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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A0PC02 | UCP1_OCHDA | MVGTTATDVAPTMGVKIFSAGVAACLADVITFPLDTAKVRLQIQGECQTTSGIRYKGVLGTITTLAKTEGPLKLYSGLPAGLQRQISFASLRIGLYDTVQEFWGGEEATPSLRSKICAGLTTGGVAVFIGQPTEVVKVRLQAQSHLHGLKPRYTGTYNAYRIIATTESLSTLWKGTTPNLLRNIIINCTELVTYDLMKGALVRNDILADDVPCHLLSALIAGFCTTLLSSPVDVVKTRFINSPQGQYTSVPSCAMSMLTKEGPTAFFKGFAPSFLRLASWNVIMFVCFEKLKRELMKSRQTVDCAT | null | null | adaptive thermogenesis [GO:1990845]; cellular response to fatty acid [GO:0071398]; cellular response to hormone stimulus [GO:0032870]; cellular response to reactive oxygen species [GO:0034614]; mitochondrial transmembrane transport [GO:1990542]; proton transmembrane transport [GO:1902600]; regulation of reactive oxygen species biosynthetic process [GO:1903426]; response to cold [GO:0009409]; response to nutrient levels [GO:0031667]; response to temperature stimulus [GO:0009266] | mitochondrial inner membrane [GO:0005743] | cardiolipin binding [GO:1901612]; long-chain fatty acid binding [GO:0036041]; oxidative phosphorylation uncoupler activity [GO:0017077]; purine ribonucleotide binding [GO:0032555] | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | PTM: May undergo sulfenylation upon cold exposure. May increase the sensitivity of UCP1 thermogenic function to the activation by noradrenaline probably through structural effects. {ECO:0000250|UniProtKB:P12242}.; PTM: May undergo ubiquitin-mediated proteasomal degradation. {ECO:0000250|UniProtKB:P04633}. | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P12242}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P04633}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:P25874}; | null | null | null | null | FUNCTION: Mitochondrial protein responsible for thermogenic respiration, a specialized capacity of brown adipose tissue and beige fat that participates in non-shivering adaptive thermogenesis to temperature and diet variations and more generally to the regulation of energy balance. Functions as a long-chain fatty acid/LCFA and proton symporter, simultaneously transporting one LCFA and one proton through the inner mitochondrial membrane. However, LCFAs remaining associated with the transporter via their hydrophobic tails, it results in an apparent transport of protons activated by LCFAs. Thereby, dissipates the mitochondrial proton gradient and converts the energy of substrate oxydation into heat instead of ATP. Regulates the production of reactive oxygen species/ROS by mitochondria. {ECO:0000250|UniProtKB:P12242}. | Ochotona dauurica (Daurian pika) |
A0PJ25 | GLYC_BCNVU | MGQLVSFIGEIPAIVHEALNVALIAVSIIAIMKGLINIWKSGLFQLIMFLILAGRSCSISIGHHLELQHFIINSTSLLPSMPTLCRINATNSLIRGPFSAQWGLDIFIGDLTILVNPEPGSKTKRMTATNITGCFPNNEDPDSVAQVLSWFFRGVHHDFHLDPTILCDESVTVFRIQMNLTERMYCDRIVSKLARLFGSFGDYCSKVGKKLVIIRNVTWSNQCHEDHVGSMQLILQNAHNQVMRFRKLQNFFSWSLVDSAGNSMPGGYCLEKWMLVASELKCFGNTAVAKCNINHDSEFCDMLRLFDYNKKAIVNLQDKTKAQLDSLIDAVNSLISDNLITKNKIRELMNIPYCNYTKFWYVNHTGLNVHSLPKCWHVRNGSYLNESDFRNEWIIESDHLVSEILAKEYEERQKRTPLSLVDLCFWSTLFYTASIFLHLLHIPTHRHIIGEGCPKPHRLTSDSLCACGFFQLKGRPTRWARIP | null | null | fusion of virus membrane with host endosome membrane [GO:0039654]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; virion attachment to host cell [GO:0019062] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | metal ion binding [GO:0046872] | PF00798; | 6.10.140.1590;2.20.28.180; | Arenaviridae GPC protein family | PTM: Specific enzymatic cleavages in vivo yield mature proteins. GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1. Only cleaved glycoprotein is incorporated into virions. {ECO:0000255|HAMAP-Rule:MF_04084}.; PTM: The SSP remains stably associated with the GP complex following cleavage by signal peptidase and plays crucial roles in the trafficking of GP through the secretory pathway. {ECO:0000255|HAMAP-Rule:MF_04084}. | SUBCELLULAR LOCATION: [Glycoprotein G1]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}.; SUBCELLULAR LOCATION: [Glycoprotein G2]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Note=Binding to the stable signal peptide masks endogenous ER localization signals in the cytoplasmic domain of G2 to ensure that only the fully assembled, tripartite GP complex is transported for virion assembly. {ECO:0000255|HAMAP-Rule:MF_04084}.; SUBCELLULAR LOCATION: [Stable signal peptide]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. | null | null | null | null | null | FUNCTION: [Glycoprotein G2]: Class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced upon acidification in the endosome. {ECO:0000255|HAMAP-Rule:MF_04084}.; FUNCTION: Stable signal peptide (SSP): cleaved and functions as a signal peptide. In addition, it is also retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion. {ECO:0000255|HAMAP-Rule:MF_04084}.; FUNCTION: [Glycoprotein G1]: Interacts with the host receptor. {ECO:0000255|HAMAP-Rule:MF_04084}. | Bear Canyon mammarenavirus (isolate Mouse/United States/AV A0070039/2000) (BCNV) |
A0PJK1 | SC5AA_HUMAN | MAANSTSDLHTPGTQLSVADIIVITVYFALNVAVGIWSSCRASRNTVNGYFLAGRDMTWWPIGASLFASSEGSGLFIGLAGSGAAGGLAVAGFEWNATYVLLALAWVFVPIYISSEIVTLPEYIQKRYGGQRIRMYLSVLSLLLSVFTKISLDLYAGALFVHICLGWNFYLSTILTLGITALYTIAGGLAAVIYTDALQTLIMVVGAVILTIKAFDQIGGYGQLEAAYAQAIPSRTIANTTCHLPRTDAMHMFRDPHTGDLPWTGMTFGLTIMATWYWCTDQVIVQRSLSARDLNHAKAGSILASYLKMLPMGLIIMPGMISRALFPDDVGCVVPSECLRACGAEVGCSNIAYPKLVMELMPIGLRGLMIAVMLAALMSSLTSIFNSSSTLFTMDIWRRLRPRSGERELLLVGRLVIVALIGVSVAWIPVLQDSNSGQLFIYMQSVTSSLAPPVTAVFVLGVFWRRANEQGAFWGLIAGLVVGATRLVLEFLNPAPPCGEPDTRPAVLGSIHYLHFAVALFALSGAVVVAGSLLTPPPQSVQIENLTWWTLAQDVPLGTKAGDGQTPQKHAFWARVCGFNAILLMCVNIFFYAYFA | null | null | hexose transmembrane transport [GO:0008645] | apical plasma membrane [GO:0016324]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886] | fructose:sodium symporter activity [GO:0140930]; glucose:sodium symporter activity [GO:0005412]; mannose:sodium symporter activity [GO:0140929]; solute:sodium symporter activity [GO:0015370] | PF00474; | 1.20.1730.10; | Sodium:solute symporter (SSF) (TC 2.A.21) family | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q5SWY8}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: [Isoform 1]: Reaction=D-mannose(out) + Na(+)(out) = D-mannose(in) + Na(+)(in); Xref=Rhea:RHEA:72907, ChEBI:CHEBI:4208, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:22212718, ECO:0000269|PubMed:24573086}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72908; Evidence={ECO:0000250|UniProtKB:Q5SWY8}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=D-fructopyranose(out) + Na(+)(out) = D-fructopyranose(in) + Na(+)(in); Xref=Rhea:RHEA:72915, ChEBI:CHEBI:29101, ChEBI:CHEBI:37714; Evidence={ECO:0000269|PubMed:22212718, ECO:0000269|PubMed:23451068}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72916; Evidence={ECO:0000250|UniProtKB:Q5SWY8}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.45 mM for D-mannose {ECO:0000269|PubMed:22212718}; KM=0.62 mM for D-fructopyranose {ECO:0000269|PubMed:22212718}; | null | null | null | FUNCTION: [Isoform 1]: Electrogenic Na+-coupled sugar symporter that actively transports D-mannose or D-fructose at the plasma membrane, with a Na+ to sugar coupling ratio of 1:1. Transporter activity is driven by a transmembrane Na+ electrochemical gradient set by the Na+/K+ pump. Exclusively recognizes sugar substrates having a pyranose ring with an axial hydroxyl group on carbon 2 (PubMed:22212718, PubMed:23451068, PubMed:24573086). Has likely evolved to enable renal reabsorption of D-mannose, an important constituent of oligosaccharide chains of glycoproteins. Contributes to dietary D-fructose reabsorption from glomerular filtrate across the brush border of the kidney (PubMed:22212718, PubMed:23451068). {ECO:0000269|PubMed:22212718, ECO:0000269|PubMed:23451068, ECO:0000269|PubMed:24573086}.; FUNCTION: [Isoform 2]: Appears to have no transporter activity. {ECO:0000269|PubMed:22212718}. | Homo sapiens (Human) |
