAITGNREVQVPNKRSAFVCLTFGDLTEKASVLPSIVRGCDAVELRVDHLAKYDSQFVSKQLSTLRTATNDLPIVFTLRTKKQGGKFPDEDYTGMARLFDVALKACVEYIDLELTLPIDVQYKVSNTKGYTKIIGSHHDFGAKYPWKDPEWENRYNQALSLDVDVIKFVGTATKFEDNLALERFREEHKSKPLIAINMGEIGKISRVLNPILTPITSEHLPNSSAPGQLTLAQINKIFASMGGITSKKFFVVGNPVSHSRSPVLHNTGYKLNGLPHHFDRFETDSAQVVKETLLDGEPSLGGLAVTIPLKLDIMKYMNQLTDAARVIGAMNTVIPLGNHHFKGDNTDWIGIKHSLTSNGVPEKVSNVAGLVIGAGGTSRAAIYSLHNLGCHRIFVINRTVSKSIELRDSFPQEYNVVAAETTQQIDHLNEHIGIAVSCVPADKDLDTELLAKLERFLHKGKHNSFVPTLLEAAYKPDVTPVMKLAHDKYQWQVVPGRELLVHQGVAQFEIWTGAKAPFQEIFNAVTRD | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF18317;PF01488;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568 / NRRL Y-229) (Candida mogii) |
C5FQ73 | ARO1_ARTOC | MEQPTTIQILGRDSIVADFGIWRRHVARDLLETLSSSTYILISDTNIAPLYVPEFERAFEEAAAEKSPKPRLLTYKIAPGESSKGRETKAEIEDWMLSCQPPCGRDTVLIALGGGVIGDLAGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPEKIYLDMEFLNTLPQREFTNGMAEVIKTAAISSETTFAELEQNADAIAAALKTENTPERSRFSGIQEILKRTILASARFKADVVSKDEREGGLRNLLNFGHSIGHAIEAILAPQILHGECVAIGMIKEVELARYLGILKGAAVARLAKCLTRYGLPTSLKDARIRRLSAGKKCPVDKLIAFMAVDKKNDGPMKKVVLLSAIGRTHEQKASVVSNEELKVVLAPSIEVLPGIPKPLNVTCTPPGSKSISNRALVLAALGSGVCRIRNLLHSDDTEVMLNALEALGAATFSWEEEGEVLVVNGKGGKLEASAHELYLGNAGTASRFLTTVATLSNEKDDVSHNILTGNARMKQRPIGDLVDALKSNGVSVDYLEQQGSLPLKVPACGGFKGGAIELAAKVSSQYVSSLLMCAPYAKEKVTLKLVGGKPISETYIAMTAAMMKSFGIDVEKSTTEEYTYHIQQGQYKNPPEYIIESDASSATYPLAIAAMSGTTCTIPNIGSKSLQGDARFAVDVLRPMGCDVKQTNSSTTVTGPTNGALKPIANVDMEPMTDAFLTASVLAAVANDKSGNTTRIYGIANQRVKECNRIKAMKDELAKFGVTCREHDDGIEIDGIDSSELKVPVNGVHCYDDHRVAMSFSVLAAAAASQPTLILEKECVGKTWPAWWDALAQTFKVKLDGKELVNDNVVDIQKSTKSIASIFIIGMRGAGKTTSGYSISKALNRPFIDLDTELENVEGMPIPEIIKQKGWEGFRDAELALLKRMMAEKPTGYIFACGGGIVETKEARDLLINYHKNKGNVFLIMRNIKKVIEFLEIDKTRPAYIEDMMGVWLRREPWYQECSNLQYYSHHSERSELDAALQGFTRFLNVVMGNTDHLALLKKKDHSFFVSLTLPDLQLSADILRAATFGSDAIELRVDLLKDPSSTSGVPSVGYVAEQMSFLRSHASQPLIFTIRTKAQGGQFPDDAVDKALELYKLAIRMGSEFVDLELSFPNDLLHAVTEMKGFSKIIASHHDVNSQLSWSNGSWIQYYNKALQHGDIIKLIGVAKTFEDNMALQQFKSWAEKSYPVPIIAINMGNKGRLSRILNRFMTPVSHPALPFKAAPGQVSAKDIRQALTLMGELDAKKFALFGKPISASRSPALHNALFTQAGFPHDYGLLETDKAENVEKFIRSDDFGGASVTIPLKEQIMGLLDEISPEAKIIGAVNTIVPITVSGRPPRLIGYNTDWQGMARCLKDAGAICSNNGESALTIGSGGTARAAIYSLHSMGYSPIYLVGRTPSNLSKLASSFPAEYNIQVVQDIKSVQAAPKVAISTIPGDQELENPLPELITQIMEKGQDSSRECILLDMAYKPDVTTMARLASPAGWKIIKGLEVLVAQGIYQFEHWTGLMPIYEDARAAVMNI | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF18317;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis) |