A0PJY2 | FEZF1_HUMAN | MDSSCHNATTKMLATAPARGNMMSTSKPLAFSIERIMARTPEPKALPVPHFLQGALPKGEPKHSLHLNSSIPCMIPFVPVAYDTSPKAGVTGSEPRKASLEAPAAPAAVPSAPAFSCSDLLNCALSLKGDLARDALPLQQYKLVRPRVVNHSSFHAMGALCYLNRGDGPCHPAAGVNIHPVASYFLSSPLHPQPKTYLAERNKLVVPAVEKYPSGVAFKDLSQAQLQHYMKESAQLLSEKIAFKTSDFSRGSPNAKPKVFTCEVCGKVFNAHYNLTRHMPVHTGARPFVCKVCGKGFRQASTLCRHKIIHTQEKPHKCNQCGKAFNRSSTLNTHTRIHAGYKPFVCEFCGKGFHQKGNYKNHKLTHSGEKQFKCNICNKAFHQVYNLTFHMHTHNDKKPFTCPTCGKGFCRNFDLKKHVRKLHDSSLGLARTPAGEPGTEPPPPLPQQPPMTLPPLQPPLPTPGPLQPGLHQGHQ | null | null | axon guidance [GO:0007411]; cell dedifferentiation [GO:0043697]; forebrain anterior/posterior pattern specification [GO:0021797]; interneuron migration [GO:1904936]; negative regulation of cell population proliferation [GO:0008285]; olfactory bulb development [GO:0021772]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of neuron differentiation [GO:0045666]; regulation of neurogenesis [GO:0050767]; regulation of transcription by RNA polymerase II [GO:0006357] | cytosol [GO:0005829]; nucleoplasm [GO:0005654] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00096;PF13912; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19318583}. | null | null | null | null | null | FUNCTION: Transcription repressor. Involved in the axonal projection and proper termination of olfactory sensory neurons (OSN). Plays a role in rostro-caudal patterning of the diencephalon and in prethalamic formation. Expression is required in OSN to cell-autonomously regulate OSN axon projections. Regulates non-cell-autonomously the layer formation of the olfactory bulb development and the interneurons. May be required for correct rostral migration of the interneuron progenitors (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
A0PK00 | T120B_HUMAN | MSGQLERCEREWHELEGEFQELQETHRIYKQKLEELAALQTLCSSSISKQKKHLKDLKLTLQRCKRHASREEAELVQQMAANIKERQDVFFDMEAYLPKKNGLYLNLVLGNVNVTLLSNQAKFAYKDEYEKFKLYLTIILLLGAVACRFVLHYRVTDEVFNFLLVWYYCTLTIRESILISNGSRIKGWWVSHHYVSTFLSGVMLTWPNGPIYQKFRNQFLAFSIFQSCVQFLQYYYQRGCLYRLRALGERNHLDLTVEGFQSWMWRGLTFLLPFLFCGHFWQLYNAVTLFELSSHEECREWQVFVLAFTFLILFLGNFLTTLKVVHAKLQKNRGKTKQP | null | null | fat cell differentiation [GO:0045444]; protein heterooligomerization [GO:0051291] | nuclear inner membrane [GO:0005637] | null | PF07851; | null | TMEM120 family | null | SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250|UniProtKB:Q3TA38}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Necessary for efficient adipogenesis. Does not show ion channel activity. {ECO:0000250|UniProtKB:Q3TA38}. | Homo sapiens (Human) |
A0PK11 | CLRN2_HUMAN | MPGWFKKAWYGLASLLSFSSFILIIVALVVPHWLSGKILCQTGVDLVNATDRELVKFIGDIYYGLFRGCKVRQCGLGGRQSQFTIFPHLVKELNAGLHVMILLLLFLALALALVSMGFAILNMIQVPYRAVSGPGGICLWNVLAGGVVALAIASFVAAVKFHDLTERIANFQEKLFQFVVVEEQYEESFWICVASASAHAANLVVVAISQIPLPEIKTKIEEATVTAEDILY | null | null | auditory receptor cell stereocilium organization [GO:0060088]; sensory perception of sound [GO:0007605]; stereocilium maintenance [GO:0120045] | stereocilium bundle [GO:0032421]; stereocilium membrane [GO:0060171] | null | null | 1.20.140.150; | Clarin family | null | SUBCELLULAR LOCATION: Cell projection, stereocilium membrane {ECO:0000250|UniProtKB:B2RVW2}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Plays a key role to hearing function. Required for normal organization and maintenance of the stereocilia bundle and for mechano-electrical transduction. {ECO:0000250|UniProtKB:B2RVW2}. | Homo sapiens (Human) |
A0PVU7 | KGD_MYCUA | MANISSPFGQNEWLVEEMYRKFRDDPSSVDPSWHEFLVDYNPESTQEATEPAVVKPAAAPAKPAPAPAPAKPAAGPPAAGNGSPAAAPSAKPAAAPAKAPAPPPAEGDEMQVLRGAAAAVVKNMSASLDVPTATSVRAVPAKLLIDNRIVINNQLKRNRGGKISFTHLLGYALVQAVKKFPNMNRHYLDVDGKPNAVTPAHTNLGLAIDLQGKDGKRALVVAGIKRCETMRFAQFVTAYEDIVRRARDGKLTAEDFSGVTISLTNPGTIGTVHSVPRLMAGQGAIIGVGAMEYPAEFQGASEERIAELGIGKLITLTSTYDHRIIQGAESGDFLRTIHQMLLADEFWDEIFRELSIPYLPVRWRPDNPDSIVDKNARIIELIAAYRNRGHLMADIDPLRLDKTRFRSHPDLDVCTHGLTLWDLDRSFKVGGCFAGPQNMKLRDVLSILRDTYCRHVGVEYTHILEPEQQQWLQQRVEAKHVKPTVAQQKYVLSKLNAAEAFETFLQTKYVGQKRFSLEGAESVIPMMDAAIDQCAEYGLDEVVIGMPHRGRLNVLANIVGKPYSQIFSEFEGNLNPSQAHGSGDVKYHLGATGVYLQMFGDNDIQVSLTANPSHLEAVDPVLEGLVRAKQDLLEHGETDTENQRAFSVVPMMLHGDAAFAGQGVVAETLNLANLPGYRVGGTIHIIVNNQIGFTTAPEYSRSTEYCTDVAKTIGAPIFHVNGDDPEACVWVARLAVDFRQRFNKDVIIDMLCYRRRGHNEGDDPSMTNPRMYDVVDTKRGVRKSYTEALIGRGDISIKEAEDALRDYQGQLEQVFNEVRELEKHGAQPSESVESDQMIPAGLATAVDKSLLARIGDAFLAVPDGFTTHPRVQPVLEKRREMAYEGKIDWAFAELLALGSLVAEGKLVRFSGQDTRRGTFSQRHSVIIDRHTREEFTPLQLLTTNKDGSPTGGKFLVYDSPLSEYAAVGFEYGYTVGNPDAVVLWEAQFGDFVNGAQSIIDEFISSGEAKWGQLSNVVLLLPHGHEGQGPDHTSGRIERFLQLWAEGSMTIAMPSTPSNYFHLLRRHALDGIQRPLIVFTPKSMLRNKAAVSDIKDFTEIKFRSVLEEPTYEDGVGDRNLVNRILLTSGKIYYEMVARKAKDKREDVAIVRVEQLAPLPRRRLRETLDRYPNAKEFFWVQEEPANQGAWPRFGLELPELLPEKLSGVKRISRRAMSAPSSGSSKVHAVEQQEILDTAFG | 1.2.4.2; 2.2.1.5; 2.3.1.61; 4.1.1.71 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250}; | tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; oxoglutarate dehydrogenase complex [GO:0045252] | 2-hydroxy-3-oxoadipate synthase activity [GO:0050439]; 2-oxoglutarate decarboxylase activity [GO:0008683]; dihydrolipoyllysine-residue succinyltransferase activity [GO:0004149]; magnesium ion binding [GO:0000287]; oxoglutarate dehydrogenase (succinyl-transferring) activity [GO:0004591]; thiamine pyrophosphate binding [GO:0030976] | PF00198;PF16078;PF00676;PF16870;PF02779; | 3.40.50.12470;3.40.50.970;3.30.559.10;3.40.50.11610;1.10.287.1150; | 2-oxoacid dehydrogenase family, Kgd subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + glyoxylate + H(+) = 2-hydroxy-3-oxoadipate + CO2; Xref=Rhea:RHEA:14341, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:36655, ChEBI:CHEBI:57712; EC=2.2.1.5; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) = CO2 + succinate semialdehyde; Xref=Rhea:RHEA:10524, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:57706; EC=4.1.1.71; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2; CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61; | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from 2-oxoglutarate (transferase route): step 1/2.; PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1. | null | null | FUNCTION: Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutarate to four-carbon succinate semialdehyde (SSA). Also catalyzes C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate dehydrogenase (ODH) complex, that catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The KG decarboxylase and KG dehydrogenase reactions provide two alternative, tightly regulated, pathways connecting the oxidative and reductive branches of the TCA cycle (By similarity). {ECO:0000250}. | Mycobacterium ulcerans (strain Agy99) |
A0Q5Y3 | CAS9_FRATN | MNFKILPIAIDLGVKNTGVFSAFYQKGTSLERLDNKNGKVYELSKDSYTLLMNNRTARRHQRRGIDRKQLVKRLFKLIWTEQLNLEWDKDTQQAISFLFNRRGFSFITDGYSPEYLNIVPEQVKAILMDIFDDYNGEDDLDSYLKLATEQESKISEIYNKLMQKILEFKLMKLCTDIKDDKVSTKTLKEITSYEFELLADYLANYSESLKTQKFSYTDKQGNLKELSYYHHDKYNIQEFLKRHATINDRILDTLLTDDLDIWNFNFEKFDFDKNEEKLQNQEDKDHIQAHLHHFVFAVNKIKSEMASGGRHRSQYFQEITNVLDENNHQEGYLKNFCENLHNKKYSNLSVKNLVNLIGNLSNLELKPLRKYFNDKIHAKADHWDEQKFTETYCHWILGEWRVGVKDQDKKDGAKYSYKDLCNELKQKVTKAGLVDFLLELDPCRTIPPYLDNNNRKPPKCQSLILNPKFLDNQYPNWQQYLQELKKLQSIQNYLDSFETDLKVLKSSKDQPYFVEYKSSNQQIASGQRDYKDLDARILQFIFDRVKASDELLLNEIYFQAKKLKQKASSELEKLESSKKLDEVIANSQLSQILKSQHTNGIFEQGTFLHLVCKYYKQRQRARDSRLYIMPEYRYDKKLHKYNNTGRFDDDNQLLTYCNHKPRQKRYQLLNDLAGVLQVSPNFLKDKIGSDDDLFISKWLVEHIRGFKKACEDSLKIQKDNRGLLNHKINIARNTKGKCEKEIFNLICKIEGSEDKKGNYKHGLAYELGVLLFGEPNEASKPEFDRKIKKFNSIYSFAQIQQIAFAERKGNANTCAVCSADNAHRMQQIKITEPVEDNKDKIILSAKAQRLPAIPTRIVDGAVKKMATILAKNIVDDNWQNIKQVLSAKHQLHIPIITESNAFEFEPALADVKGKSLKDRRKKALERISPENIFKDKNNRIKEFAKGISAYSGANLTDGDFDGAKEELDHIIPRSHKKYGTLNDEANLICVTRGDNKNKGNRIFCLRDLADNYKLKQFETTDDLEIEKKIADTIWDANKKDFKFGNYRSFINLTPQEQKAFRHALFLADENPIKQAVIRAINNRNRTFVNGTQRYFAEVLANNIYLRAKKENLNTDKISFDYFGIPTIGNGRGIAEIRQLYEKVDSDIQAYAKGDKPQASYSHLIDAMLAFCIAADEHRNDGSIGLEIDKNYSLYPLDKNTGEVFTKDIFSQIKITDNEFSDKKLVRKKAIEGFNTHRQMTRDGIYAENYLPILIHKELNEVRKGYTWKNSEEIKIFKGKKYDIQQLNNLVYCLKFVDKPISIDIQISTLEELRNILTTNNIAATAEYYYINLKTQKLHEYYIENYNTALGYKKYSKEMEFLRSLAYRSERVKIKSIDDVKQVLDKDSNFIIGKITLPFKKEWQRLYREWQNTTIKDDYEFLKSFFNVKSITKLHKKVRKDFSLPISTNEGKFLVKRKTWDNNFIYQILNDSDSRADGTKPFIPAFDISKNEIVEAIIDSFTSKNIFWLPKNIELQKVDNKNIFAIDTSKWFEVETPSDLRDIGIATIQYKIDNNSRPKVRVKLDYVIDDDSKINYFMNHSLLKSRYPDKVLEILKQSTIIEFESSGFNKTIKEMLGMKLAGIYNETSNN | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:26875867}; | defense response to virus [GO:0051607] | null | DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; RNA binding [GO:0003723] | PF21069; | 1.10.30.50; | CRISPR-associated protein Cas9 family, Subtype II-B subfamily | null | null | null | null | null | null | null | FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). In type II CRISPR systems correct processing of pre-crRNA requires a trans-encoded small RNA (tracrRNA), endogenous ribonuclease 3 (rnc) and this protein. The tracrRNA serves as a guide for ribonuclease 3-aided processing of pre-crRNA. Subsequently Cas9/crRNA/tracrRNA endonucleolytically cleaves linear or circular dsDNA target complementary to the spacer; Cas9 is inactive in the absence of the 2 guide RNAs (gRNA). Cas9 recognizes a short motif in the CRISPR repeat sequences (the PAM or protospacer adjacent motif) to help distinguish self versus nonself, as targets within the bacterial CRISPR locus do not have PAMs. PAM recognition is also required for catalytic activity. Cuts target DNA when Cas9 and gRNAs are mixed (PubMed:24270795, PubMed:26875867). {ECO:0000250|UniProtKB:Q99ZW2, ECO:0000269|PubMed:24270795, ECO:0000269|PubMed:26875867}.; FUNCTION: Plays a role in repression of expression of endogenous bacterial lipoprotein FTN_1103. Cas9 plays a possibly non-enzymatic role in the degradation of FTN_1103 mRNA, which is dependent on formation of an RNA:RNA complex of tracrRNA and scaRNA (the latter is not found in all type II CRISPR-Cas systems). {ECO:0000269|PubMed:23584588}. | Francisella tularensis subsp. novicida (strain U112) |
A0Q7Q2 | CS12A_FRATN | MSIYQEFVNKYSLSKTLRFELIPQGKTLENIKARGLILDDEKRAKDYKKAKQIIDKYHQFFIEEILSSVCISEDLLQNYSDVYFKLKKSDDDNLQKDFKSAKDTIKKQISEYIKDSEKFKNLFNQNLIDAKKGQESDLILWLKQSKDNGIELFKANSDITDIDEALEIIKSFKGWTTYFKGFHENRKNVYSSNDIPTSIIYRIVDDNLPKFLENKAKYESLKDKAPEAINYEQIKKDLAEELTFDIDYKTSEVNQRVFSLDEVFEIANFNNYLNQSGITKFNTIIGGKFVNGENTKRKGINEYINLYSQQINDKTLKKYKMSVLFKQILSDTESKSFVIDKLEDDSDVVTTMQSFYEQIAAFKTVEEKSIKETLSLLFDDLKAQKLDLSKIYFKNDKSLTDLSQQVFDDYSVIGTAVLEYITQQIAPKNLDNPSKKEQELIAKKTEKAKYLSLETIKLALEEFNKHRDIDKQCRFEEILANFAAIPMIFDEIAQNKDNLAQISIKYQNQGKKDLLQASAEDDVKAIKDLLDQTNNLLHKLKIFHISQSEDKANILDKDEHFYLVFEECYFELANIVPLYNKIRNYITQKPYSDEKFKLNFENSTLANGWDKNKEPDNTAILFIKDDKYYLGVMNKKNNKIFDDKAIKENKGEGYKKIVYKLLPGANKMLPKVFFSAKSIKFYNPSEDILRIRNHSTHTKNGSPQKGYEKFEFNIEDCRKFIDFYKQSISKHPEWKDFGFRFSDTQRYNSIDEFYREVENQGYKLTFENISESYIDSVVNQGKLYLFQIYNKDFSAYSKGRPNLHTLYWKALFDERNLQDVVYKLNGEAELFYRKQSIPKKITHPAKEAIANKNKDNPKKESVFEYDLIKDKRFTEDKFFFHCPITINFKSSGANKFNDEINLLLKEKANDVHILSIDRGERHLAYYTLVDGKGNIIKQDTFNIIGNDRMKTNYHDKLAAIEKDRDSARKDWKKINNIKEMKEGYLSQVVHEIAKLVIEYNAIVVFEDLNFGFKRGRFKVEKQVYQKLEKMLIEKLNYLVFKDNEFDKTGGVLRAYQLTAPFETFKKMGKQTGIIYYVPAGFTSKICPVTGFVNQLYPKYESVSKSQEFFSKFDKICYNLDKGYFEFSFDYKNFGDKAAKGKWTIASFGSRLINFRNSDKNHNWDTREVYPTKELEKLLKDYSIEYGHGECIKAAICGESDKKFFAKLTSVLNTILQMRNSKTGTELDYLISPVADVNGNFFDSRQAPKNMPQDADANGAYHIGLKGLMLLGRIKNNQEGKKLNLVIKNEEYFEFVQNRNN | 3.1.21.1; 4.6.1.22 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:26593719}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:26422227, ECO:0000269|PubMed:26593719, ECO:0000269|PubMed:27096362, ECO:0000269|PubMed:28562584}; Note=Cleavage of dsDNA requires Mg(2+) (PubMed:26422227, PubMed:28562584). Another report shows DNA cleavage occurs equally well in the presence of Ca(2+) or Mg(2+) (PubMed:27096362). Processing of pre-crRNA requires a divalent cation, preferably Mg(2+) which is bound by the crRNA (PubMed:26593719, PubMed:28431230). {ECO:0000269|PubMed:26422227, ECO:0000269|PubMed:26593719, ECO:0000269|PubMed:27096362, ECO:0000269|PubMed:28431230, ECO:0000269|PubMed:28562584}; | defense response to virus [GO:0051607] | null | Bacillus subtilis ribonuclease activity [GO:0033898]; deoxyribonuclease I activity [GO:0004530]; DNA binding [GO:0003677]; lyase activity [GO:0016829]; RNA binding [GO:0003723] | PF18510;PF18501;PF18516; | null | CRISPR-associated endonuclease Cas12a family | null | null | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products.; EC=3.1.21.1; Evidence={ECO:0000269|PubMed:28431230}; CATALYTIC ACTIVITY: Reaction=RNA = a 5'-hydroxy-ribonucleotide + n nucleoside-2',3'-cyclophosphates.; EC=4.6.1.22; Evidence={ECO:0000269|PubMed:28431230}; | null | null | null | null | FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Has endonuclease activity on pre-crRNA and dsDNA, using different active sites. A single-RNA guided endonuclease that is also capable of guiding crRNA processing; correct processing of pre-crRNA requires only this protein and the CRISPR locus (PubMed:26422227, PubMed:27096362). pre-crRNA processing proceeds by an intramolecular nucleophilic attack on the scissile phosphate by the 2'-OH of the upstream ribonucleotide, the divalent cation (which is bound by the crRNA) is probably required for ordering the crRNA pseudoknot and/or increasing RNA binding (PubMed:28431230). RNA mutagenesis studies show pre-crRNA cleavage is highly sequence- and structure-specific (PubMed:27096362). Forms a complex with crRNA and complementary dsDNA, where the crRNA displaces the non-target DNA strand and directs endonucleolytic cleavage of both strands of the DNA (PubMed:26422227, PubMed:27096362, PubMed:28431230). Cleavage results in staggered 5-base 5' overhangs 14-18 and 21-23 bases downstream of the PAM (protospacer adjacent motif) on the non-target and target strands respectively (PubMed:26422227, PubMed:28431230, PubMed:28562584). Both target and non-target strand DNA are probably independently cleaved in the same active site (PubMed:28431230, PubMed:28562584). When this protein is expressed in E.coli it prevents plasmids homologous to the first CRISPR spacer from transforming, formally showing it is responsible for plasmid immunity (PubMed:26422227). {ECO:0000269|PubMed:26422227, ECO:0000269|PubMed:27096362, ECO:0000269|PubMed:28431230, ECO:0000269|PubMed:28562584}. | Francisella tularensis subsp. novicida (strain U112) |