C5G6D7 | CABC2_BACT4 | MLILSFLCPAFLNAQIVTDERMFSFEEPQLPACITGVQSQLGISGAHYKDGKHSLEWTFEPNGRLELRKDLKFEKKDPTGKDLYLSAFIVWIYNEQPQDAAIEFEFLKDGRKCASFPFGINFKGWRAAWVCYERDMQGTPEEGMNELRIVAPDAKGRLFIDHLITATKVDARQQTADLQVPFVNAGTTNHWLVLYKHSLLKPDIELTPVSDKQRQEMKLLEKRFRDMIYTKGKVTEKEAETIRKKYDLYQITYKDGQVSGVPVFMVRASEAYERMIPDWDKDMLTKMGIEMRAYFDLMKRIAVAYNNSEAGSPIRKEMRRKFLAMYDHITDQGVAYGSCWGNIHHYGYSVRGLYPAYFLMKDVLREEGKLLEAERTLRWYAITNEVYPKPEGNGIDMDSFNTQTTGRIASILMMEDTPEKLQYLKSFSRWIDYGCRPAPGLAGSFKVDGGAFHHRNNYPAYAVGGLDGATNMIYLFSRTSLAVSELAHRTVKDVLLAMRFYCNKLNFPLSMSGRHPDGKGKLVPMHYAIMAIAGTPDGKGDFDKEMASAYLRLVSSDSSSAEQAPEYMPKVSNAQERKIAKRLVENGFRAEPDPQGNLSLGYGCVSVQRRENWSAVARGHSRYLWAAEHYLGHNLYGRYLAHGSLQILTAPPGQTVTPTTSGWQQEGFDWNRIPGVTSIHLPLDLLKANVLNVDTFSGMEEMLYSDEAFAGGLSQGKMNGNFGMKLHEHDKYNGTHRARKSFHFIDGMIVCLGSDIENTNMDYPTETTIFQLAVTDKAAHDYWKNNAGEGKVWMDHLGTGYYVPVAARFEKNFPQYSRMQDTGKETKGDWVSLIIDHGKAPKAGSYEYAILPGTDRKTMTAFAKKPAYSVLQQDRNAHILESPSDRITSYVLFETPQSLLPGGLLQRTDTSCLVMVRKESADKVLLTVAQPDLALYRGPSDEAFDKDGKRMERSIYSRPWIDNESGEIPVTVTLKGRWKVVETPYCKVVSEDKKQTVLRFLCKDGASYEVELEK | 4.2.2.21 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954}; Note=Divalent metal cation. Requires divalent metal cation for binding of dermatan sulfate substrate, whereas it is not necessary for the binding of chondroitin sulfate substrates. Prefers Ca(2+) or Mg(2+), binding 1 ion per subunit. {ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954}; | carbohydrate metabolic process [GO:0005975]; dermatan sulfate catabolic process [GO:0030209]; glycosaminoglycan catabolic process [GO:0006027] | extracellular region [GO:0005576]; periplasmic space [GO:0042597] | calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; chondroitin-sulfate-ABC endolyase activity [GO:0034000]; chondroitin-sulfate-ABC exolyase activity [GO:0034001]; magnesium ion binding [GO:0000287] | PF02278;PF09093;PF09092; | 2.70.98.10;1.50.10.100;2.60.120.430;2.60.220.10; | Polysaccharide lyase 8 family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:Q8A2I1}. | CATALYTIC ACTIVITY: Reaction=Exolytic removal of Delta(4)-unsaturated disaccharide residues from the non-reducing ends of both polymeric chondroitin/dermatan sulfates and their oligosaccharide fragments.; EC=4.2.2.21; Evidence={ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=67 uM for chondroitin 4-sulfate from porcine or bovine trachea (at 37 degrees Celsius and pH 7.6) {ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954}; KM=33 uM for chondroitin 6-sulfate from shark cartilage (at 37 degrees Celsius and pH 7.6) {ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954}; KM=61 uM for dermatan sulfate from porcine intestinal mucosa (at 37 degrees Celsius and pH 7.6) {ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954}; Vmax=77.6 umol/min/mg enzyme with chondroitin 4-sulfate