A0QNE0 | GYRB_MYCS2 | MAAQKNNAPKEYGADSITILEGLEAVRKRPGMYIGSTGERGLHHLIWEVVDNAVDEAMAGFATRVDVKIHADGSVEVRDDGRGIPVEMHATGMPTIDVVMTQLHAGGKFDGETYAVSGGLHGVGVSVVNALSTRLEATVLRDGYEWFQYYDRSVPGKLKQGGETKETGTTIRFWADPEIFETTDYNFETVARRLQEMAFLNKGLTIELTDERVTAEEVVDDVVKDTAEAPKTADEKAAEATGPSKVKHRVFHYPGGLVDYVKHINRTKTPIQQSIIDFDGKGPGHEVEIAMQWNAGYSESVHTFANTINTHEGGTHEEGFRAALTSVVNRYAKDKKLLKDKDPNLTGDDIREGLAAVISVKVAEPQFEGQTKTKLGNTEVKSFVQKICNEQLQHWFEANPAEAKTVVNKAVSSAQARIAARKARELVRRKSATDIGGLPGKLADCRSTDPSKSELYVVEGDSAGGSAKSGRDSMFQAILPLRGKIINVEKARIDRVLKNTEVQSIITALGTGIHDEFDISKLRYHKIVLMADADVDGQHISTLLLTLLFRFMKPLVENGHIFLAQPPLYKLKWQRSEPEFAYSDRERDGLLEAGRAAGKKINVDDGIQRYKGLGEMDAKELWETTMDPSVRVLRQVTLDDAAAADELFSILMGEDVEARRSFITRNAKDVRFLDV | 5.6.2.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; 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]; 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}. | 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}; | null | null | null | null | FUNCTION: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner (PubMed:8878580) 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, ECO:0000269|PubMed:8878580}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QNG1 | PKNB_MYCS2 | MTTPQHLSDRYELGEILGFGGMSEVHLARDLRLHRDVAVKVLRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETPNGPLPYIVMEYVDGVTLRDIVHTDGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIARALADTGNSVTQTAAVIGTAQYLSPEQARGETVDARSDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPVPPSRRHADVTPELDAVVLKALAKNPDNRYQTAAEMRADLIRVHEGQAPDAPKVLTDAERTSMLAAPPADRAGAATQDMPVPRPAGYSKQRSTSVARWLIAVAVLAVLTVVVTVAINMVGGNPRNVQVPDVAEQSADDAQAALQNRGFKTVIDRQPDNEVPPGLVIGTDPEAGSELGAGEQVTINVSTGPEQALVPDVAGLTPTQARQKLKDAGFEKFRESPSPSTPEQKGRVLATNPQANQTAAIINEITIVVGAGPEDAPVLSCAGQNAESCKAILAAGGFTNTVVVEVDNPAAAGQVVGTEPADGQSVPKDTVIQIRVSKGNQFVMPDLVGQFWSDAYPRLTALGWTGVLDKGPDVRDSGQRTNAVVTQSPSAGTPVNKDAKITLSFAA | 2.7.11.1 | null | phosphorylation [GO:0016310]; regulation of cellular biosynthetic process [GO:0031326]; regulation of primary metabolic process [GO:0080090] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF03793;PF00069; | 3.30.10.20;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Autophosphorylated. Dephosphorylated by PstP (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass 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: Protein kinase that regulates many aspects of mycobacterial physiology. Is a key component of a signal transduction pathway that regulates cell growth, cell shape and cell division via phosphorylation of target proteins (By similarity). Probably phosphorylates RseA (PubMed:20025669). {ECO:0000250|UniProtKB:P9WI81, ECO:0000305|PubMed:20025669}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QP27 | MMPL3_MYCS2 | MFAWWGRTVYQFRYIVIGVMVALCLGGGVYGISLGNHVTQSGFYDEGSQSVAASLIGDEVYGRDRTSHVVAILTPPDDKKVTDKAWQKKVTEELDQVVKDHEDQIVGWVGWLKAPDTTDPTVSAMKTQDLRHTFISIPLQGDDDDEILKNYQVVEPELQQVNGGDIRLAGLNPLASELTGTIGEDQKRAEVAAIPLVAVVLFFVFGTVIAAALPAIIGGLAIAGALGIMRLVAEFTPVHFFAQPVVTLIGLGIAIDYGLFIVSRFREEIAEGYDTEAAVRRTVMTSGRTVVFSAVIIVASSVPLLLFPQGFLKSITYAIIASVMLAAILSITVLAAALAILGPRVDALGVTTLLKIPFLANWQFSRRIIDWFAEKTQKTKTREEVERGFWGRLVNVVMKRPIAFAAPILVVMVLLIIPLGQLSLGGISEKYLPPDNAVRQSQEQFDKLFPGFRTEPLTLVMKREDGEPITDAQIADMRAKALTVSGFTDPDNDPEKMWKERPANDSGSKDPSVRVIQNGLENRNDAAKKIDELRALQPPHGIEVFVGGTPALEQDSIHSLFDKLPLMALILIVTTTVLMFLAFGSVVLPIKAALMSALTLGSTMGILTWMFVDGHGSGLMNYTPQPLMAPMIGLIIAVIWGLSTDYEVFLVSRMVEARERGMSTAEAIRIGTATTGRLITGAALILAVVAGAFVFSDLVMMKYLAFGLLIALLLDATIIRMFLVPAVMKLLGDDCWWAPRWMKRVQEKLGLGETELPDERKRPTVRESETDQRALVGVGAPPPPPRPHDPTHPAPEPVRPMPPMRSNAPSAAGTARISTPPQPPQPPQAPAQQAGDEPATTRFAMARNAVRNAVNSAVHGGAGSAAAPTERAPRPGGPAQPPAPPQREEREIESWLGALRGPAPAKNVPQPPAQPQRPSTDTTRAMPPQGRPPAGPADRGNENAPTTAFSAQRPPNGGAPADATTAIPTPPQREQEPSTEKLNTREDAPEDPETKRRGGGMSAQDLLRREGRL | null | null | cell wall biogenesis [GO:0042546]; cell wall organization [GO:0071555]; mycolate cell wall layer assembly [GO:0071769]; mycolic acid biosynthetic process [GO:0071768]; phospholipid transport [GO:0015914]; regulation of membrane potential [GO:0042391]; response to antibiotic [GO:0046677]; response to xenobiotic stimulus [GO:0009410]; trehalose transport [GO:0015771] | cell pole [GO:0060187]; cell septum [GO:0030428]; cell tip [GO:0051286]; plasma membrane [GO:0005886] | cardiolipin binding [GO:1901612]; diacylglycerol binding [GO:0019992]; phosphatidylethanolamine binding [GO:0008429]; phosphatidylethanolamine transfer activity [GO:1904121]; phosphatidylglycerol binding [GO:1901611]; phosphatidylinositol binding [GO:0035091]; trehalose transmembrane transporter activity [GO:0015574] | PF03176; | 1.20.1640.10; | Resistance-nodulation-cell division (RND) (TC 2.A.6) family, MmpL subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:28698380, ECO:0000269|PubMed:30682372, ECO:0000269|PubMed:31113875}; Multi-pass membrane protein {ECO:0000255, ECO:0000305|PubMed:30682372, ECO:0000305|PubMed:31113875}. Cell septum {ECO:0000269|PubMed:31239378}. Cell tip {ECO:0000269|PubMed:31239378}. Note=Colocalizes with TtfA to the cell poles and septa. Trehalose monomycolate (TMM) synthesis is not required for localization to the poles or septa. {ECO:0000269|PubMed:31239378}. | null | null | null | null | null | FUNCTION: Transports trehalose monomycolate (TMM) to the cell wall (PubMed:22520756, PubMed:28698380, PubMed:31239378). Flips TMM across the inner membrane. Membrane potential is not required for this function (PubMed:28698380). Transports probably phosphatidylethanolamine (PE) as well. Binds specifically both TMM and PE, but not trehalose dimycolate (TDM). Binds also diacylglycerol (DAG) and other phospholipids, including phosphatidylglycerol (PG), phosphatidylinositol (PI), and cardiolipin (CDL) (PubMed:31113875). Contributes to membrane potential, cell wall composition, antibiotic susceptibility and fitness (PubMed:28703701). {ECO:0000269|PubMed:22520756, ECO:0000269|PubMed:28698380, ECO:0000269|PubMed:28703701, ECO:0000269|PubMed:31113875, ECO:0000269|PubMed:31239378}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QQF4 | TTFA_MYCS2 | MVPLWFTLSALCFVGAAVLLYVDIDRRRGLGRRRKSWAKSHGFDYEYESEDLLKRWKRGVMSTVGDVTAKNVVLGQIRGEAVFIFDIEEVATVIALHRKVGTNVVVDLRLKGLKEPRENDIWLLGAIGPRMVYSTNLDAARRACDRRMVTFAHTAPDCAEIMWNEQNWTLVAMPVTSNRAQWDEGLRTVRQFNDLLRVLPPVPQNGSQAALPRRGGSPSRPLAPTPAGRRELPPGRADVPPARGDVSRFAPRPEAGRSDAFRRPPPARNGREASHFQR | null | null | cell wall organization [GO:0071555]; lipid transport [GO:0006869] | cell septum [GO:0030428]; cell tip [GO:0051286]; plasma membrane [GO:0005886] | null | null | null | null | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:31239378}; Single-pass membrane protein {ECO:0000255}. Cell septum {ECO:0000269|PubMed:31239378}. Cell tip {ECO:0000269|PubMed:31239378}. Note=Colocalizes with MmpL3 to the cell poles and septa. Trehalose monomycolate (TMM) synthesis is not required for localization to the poles or septa. {ECO:0000269|PubMed:31239378}. | null | null | null | null | null | FUNCTION: Required for MmpL3-dependent trehalose monomycolate (TMM) transport to the cell wall. Required for growth and cell elongation. {ECO:0000269|PubMed:31239378}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QQJ4 | FGD_MYCS2 | MAELKLGYKASAEQFAPRELVELAVLAESAGMDSATVSDHFQPWRHEGGHAPFSLAWMTAVGERTKNLVLGTSVLTPTFRYNPAVIAQAFATMGCLYPGRIFLGVGTGEALNEIATGYAGEWPEFKERFARLRESVRLMRELWLGDRVDFDGEYYRTKGASIYDVPEGGIPVYIAAGGPVVAKYAGRAGDGFICTSGKGEELYAEKLIPAVKEGAAAADRDADAIDRMIEIKISYDTDPELALENTRFWAPLSLTAEQKHSIDDPIEMEKAADALPIEQVAKRWIVASDPDEAVEKVGQYVKWGLNHLVFHAPGHDQRRFLELFKRDLEPRLRKLA | 1.1.98.2 | null | carbohydrate metabolic process [GO:0005975] | null | coenzyme F420 binding [GO:0070967]; glucose-6-phosphate dehydrogenase (coenzyme F420) activity [GO:0052749]; oxidoreductase activity, acting on CH-OH group of donors [GO:0016614]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; protein homodimerization activity [GO:0042803] | PF00296; | 3.20.20.30; | F420-dependent glucose-6-phosphate dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) = 6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420-(gamma-L-Glu)(n); Xref=Rhea:RHEA:27294, Rhea:RHEA-COMP:12939, Rhea:RHEA-COMP:14378, ChEBI:CHEBI:15378, ChEBI:CHEBI:57955, ChEBI:CHEBI:61548, ChEBI:CHEBI:133980, ChEBI:CHEBI:139511; EC=1.1.98.2; Evidence={ECO:0000269|PubMed:8631674, ECO:0000269|PubMed:9555906}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.004 mM for coenzyme F420 (at pH 7 and 40 degrees Celsius) {ECO:0000269|PubMed:8631674}; KM=1.6 mM for D-glucose 6-phosphate (at pH 7 and 40 degrees Celsius) {ECO:0000269|PubMed:8631674}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pHs are 5.5 and 8.0. {ECO:0000269|PubMed:8631674}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:8631674}; | FUNCTION: Catalyzes the coenzyme F420-dependent oxidation of glucose 6-phosphate (G6P) to 6-phosphogluconolactone. Appears to have a role in resistance to oxidative stress, via its consumption of G6P that serves as a source of reducing power to combat oxidative stress in mycobacteria. Cannot use NAD, NADP, FAD or FMN instead of coenzyme F420 as an electron acceptor. Exhibits nearly no activity with D-mannose-6-phosphate or D-fructose-6-phosphate as substrate. {ECO:0000269|PubMed:20075070, ECO:0000269|PubMed:8631674}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QQU5 | CH602_MYCS2 | MAKTIAYDEEARRGLERGLNSLADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKEQIAATAGISAGDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRFDKGYISGYFVTDAERQEAVLEDPYILLVSSKVSTVKDLLPLLEKVIQSGKPLLIIAEDVEGEALSTLVVNKIRGTFKSVAVKAPGFGDRRKAMLQDMAILTGGQVISEEVGLSLETADVSLLGKARKVVVTKDETTIVEGAGDAEAIQGRVAQIRAEIENSDSDYDREKLQERLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGVALLQSAPSLEELSLTGDEATGANIVRVALSAPLKQIALNGGLEPGVVAEKVSNLPAGHGLNAATGEYEDLLAAGVADPVKVTRSALQNAASIAALFLTTEAVVADKPEKAAAPAGDPTGGMGGMDF | 5.6.1.7 | null | chaperone cofactor-dependent protein refolding [GO:0051085]; mitochondrial unfolded protein response [GO:0034514]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of T cell activation [GO:0050870]; positive regulation of type II interferon production [GO:0032729]; protein import into mitochondrial intermembrane space [GO:0045041]; protein refolding [GO:0042026]; response to heat [GO:0009408] | capsule [GO:0042603]; cell surface [GO:0009986]; extracellular region [GO:0005576]; GroEL-GroES complex [GO:1990220] | ATP binding [GO:0005524]; ATP-dependent protein folding chaperone [GO:0140662]; isomerase activity [GO:0016853]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082] | PF00118; | 3.50.7.10;1.10.560.10;3.30.260.10; | Chaperonin (HSP60) family | null | SUBCELLULAR LOCATION: Secreted, capsule {ECO:0000250|UniProtKB:P9WPE7}. Cell surface {ECO:0000250|UniProtKB:P9WPE7}. Secreted, cell wall {ECO:0000250|UniProtKB:P9WPE7}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00600}; | null | null | null | null | FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. {ECO:0000255|HAMAP-Rule:MF_00600}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QR29 | MSPA_MYCS2 | MKAISRVLIAMVAAIAALFTSTGTSHAGLDNELSLVDGQDRTLTVQQWDTFLNGVFPLDRNRLTREWFHSGRAKYIVAGPGADEFEGTLELGYQIGFPWSLGVGINFSYTTPNILIDDGDITAPPFGLNSVITPNLFPGVSISADLGNGPGIQEVATFSVDVSGAEGGVAVSNAHGTVTGAAGGVLLRPFARLIASTGDSVTTYGEPWNMN | null | null | iron ion transport [GO:0006826] | cell outer membrane [GO:0009279]; extracellular region [GO:0005576]; pore complex [GO:0046930] | porin activity [GO:0015288] | PF09203; | 2.60.40.1650;2.10.300.10; | Mycobacterial porin (TC 1.B.24) family | null | SUBCELLULAR LOCATION: Cell outer membrane. Secreted, cell wall. | null | null | null | null | null | FUNCTION: The major porin in this organism, forms a water-filled channel which favors the permeation of cations, amino acids, iron Fe(3+) and less efficiently phosphate. Does not transport Fe-ExoMS, the predominant siderophore. Plays a role in transport of beta-lactamase and hydrophilic fluoroquinolone antibiotics such as norfloxacin as well as chloramphenicol. There are about 2400 porins in wild-type, 800 in an mspA deletion and 150 in a double mspA-mspC deletion. Different conductance values with maxima at 2.3 and 4.6 nanosiemens might be caused by a simultaneous reconstitution of MspA channels into the membrane or by the existence of different MspA conformations. {ECO:0000269|PubMed:10476028, ECO:0000269|PubMed:16238622, ECO:0000269|PubMed:17209034, ECO:0000269|PubMed:18559650, ECO:0000269|PubMed:20952578}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QS29 | RECB_MYCS2 | MKVFDLLGPLPAPNTTTVLEASAGTGKTFALAGLVTRFVAEGVATLDQMLLITFGRAASQELRERVRAQIVAALVALDDPSRACNDLEEYLVKTDQQARRRRLRDALAGFDAATIATTHQFCQIVLKSLGVAGDSDAGVTLVESLDDLVSEIVDDLYLAHFGGQKDDPELSYPEALKLARVVVGNPATQLRPRDPDPDSPAAVRLKFARDVLAELEIRKRRRGVLGYDDLLTRLADALEPEDSPARVRMQQRWPIVMVDEFQDTDPVQWQVIERAFSGRSTLVLIGDPKQAIYAFRGGDIATYLRAAATAGDKQTLGTNWRSDRALVDRLQAVLRGAQLGGPDIVVHDVQARHQGHRLVGAPRNDPFRLRVVSRKPGNTRVIPIDQLRRHIGRDLAADISALLNSGATWCDQPVQAKDIAVITETHKDARACHAALLAAGIPAVYTGDSDVFTSEAAEDWLYLLEAFDQPHRPGLVRAAAATMFFGETAESLAAGGDALTDRVADTLREWAGHARERGVAAIFEAAQLAGMGKRVLSWQGGERLMTDLAHMTQLLQDTAHREGFGLAALRDWLRTQRSERGGESERNRRLDSDAAAVQIMTVWVSKGLQFPVVYLPFAFNRYVPEPDLVLFHDDGQRCLHVGGADPAVARAGRAEAAGDDSRLTYVALTRAQSQVVAWWAPSYDEPNGGLSRLMRGRAPGEAIVPDKCSPPKISDEDALERLRAWEAAGGPVIEESVIGAVSPVPPEPAPEDLAARKFFRAIDMAWKRTSYSGLLRAAETAGVGVSSEPEVTERDDEFDDIPVVAPAEGADVPSPMAHLPTGAAFGSLVHAVLETADPFAEDLTAELATHIDAHSQHWPVEVETAELAAALVPMHDTPLGPLAPGLTLRQIGLRDRLCELDFEFPMAGGDLRGGRFARLSDVGELLREYLPADDPLAVYAERLSTGILGVQPLRGYLSGSVDAVLRVGEKFVIVDYKTNWLGTGDGTLTAADYGRRRMVEAMLHSDYPLQALLYAVVLHRYLGWRLSGYDPATHLGGVLYLFVRGMCGAGTPVVDGHPAGVFSWEPPADLVVALSKLLDAEAP | 3.1.11.5; 5.6.2.4 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01485}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01485}; | double-strand break repair via homologous recombination [GO:0000724] | cytosol [GO:0005829]; exodeoxyribonuclease V complex [GO:0009338] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; exodeoxyribonuclease V activity [GO:0008854]; isomerase activity [GO:0016853]; magnesium ion binding [GO:0000287] | PF00580;PF13361; | 3.90.320.10;3.40.50.300; | Helicase family, UvrD subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides.; EC=3.1.11.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01485}; CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_01485}; 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=5.