from bovine trachea as substrate (at 37 degrees Celsius and in 50 mM phosphate at pH 7.6) {ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954}; Vmax=47.4 umol/min/mg enzyme with chondroitin 6-sulfate from shark cartilage as substrate (at 37 degrees Celsius and in 50 mM phosphate at pH 7.6) {ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954}; Vmax=14.4 umol/min/mg enzyme with chondroitin 2,6-sulfate from skate cartilage as substrate (at 37 degrees Celsius and in 50 mM phosphate at pH 7.6) {ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954}; Vmax=28.5 umol/min/mg enzyme with chondroitin 4,6-sulfate from squid cartilage as substrate (at 37 degrees Celsius and in 50 mM phosphate at pH 7.6) {ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954}; Vmax=9.1 umol/min/mg enzyme with dermatan sulfate from porcine intestinal mucosa as substrate (at 37 degrees Celsius and in 50 mM phosphate at pH 7.6) {ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954}; Note=kcat is 15792 min(-1) with chondroitin 4-sulfate from porcine or bovine trachea as substrate. kcat is 10404 min(-1) with chondroitin 6-sulfate from shark cartilage as substrate. kcat is 2307 min(-1) with dermatan sulfate from porcine intestinal mucosa as substrate. {ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.6. Decreased activity at pH values below 7.0 and above 8.0. The activity against chondroitin 6-sulfate remains higher than with other substrates at low pH. At pH 6.5 the enzyme exhibits almost 60% of its maximal activity against chondroitin 6-sulfate, only 20% activity against chondroitin 4-sulfate and no measurable activity against dermatan sulfate. In contrast, at pH of 8.5 about 30% of enzyme's maximal activity against all substrates is displayed. {ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. No significant reduction in activity at temperatures in the range of 25-40 degrees Celsius. At 50 degrees Celsius, activity of 45% for dermatan sulfate, 60% for chondroitin 4-sulfate and 75% for chondroitin 6-sulfate is detected. Thermal denaturation curve is bimodal with two consecutive thermal denaturation midpoints (Tm) corresponding to 44 and 50 degrees Celsius, respectively. {ECO:0000269|PubMed:18227125, ECO:0000269|PubMed:18512954}; | FUNCTION: Broad-specificity glycosaminoglycan lyase, which acts in an exolytic fashion degrading chondroitin sulfates and dermatan sulfate to yield only disaccharide products. Has a preference for chondroitin 4-sulfate over chondroitin 6-sulfate. Has extremely low activity against hyaluronic acid. Is not active against acharan sulfate, heparin or heparan sulfate. {ECO:0000269|PubMed:18512954}. | Bacteroides thetaiotaomicron |