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_01485}; | null | null | null | null | FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit contributes DNA-dependent ATPase activity, exonuclease activity and 3'-5' helicase activity (By similarity). Unlike the case in E.coli, suppresses RecA-dependent homologous recombination, is instead required for single-strand annealing pathway repair of DSB (PubMed:21219454). {ECO:0000250|UniProtKB:P08394, ECO:0000269|PubMed:21219454}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QS56 | SIWR_MYCS2 | MARTVDTTGRVVQLLGLLQSRRVWTGEELAERLGVTGRSVRRDIERLRELGYPVHASKGQGGGYQLGAGMALPPLLLDPDEAVAMAVCLRLAAGGSVAGVGESALRALSKLDQVMPARLRSQVAAIHDATVTLGPNATDTAVAPDVLMTLARACRDREHVSTGYTDLRGNQTQRRLEPYQLVTTGRRWYLMAYDRDREDWRSLRLDRMSDVRATGTTFTARPAPDAAAYVGRAISASAYPYVARVRYFAPEKVVAQRFPPGTATFEPDGPDACIVTSGAEYPEQLAMYFATVGHDFEVLEPAEVIDAVGAMADRLRRAVR | null | null | DNA damage response, signal transduction resulting in transcription [GO:0042772]; regulation of cellular response to stress [GO:0080135] | null | core promoter sequence-specific DNA binding [GO:0001046]; DNA-binding transcription activator activity [GO:0001216]; protein homodimerization activity [GO:0042803]; single-stranded DNA binding [GO:0003697] | PF08279;PF13280; | 1.10.10.10; | null | null | null | null | null | null | null | null | FUNCTION: Transcriptional activator (PubMed:38042942). Acts as a transcriptional activator of the MSMEG_1357-56 operon upon genotoxic stress (PubMed:38042942). Controls adjacent genes that belong to the DinB/YfiT-like putative metalloenzymes superfamily by upregulating their expression in response to various genotoxic stress conditions, including exposure to H(2)O(2) or the natural antibiotic zeocin, as well as mitomycin C (MMC), diamide and UVC radiation (PubMed:38042942). Upon genotoxic stress, upregulates two genes encoding proteins of the DinB/YfiT-like putative metalloenzymes superfamily, MSMEG_1357 and MSMEG_1356 (PubMed:38042942). Binds different forms of single-stranded DNA (ssDNA) with high affinity, primarily through its characteristic WYL domain (PubMed:38042942). Binds nucleic acids with single-stranded regions, such as polyT 20mer ssDNA, 5' tailed, 3' tailed and fork DNA, but not ssRNA (PubMed:38042942). {ECO:0000269|PubMed:38042942}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QTP2 | SIGH_MYCS2 | MTDVDRVEPETPPEREETDAELTARFERDAIPLLDQLYGGALRMTRNPADAEDLLQETMVKAYAGFRSFREGTNLKAWLYRILTNTYINSYRKKQRQPSEYPTDEITDWQLASNAEHSSTGLRSAEVEALEALPDTEIKAALQALPEEFRMAVYYADVEGFPYKEIAEIMETPIGTVMSRLHRGRRQLRDLLAGVARDRGFIRGPQLGEPEEVTS | null | null | DNA-templated transcription initiation [GO:0006352]; response to abiotic stimulus [GO:0009628]; response to stress [GO:0006950] | null | DNA binding [GO:0003677]; sigma factor activity [GO:0016987] | PF04542;PF08281; | 1.10.1740.10;1.10.10.10; | Sigma-70 factor family, ECF subfamily | null | null | null | null | null | null | null | FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by an anti-sigma factor until released. This sigma factor is involved in heat shock and oxidative stress responses. {ECO:0000269|PubMed:14617153}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QUA1 | MBTM_MYCS2 | MNVLSAALTEAMTTSSADLVVFEPETRTWHRHPWGQVHLRAQNVAERIGQDGSSAVGIVGEPTVEGVAAILGALLAGSAVSILPGLVRGADPDQWADSTLNRFANIGVTTVFSHGSYLEQLRTRDSSLVIHDDAEVAHAQRSTTLELGAPLGEFAVLQGTAGSTGTPRTAQLRPDAVLANLRGLAERVGLAGSDIGCSWLPLYHDMGLTFLLSAAVGGTETWQAPTTAFASAPFSWVHWLTESRATLTAAPNMAYGLIGKYSRRLTDVDLSAMRFALNGGEPVDIDGTARFGTELSRFGFDPGALSPSYGLAESSCAVTVPVPGVGLKVDEITVTTEAGSSTQKLAVLGHAIAGMEVRLQPGDEDAGVVDREVGEVEIRGTSMMSGYRGEAPLDPGEWFPTGDLGYLTDDGLVICGRKKELITVAGRNIFPTEIERIAARVKGVREGAVVAVGTNERAVRPGLVIAAEFRGPDEAGARSEVVQRVASECGVVPADVVFLAPGSLPRTSSGKLRRLEVKRQLEESKG | 6.2.1.20; 6.2.1.47 | null | fatty acid biosynthetic process [GO:0006633] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | adenylyltransferase activity [GO:0070566]; ATP binding [GO:0005524]; long-chain fatty acid [acyl-carrier-protein] ligase activity [GO:0008922] | PF00501; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | PTM: Acetylated on Lys-511 and Lys-260 by Pat. Lys-511 is the major acetylation site. Acetylation results in the inactivation of the enzyme. {ECO:0000269|PubMed:23935107}. | null | CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:45588, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12682, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57560, ChEBI:CHEBI:64479, ChEBI:CHEBI:133243, ChEBI:CHEBI:456215; EC=6.2.1.20; Evidence={ECO:0000269|PubMed:23935107}; CATALYTIC ACTIVITY: Reaction=a medium chain fatty acid + ATP + holo-[ACP] = a medium-chain fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:50460, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:59558, ChEBI:CHEBI:64479, ChEBI:CHEBI:133242, ChEBI:CHEBI:456215; EC=6.2.1.47; Evidence={ECO:0000269|PubMed:23935107}; CATALYTIC ACTIVITY: Reaction=ATP + hexadecanoate + holo-[ACP] = AMP + diphosphate + hexadecanoyl-[ACP]; Xref=Rhea:RHEA:63628, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:64479, ChEBI:CHEBI:78483, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23935107}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63629; Evidence={ECO:0000269|PubMed:23935107}; CATALYTIC ACTIVITY: Reaction=ATP + H(+) + hexadecanoate = diphosphate + hexadecanoyl-AMP; Xref=Rhea:RHEA:43708, ChEBI:CHEBI:7896, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83627; Evidence={ECO:0000269|PubMed:23935107}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43709; Evidence={ECO:0000269|PubMed:23935107}; CATALYTIC ACTIVITY: Reaction=hexadecanoyl-AMP + holo-[ACP] = AMP + H(+) + hexadecanoyl-[ACP]; Xref=Rhea:RHEA:63624, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:78483, ChEBI:CHEBI:83627, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23935107}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63625; Evidence={ECO:0000269|PubMed:23935107}; CATALYTIC ACTIVITY: Reaction=ATP + dodecanoate + holo-[ACP] = AMP + diphosphate + dodecanoyl-[ACP]; Xref=Rhea:RHEA:63620, Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:64479, ChEBI:CHEBI:65264, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23935107}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63621; Evidence={ECO:0000269|PubMed:23935107}; CATALYTIC ACTIVITY: Reaction=ATP + dodecanoate + H(+) = diphosphate + dodecanoyl-AMP; Xref=Rhea:RHEA:43712, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83623; Evidence={ECO:0000269|PubMed:23935107}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43713; Evidence={ECO:0000269|PubMed:23935107}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-AMP + holo-[ACP] = AMP + dodecanoyl-[ACP] + H(+); Xref=Rhea:RHEA:46504, Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:65264, ChEBI:CHEBI:83623, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23935107}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46505; Evidence={ECO:0000269|PubMed:23935107}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=129 uM for hexanoic acid {ECO:0000269|PubMed:23935107}; KM=121 uM for decanoic acid {ECO:0000269|PubMed:23935107}; KM=21 uM for lauric acid {ECO:0000269|PubMed:23935107}; KM=1.9 uM for palmitic acid {ECO:0000269|PubMed:23935107}; KM=15 uM for ATP {ECO:0000269|PubMed:23935107}; KM=106 uM for MbtL-holo {ECO:0000269|PubMed:23935107}; Note=kcat is 0.11 min(-1) with hexanoic acid as substrate. kcat is 1.5 min(-1) with decanoic acid as substrate. kcat is 2.4 min(-1) with lauric acid as substrate. kcat is 4.2 min(-1) with palmitic acid as substrate. kcat is 1.3 min(-1) with ATP as substrate. kcat is 2.0 min(-1) with MbtL-holo as substrate. {ECO:0000269|PubMed:23935107}; | PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis. {ECO:0000269|PubMed:23935107}. | null | null | FUNCTION: Activates lipidic moieties required for mycobactin biosynthesis (PubMed:23935107). Converts medium- to long-chain aliphatic fatty acids into acyl adenylate, which is further transferred on to the phosphopantetheine arm of the carrier protein MbtL (PubMed:23935107). Shows a strong preference for palmitic acid (C16) and cannot use short-chain fatty acids (PubMed:23935107). Proceeds via a Bi Uni Uni Bi ping-pong mechanism. During the first half-reaction (adenylation), fatty acid binds first to the free enzyme, followed by ATP and the release of pyrophosphate to form the adenylate intermediate. During the second half-reaction (ligation), holo-MbtL binds to the enzyme followed by the release of products AMP and acylated MbtL (PubMed:23935107). {ECO:0000269|PubMed:23935107}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QUZ2 | MUTT1_MYCS2 | MMPVDDLQEIPLSKDTTEKSKHTVRAAGAVLWRDASEHGGTTGHPATVEVAVIHRPRYDDWSLPKGKLDQGETEPVAAAREIHEETGHTAVLGRRLGRVTYPIPQGTKRVWYWAAKSTGGDFSPNDEVDKLVWLPVDAAMDQLQYPDDRKVLRRFVKRPVDTKTVLVVRHGTAGRRSRYKGDDRKRPLDKRGRAQAEALVAQLMAFGATTLYAADRVRCHQTIEPLAQELDQLIHNEPLLTEEAYAADHKAARKRLLEIAGRPGNPVICTQGKVIPGLIEWWCERAKVRPETTGNRKGSTWVLSLSDGELVGADYLSPPDEK | 3.6.1.58; 3.6.1.61; 3.6.1.69 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:28375146, ECO:0000269|PubMed:28705712}; Note=Can also use Mn(2+), with lower efficiency. {ECO:0000269|PubMed:28705712}; | DNA repair [GO:0006281]; DNA replication [GO:0006260] | null | 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity [GO:0008413]; 8-oxo-dGDP phosphatase activity [GO:0044715]; 8-oxo-GDP phosphatase activity [GO:0044716]; metal ion binding [GO:0046872] | PF00300;PF00293; | 3.90.79.10;3.40.50.1240; | Nudix hydrolase family | null | null | CATALYTIC ACTIVITY: Reaction=8-oxo-dGTP + H2O = 8-oxo-dGDP + H(+) + phosphate; Xref=Rhea:RHEA:59980, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:63715, ChEBI:CHEBI:77896; EC=3.6.1.69; Evidence={ECO:0000269|PubMed:28375146}; CATALYTIC ACTIVITY: Reaction=8-oxo-GTP + H2O = 8-oxo-GDP + H(+) + phosphate; Xref=Rhea:RHEA:60032, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:143553, ChEBI:CHEBI:143554; EC=3.6.1.69; Evidence={ECO:0000269|PubMed:28375146}; CATALYTIC ACTIVITY: Reaction=8-oxo-dGDP + H2O = 8-oxo-dGMP + H(+) + phosphate; Xref=Rhea:RHEA:32063, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:63224, ChEBI:CHEBI:63715; EC=3.6.1.58; Evidence={ECO:0000269|PubMed:28375146}; CATALYTIC ACTIVITY: Reaction=8-oxo-GDP + H2O = 8-oxo-GMP + H(+) + phosphate; Xref=Rhea:RHEA:62356, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:143554, ChEBI:CHEBI:145694; EC=3.6.1.58; Evidence={ECO:0000269|PubMed:28375146}; CATALYTIC ACTIVITY: Reaction=H2O + P(1),P(6)-bis(5'-adenosyl) hexaphosphate = 2 ATP + 2 H(+); Xref=Rhea:RHEA:32043, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:63740; EC=3.6.1.61; Evidence={ECO:0000269|PubMed:28705712}; CATALYTIC ACTIVITY: Reaction=H2O + P(1),P(5)-bis(5'-adenosyl) pentaphosphate = ADP + ATP + 2 H(+); Xref=Rhea:RHEA:30527, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:62041, ChEBI:CHEBI:456216; EC=3.6.1.61; Evidence={ECO:0000269|PubMed:28705712}; CATALYTIC ACTIVITY: Reaction=H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = AMP + ATP + 2 H(+); Xref=Rhea:RHEA:32039, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58141, ChEBI:CHEBI:456215; EC=3.6.1.61; Evidence={ECO:0000269|PubMed:28705712}; | null | null | null | null | FUNCTION: Catalyzes the conversion of 8-oxo-dGTP to 8-oxo-dGDP, and 8-oxo-GTP to 8-oxo-GDP (PubMed:16585780, PubMed:28375146). At high enzyme concentrations, can also catalyze the conversion of 8-oxo-dGDP to 8-oxo-dGMP, and 8-oxo-GDP to 8-oxo-GMP (PubMed:28375146). In addition, catalyzes the hydrolysis of the diadenosine polyphosphates diadenosine hexaphosphate (Ap6A), diadenosine pentaphosphate (Ap5A) and diadenosine tetraphosphate (Ap4A) (PubMed:28705712). {ECO:0000269|PubMed:16585780, ECO:0000269|PubMed:28375146, ECO:0000269|PubMed:28705712}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QVH8 | RIP1_MYCS2 | MMFGIGIVLFALAILVSVALHECGHMWVARATGMKVRRYFVGFGPTLWSTRRANRLGSTEYGIKAIPLGGFCDIAGMTSVDEIAPEDRPYAMYKQKVWKRVAVLFAGPAMNFVIGLVLIYGIAIVWGLPNLHQPTTAIVGETGCVAPQITLEEMGECTGPGPAALAGIQAGDEIVKVGDTEVKDFAGMAAAVRKLDGPTRIEFKRDGRVMDTVVDVTPTQRFTSADASAPSTVGAIGVSAVPVQPPAQYNPITAVPATFAFTGDLAVELGKSLAKIPTKIGALVEAIGGGERDKETPISVVGASIIGGETVDAGLWVAFWFFLAQLNFVLGAINLVPLLPFDGGHIAVATYEKIRNMIRSARGMVAAGPVNYLKLMPATYVVLAVVAGYMLLTVTADLVNPLSIFQ | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; | proteolysis [GO:0006508] | plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF17820;PF02163; | 2.30.42.10; | Peptidase M50B family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: A probable intramembrane site-2 protease (S2P) that cleaves type-2 transmembrane proteins within their membrane-spanning domains. Degrades PbpB (PBP3, FtsI) under conditions of oxidatives stress; degradation is inhibited by Wag31-PbpB interaction. Also cleaves anti-sigma factors RskA, RslA and RslM. Site-1 proteases have not yet been identified in this organism.; FUNCTION: Regulated intramembrane proteolysis (RIP) occurs when an extracytoplasmic signal (possibly oxidative stress) triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein (includes anti-sigma factors RskA, RslA, RsmA, and PbpB) is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, this entry), while cytoplasmic proteases finish degrading the regulatory protein, liberating the effector protein (ECF sigma factors SigK, SigL and SigM). | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QWG5 | ACYLT_MYCS2 | MTLSGRIPLGGQVTDLGYAAGWRLVRAMPEAMAQGVFGAGARYAARNGGPEQLRRNLARVVGKPPADVPDDLIRASLASYARYWREAFRLPAMDHGRLGEQLDVIDIDHLWSALDAGRGAVLALPHSGNWDMAGVWLVQNYGPFTTVAERLKPESLYRRFVEYRESLGFEVLPLTGGERPPFEVLAERLTDNRPICLMAERDLTRSGVQVDFFGEATRMPAGPAKLAIETGAALFPVHCWFEGDGWGMRVYPELDTSSGDVTAITQALADRFAANIATYPADWHMLQPQWIADLSDERRARLGT | 2.3.1.265 | null | glycolipid biosynthetic process [GO:0009247]; phosphatidylinositol metabolic process [GO:0046488]; phospholipid biosynthetic process [GO:0008654] | plasma membrane [GO:0005886] | acyltransferase activity [GO:0016746] | PF03279; | null | LpxL/LpxM/LpxP family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:12851411, ECO:0000269|PubMed:26965057, ECO:0000269|PubMed:29185694}; Peripheral membrane protein {ECO:0000269|PubMed:26965057, ECO:0000269|PubMed:29185694}; Cytoplasmic side {ECO:0000269|PubMed:26965057, ECO:0000269|PubMed:29185694}. Note=Permanently associated with the membrane. {ECO:0000305|PubMed:29185694}. | CATALYTIC ACTIVITY: Reaction=a 2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + an acyl-CoA = 