C5G8R4 | ARO1_AJEDR | MGVPTKISILGRESIVADFGIWRNYVAKDLLNSCSSSTYILISDTNITPLYLDGFQKSFDDAAANLSPKPRLLTYEIPPGESSKSRETKAGIEDWMLTRQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALEDDAEIILAAVKSKNTPERPRFSGIEETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVAIGMVKEAELARHLGILNNVSVSRISKCLASYGLPTSLKDERIRKLTADKHCSVEQLITYMGVDKKNDGPKKKVVLLSAIGRTHEPRASTVSNEEIQIVLAPSIEVSPGVPKNLNVTCTPPGSKSISNRALVLAALGSGTCRLKNLLHSDDTEVMLNALERLGAATFSWENEGEVLVVNGKGGKMKASPDELYLGNAGTASRFLTTVATLAQKSSVDSSVLTGNARMKQRPIGDLVDALAANGAGVEYLENSGSLPLKIAASGGFAGGEINLAAKVSSQYVSSLLMCAPYAKKPVTLRLVGGKPISQTYIDMTTTMMRSFGIDVKKSETEEHTYHIPLGFYISPAEYIVESDASSSTYPLAVAAITGTSCTVPNIGSKSLQGDARFAVEVLRPMGCTVDQKDFSTTVTGPANGILRPLPNVDMEPMTDAFLTASVLAAVARGGGSNHTTRIFGIANQRVKECNRIKAMKDELAKFGVTCREHDDGLEIDGIDRSTLRHPSDGVYCYDDHRVAMSFSVLSLVAPQPTLILEKECVGKTWPGWWDSLAQTFKVKLDGKEVEKKTGRGGIVHLDKPAASIFIIGMRGAGKTTSGVWVSKALQRPFIDLDDELERTEGMTIPEIIKQRGWEGFREAELSLLRRVMTEKPTRYIFACGGGIVETPEARKLLIQYHKTKGNVILVMRDIKEIMDFLKIDKTRPAYVEDMMSVWLRRKPWYQECSNVQYFSRLTGLDGMAQVLGGFNRFLKVITGQVDSLAQMRSKENTFFVSLTLPDLAPAAPILKEVTLGSDAVELRVDLLKDPQSDSEIPSVDYVAEQISVLRSRTSVPLVFTIRTKAQGGRFPDDAYDAALQLYRLAIRMGSEFVDLEISFPEQLLRTVTEMKGFSKIIASHHDPKGELSWANGSWIQFYNKALQYGDVIKLVGVARSLDDNASLKKFKTWAEEKHDVPIIAINMGDKGQLSRMLNGFMTPVSHPSLPFKAAPGQLSAREIRKGLSLIGEIKSKKFAVIGNPVSASRSPAMHNALFRQMGLPHIYGTLETEDPEIVKKFIRSPDFGGASITIPLKLDIMPLLDEIAPEAVSIGAVNTIVCAPPAPDDQSQAPRLIGRNTDWQGMVRCLSDAGAYPAATPTTTSAGLVIGGGGTARAAIFALQSMGYSPIYVVGRSPDKLSSMTSTFAPDHDIRILEDVKALESLPTVAIGTIPGDKPIEPHMREILCELFDLCEKANSDAEQARGISTKRILLEMAYKPSVTSLMQLASDSGWTVLPGLEALVAQGVYQCEYWTDITPVYEDARNAVMGVQPKDDDIST | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces dermatitidis) |
C5H429 | DBR2_ARTAN | MSENPPTLFSAYKMGNFNLSHRVVLAPMTRCRAINAIPNEALVEYYRQRSTAGGFLITEGTMISPSSAGFPHVPGIFTKEQVEGWKKVVDAAHKEGAVIFCQLWHVGRASHQVYQPGGAAPISSTSKPISKKWEILLPDATYGTYPEPRPLAANEILEVVEDYRVAAINAIEAGFDGIEIHGAHGYLLDQFMKDGINDRTDEYGGSLENRCKFILQVVQAVSAAIATDRVLIRISPAIDHTDAMDSDPRSLGLAVIERLNKLQFKLGSRLAYLHVTQPRYTADGHGQTEAGANGSEEEVAQLMKTWRGAYVGTFICCGGYTRELGLQAVAQGDADLVAFGRYFVSNPDLVLRLKLNAPLNRYDRATFYTHDPVVGYTDYPSLDKGSLL | 1.3.1.92 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; | jasmonic acid biosynthetic process [GO:0009695]; oxylipin biosynthetic process [GO:0031408] | cytosol [GO:0005829]; peroxisome [GO:0005777] | 12-oxophytodienoate reductase activity [GO:0016629]; FMN binding [GO:0010181]; oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor [GO:0016628] | PF00724; | 3.20.20.70; | NADH:flavin oxidoreductase/NADH oxidase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18495659}. | CATALYTIC ACTIVITY: Reaction=(11R)-dihydroartemisinic aldehyde + NADP(+) = (+)-artemisinic aldehyde + H(+) + NADPH; Xref=Rhea:RHEA:32883, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64688, ChEBI:CHEBI:64691; EC=1.3.1.92; Evidence={ECO:0000269|PubMed:18495659}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:32885; Evidence={ECO:0000269|PubMed:18495659}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=19 uM for artemisinic aldehyde {ECO:0000269|PubMed:18495659}; KM=790 uM for 2-cyclohexen-1-one {ECO:0000269|PubMed:18495659}; KM=650 uM for (+)-carvone {ECO:0000269|PubMed:18495659}; KM=95 uM for NADPH {ECO:0000269|PubMed:18495659}; KM=770 uM for NADH {ECO:0000269|PubMed:18495659}; Note=kcat is 2.6 sec(-1) with artemisinic aldehyde as substrate. kcat is 1.8 sec(-1) with 2-cyclohexen-1-one as substrate. kcat is 0.86 sec(-1) with (+)-carvone as substrate. kcat is 1.3 sec(-1) for the NADH-dependent reduction of artemisinic aldehyde. {ECO:0000269|PubMed:18495659}; | PATHWAY: Sesquiterpene biosynthesis. {ECO:0000303|PubMed:30468448}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:18495659}; | null | FUNCTION: Involved in the biosynthesis of the antimalarial endoperoxide artemisinin (PubMed:18495659, PubMed:27488942). Catalyzes the double bond reduction of artemisinic aldehyde to produce (11R)-dihydroartemisinic aldehyde (PubMed:18495659). Also able to reduce 2-cyclohexen-1-one into cyclohexanone to a lesser extent (PubMed:18495659). {ECO:0000269|PubMed:18495659, ECO:0000303|PubMed:27488942}. | Artemisia annua (Sweet wormwood) |
C5H431 | POLG_WSLV | MATKGMNKSRARSRGVNMVAARVKNLAVKVKNKTKQSARGLRGFLLFLVAQIFWARKLTPQVKRLWRMVDKVQGLRILKNIRNIVTNLMKGLAGRKKKRSLTVPLVLLLIPLIAYSATVTRQRGLGLLLNVTFADVGKTYEVEGGNCSVNTLDAGKWCEDYVEYECVTLSEGEEPDDLDCWCYGVDNVRVTYGRCKSGGSRRSRRSAVITPHVDKGLTTRQEKWLPTKIGEQQLQKVEKWIMRNPLYALGAVALAYFVGTSNVQRVVIAILLLGIGPAYSTHCLGIPKRDFIRGLDGNTWVSVVLEQGSCVTLIADNKPSVDIWLSSIVVDTPTLVRKVCYASSVTGSKATGACPTMGDAHMSEEGNEEWECKRSYSDRGWGNGCGLFGKGSIVACAKFSCTHEMEVYQIDATKIEYTISAQVHSGAKKDDWENHTKLVTFVPTTGTSTVAFTGYGNFGLECHVQMMVDLSNSYLVKVGTDAWLVNKQWVHDITLPWQSGTGGHWRDKHFMVDFEEPHAVTMKALVLGSQEGALRTALSGAMVVELNSNRYSLKGGHVTCKAYMNNLILKGSTYSMCKRGMSFAKQPVETDHGTAVMQIKVTTGAPCRIPVIAADSMAGTENRGSVITTNPIAASNNDEVLVEISPPFGESYIIVGNGDDKLTYHWQRSGSTIGNLFTETMKGAQRMIITGEHSWDFGSTGGFFSSIAKAVHTVFGAAFHAIFGGLSWITKILIGGLLIWLGLNSRSSSMSMGFICIGALLLVLATGVGAEVGCSLSWKQREMKCGDGVFVFKDSDDWFSKYQYIPEDPKTMATLIHQAHQDGLCGLSSVSDLEHRMWYSRVDEINAILDENEVDLTVVVQESDAVYLRGSHAFPRPKSELKYGWKTWGKNIIFNPSRKNGTFIIDGKSKAECPFNKRVWNSIRVEEFGTGVYQTRVFMRPEFDYTKLCDTGTLGAAVKGSVSAHGDPMFWMESEEINGTWMITTLEALNYRECEWPSSHTLDGAKVVESDMFMPRSLAGPISKHNHIPGYKVQTSGPWHNVPLEIKREECPGTTVVVDEKCDDRAKSVRSTTDSGKIIPEWCCRSCTMPPVSFWGPDGCWYSMEVRPKHTNEAHLVKSWVVASKGDVDPFSLGLLMLFLCSDMFLMKRFSMRAILVGSLVMLGAMTLGSLSYLDLLRYAITVGMYMAEINSGGDVTHLALLAVFRVRAGFVSMLALKRLWSPREGFVATCGIVMVQLALGDILSTDIMEWLNAAGMAVLIIKSIVEPKRCNAVLPLLCLLTPLTVAEIQRAVMFVCSIVIFVTVWQTDSVSTRKTIPLVALTVCSFFKWTSPFLGIVCYLAFTRLPQRSWPLGETMAAVGLVGVLAGMGLKDMNGMLGPVAVGGVLLIVMSLSGKVDGLVIKKVADVTWDEDAEISGASHRYDVEQTDTGEFKLRNEEPAPWIQVAVLTIAILSAATHPACLAVVTIGWFAWQKTTTRSGVLWDIPTVVPPEEVSYLEDGVYTINQNSFLGLAQKGVGVVKDGVFHTMWHVTRGAFLLHAGKRMTPSWANVKEDLISYGGGWKLDAKWDGSEEVQLIAVSPGKVPVNVQTTPSVFQLKNGKEIGAVNLDYPSGTSGSPILNKNGDVIGLYGNGILIGNNTYVSAIAQSDSVEEGGTEQLQDIPTMLKKGMLTVLDFHPGAGKTRIYLPQILKECEKLKLKTLVLAPTRVVLSEMREAMPKMSIKYHTQAFSNTSTGKEIIDAMCHATLTHRMLEPTRVTNWEVVIMDEAHFMDPASIAARGWAAHRSRARECATIFMSATPPGTSNEFPESNGMIEDVKKDVPSEPWTKGHEWILEDRRPTAWFLPSIRIANSIANCLRKADRTVVVLNRKTFEKEYPTIKSKKPDFILATDIAEMGANLKVERVIDCRTAYKPILVDDATKVMVKGPLRISASSAAQRRGRIGRDPNRDTDTYIYGDSTTEDNGHYVCWTEGSMLLDNMEIRNGMIAPLYGVEGTKTTTSPGETRLREDQRKVFRELVKRLDMPVWFSWQVAKAGLKVQDRSWCFDGEDDNTLLNDNGEPILARSPGGAKKPLKPRWVDTRVCSDNASLIDFIKFAEGRRSASGILLGLQGFPEFLSGKMREAIDTVTVLYTSDTGSRAYKHALAMMPEATTIFLLVMLAIICTSGVIMFFLAPKGLSRMSMAMMTMLVSAYLMSLGGMNPVQISCVMLVFFIFMVVLIPEPGTQRSTYDNQIIYLLVGVLSLILLVAANEMELLEKTKRDIFGAVVVEEAKRWTFPEFDLRPGAAWTVYVGLVTPGNPMLHHWIKIDYGNISLSGITQNAQVLGLMDRGIPFIKMNMSVVILLLSAWNGITLLPLFAGMGAAALHWGFILPGLRAQAAKAAQKRVYHGVAKNPVVDGNPTVDIDDAPGMPAMYEKKLALVILLALSILNLVLTRTPFATAEMVVLGSAAVGPLIEGDTNAYWNGPIAVAFSGLMRGNYYATIGLAYNGWLAKQTRRGKAAGVTLGEVWKRQLNMLGKQEFERYKVPDITEVDRTAARRYLKEGRTDVGISVSRGAAKIRWLHERGYLRITGRVLDLGCGRGGWSYYAAAQKEVMSVKGYTLGIEGHEKPIHMQTLGWNIVKFKDKSNVFTMPTEPSDTLLCDIGESSSNPLVERDRTMKVLENFERWKHVNTENFCVKVLAPYHPDVIEKLERLQLRFGGGIVRVPFSRNSTHEMYYISGARNNITHMVNTTSRSLLRRMTRPSGKAIIEGDVFLPTGTRSVASEAGTIDHEALKLRVDQIKAEYSKTWTHDSNHPYRTWHYLGSYLCKATGSSSSMINGIVKMLSMPWDKFESVTLLAMTDTTPFGQQRVFKEKVDTKAPPPPPGTRAIMRVVNAWLFQHLARKKKPRICTREEFVAKVRSHAALGAYLEEQDKWKSASEAVQDPQFWKLVDDERKLHLQGQCRTCVYNMMGKREKKPSEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWVSRENSGGGVEGTGLQYLGYILKELGGKTGGNMYADDTAGWDTRITEEDLEDEQEILKYMDEKHKKLAWAVTELAYKNKVVKVMRPGPGGLTFMDIISRRDQRGSGQVVTYALNTVTNLKVQLIRMAEAEHVITNFDVDTVSQKTLQDLRCWLDRFGADRLSRMAVSGDDCVVKPIDDQFADALTHLNSMSKIRKDIDDWKPSQGWASWEDVPFCSHHFHELILKDGRSIIAPCRDQDELIGRARVSPGNGWMIRETACLSKAYAQMWLLMYFHRRDLRVMANAINSTVPVDWVPTGRTTWSIHGKGEWMTTEDMLQVWNRVWIEDNPHQTDKTPITEWRDIPYLPKSIDKTCNSLVGTTQRASWARDIKHTVHRIRGLVGNEKYTDYLATMDRFRELDESGPGEVLW | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | null | fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity [GO:0039564]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049] | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; virion membrane [GO:0055036] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization activity [GO:0046983]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198] | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;2.40.10.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. The nascent capsid protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature capsid protein C is cleaved at a site upstream of this hydrophobic domain by NS3. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. Non-structural protein 2A-alpha, a C-terminally truncated form of non-structural protein 2A, results from partial cleavage by NS3. Specific enzymatic cleavages in vivo yield mature proteins peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site. {ECO:0000250|UniProtKB:P03314}.; PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.; PTM: [Envelope protein E]: N-glycosylated. {ECO:0000250|UniProtKB:P17763}.; PTM: [Non-structural protein 1]: N-glycosylated. The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.; PTM: Polyubiquitinated; ubiquitination is probably mediated by host TRIM23 and is prerequisite for NS5-STAT2 interaction. NS5 is not ISGylated or sumoylated. {ECO:0000250|UniProtKB:P03314}.; PTM: [Serine protease NS3]: Acetylated by host KAT5. Acetylation modulates NS3 RNA-binding and unwinding activities and plays an important positive role for viral replication. {ECO:0000250|UniProtKB:Q32ZE1}.; PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization. {ECO:0000250|UniProtKB:P17763}. | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.; SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.; SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-ProRule:PRU00860}.; SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}. | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; 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}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; 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=3.6.4.13; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; | null | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}.; FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}.; FUNCTION: [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (By similarity). {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-ProRule:PRU00860}.; FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition. {ECO:0000250|UniProtKB:P03314}. | Wesselsbron virus (WSLV) |
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