2-O-(alpha-D-mannosyl)-6-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA; Xref=Rhea:RHEA:52436, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:136624, ChEBI:CHEBI:136625; EC=2.3.1.265; Evidence={ECO:0000269|PubMed:24810911}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-[alpha-D-mannopyranosyl-(1<->6)-D-myo-inositol] + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phospho-[alpha-D-6-acyl-mannopyranosyl-(1<->6)-D-myo-inositol] + CoA; Xref=Rhea:RHEA:47412, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:87673, ChEBI:CHEBI:88053; EC=2.3.1.265; Evidence={ECO:0000269|PubMed:24810911}; | null | PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism. {ECO:0000269|PubMed:12851411}. | null | null | FUNCTION: Catalyzes the transfer of a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to the 2-position of myo-inositol in phosphatidyl-myo-inositol monomannoside (PIM1) or dimannoside (PIM2). {ECO:0000269|PubMed:12851411, ECO:0000269|PubMed:24810911, ECO:0000269|PubMed:26965057, ECO:0000269|PubMed:29185694}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QWG6 | PIMA_MYCS2 | MRIGMVCPYSFDVPGGVQSHVLQLAEVLRDAGHEVSVLAPASPHVKLPDYVVSGGKAVPIPYNGSVARLRFGPATHRKVKKWIAEGDFDVLHIHEPNAPSLSMLALQAAEGPIVATFHTSTTKSLTLSVFQGILRPYHEKIIGRIAVSDLARRWQMEALGSDAVEIPNGVDVASFADAPLLDGYPREGRTVLFLGRYDEPRKGMAVLLAALPKLVARFPDVEILIVGRGDEDELREQAGDLAGHLRFLGQVDDATKASAMRSADVYCAPHLGGESFGIVLVEAMAAGTAVVASDLDAFRRVLADGDAGRLVPVDDADGMAAALIGILEDDQLRAGYVARASERVHRYDWSVVSAQIMRVYETVSGAGIKVQVSGAANRDETAGESV | 2.4.1.345 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P9WMZ5}; | glycolipid biosynthetic process [GO:0009247]; phosphatidylinositol metabolic process [GO:0046488]; phospholipid biosynthetic process [GO:0008654]; sulfolipid biosynthetic process [GO:0046506] | plasma membrane [GO:0005886] | GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity [GO:0004377]; phosphatidylinositol alpha-mannosyltransferase activity [GO:0043750]; UDP-sulfoquinovose:DAG sulfoquinovosyltransferase activity [GO:0046510] | PF13692;PF13439; | 3.40.50.2000; | Glycosyltransferase group 1 family, Glycosyltransferase 4 subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:12068013, ECO:0000305|PubMed:19520856}; Peripheral membrane protein {ECO:0000305|PubMed:19520856}; Cytoplasmic side {ECO:0000305|PubMed:19520856}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + GDP-alpha-D-mannose = a 1,2-diacyl-sn-glycero-3-phospho-[alpha-D-mannopyranosyl-(1<->6)-D-myo-inositol] + GDP + H(+); Xref=Rhea:RHEA:47368, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:57880, ChEBI:CHEBI:58189, ChEBI:CHEBI:87673; EC=2.4.1.345; Evidence={ECO:0000269|PubMed:12068013, ECO:0000269|PubMed:19638342}; | null | PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism. {ECO:0000305|PubMed:19638342}. | null | null | FUNCTION: Involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM). Catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1) (PubMed:12068013, PubMed:19520856, PubMed:19638342). In contrary to PimB, the mannosyltransferase PimA is unable to transfer a mannose residue to the position 6 of the phosphatidyl-myo-inositol of PIM1 (PubMed:19638342). {ECO:0000269|PubMed:12068013, ECO:0000269|PubMed:19520856, ECO:0000269|PubMed:19638342}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QWS8 | IHF_MYCS2 | MALPQLTDEQRAAALEKAAAARRARAELKDRLKRGGTNLKQVLTDAETDEVLGKMKVSALLEALPKVGKVKAQEIMTELEIAPTRRLRGLGDRQRKALLEKFDQS | null | null | chromosome condensation [GO:0030261]; DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; symbiont entry into host cell [GO:0046718]; viral genome integration into host DNA [GO:0044826] | cytoplasm [GO:0005737]; nucleoid [GO:0009295] | DNA binding [GO:0003677] | null | 1.10.8.50; | Actinobacterial IHF (aIHF) family | null | SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:36960278}. Note=Found along the cell length in a bead-like pattern corresponding to DNA. Association with the chromosome is dynamic and responds to changes in DNA topology, colocalizes with HupB (hup). {ECO:0000269|PubMed:36960278}. | null | null | null | null | null | FUNCTION: A nucleoid-associated protein (NAP) that binds DNA without any sequence specificity (PubMed:31733417, PubMed:36960278, PubMed:8986825). Compacts DNA (PubMed:31733417). Binds along the whole chromosome in a dynamic manner, has equal affinity for the oriC site, attB and a randon 62% GC-rich sequence (PubMed:36960278). Plays a role in transcription regulation (By similarity). {ECO:0000250|UniProtKB:P71658, ECO:0000269|PubMed:31733417, ECO:0000269|PubMed:36960278, ECO:0000269|PubMed:8986825}.; FUNCTION: (Microbial infection) Stimulates temperate Mycobacterium phage L5 Int-mediated recombination in vitro using supercoiled attP (phage attachment site) DNA, linear attB DNA (bacterial attachment site) and L5 integrase (L5 Int or Int-L5, AC P22884). mIHF acts on L5 Int to stimulate formation of a specific intasome complex (PubMed:8986825, PubMed:9882658). mIHF probably stabilizes a sharp bend in the DNA during phage integration (PubMed:9882658). {ECO:0000269|PubMed:8986825, ECO:0000269|PubMed:9882658}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QWT2 | COABC_MYCS2 | MSARKRIVVGVAGGIAAYKACTVVRQLTEAGHSVRVVPTESALRFVGAATFEALSGNPVHTGVFTDVHEVQHVRIGQQADLVVIAPATADLLARAVAGRADDLLTATLLTARCPVLFAPAMHTEMWLHPATVDNVATLRRRGAVVLEPASGRLTGADSGPGRLPEAEEITTLAQLLLERADALPYDMAGVKALVTAGGTREPLDPVRFIGNRSSGKQGYAVARVLAQRGADVTLIAGNTAGLIDPAGVEMVHIGSATQLRDAVSKHAPDANVLVMAAAVADFRPAHVAAAKIKKGASEPSSIDLVRNDDVLAGAVRARADGQLPNMRAIVGFAAETGDANGDVLFHARAKLERKGCDLLVVNAVGENRAFEVDHNDGWLLSADGTESALEHGSKTLMATRIVDSIAAFLKSQDG | 4.1.1.36; 6.3.2.5 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_02225}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-Rule:MF_02225}; Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_02225}; | coenzyme A biosynthetic process [GO:0015937]; pantothenate catabolic process [GO:0015941] | phosphopantothenoylcysteine decarboxylase complex [GO:0071513] | FMN binding [GO:0010181]; metal ion binding [GO:0046872]; phosphopantothenate--cysteine ligase activity [GO:0004632]; phosphopantothenoylcysteine decarboxylase activity [GO:0004633] | PF04127;PF02441; | 3.40.50.10300;3.40.50.1950; | HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily; PPC synthetase family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine = (R)-4'-phosphopantetheine + CO2; Xref=Rhea:RHEA:16793, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:59458, ChEBI:CHEBI:61723; EC=4.1.1.36; Evidence={ECO:0000255|HAMAP-Rule:MF_02225}; CATALYTIC ACTIVITY: Reaction=(R)-4'-phosphopantothenate + CTP + L-cysteine = CMP + diphosphate + H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine; Xref=Rhea:RHEA:19397, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:35235, ChEBI:CHEBI:37563, ChEBI:CHEBI:59458, ChEBI:CHEBI:60377; EC=6.3.2.5; Evidence={ECO:0000255|HAMAP-Rule:MF_02225}; | null | PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5. {ECO:0000255|HAMAP-Rule:MF_02225}.; PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 3/5. {ECO:0000255|HAMAP-Rule:MF_02225}. | null | null | FUNCTION: Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine. {ECO:0000255|HAMAP-Rule:MF_02225}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QX20 | ACNA_MYCS2 | MSSENTGKSSLNSFGARDTLTVGDQSYEIYRLNAVPGTEKLPYSLKVLAENLLRTEDGANITKDHIEAIANWDPNAEPSIEIQFTPARVIMQDFTGVPCIVDLATMREAVAALGGDPNKVNPLAPAELVIDHSVILDVFGNASAFERNVELEYERNAERYQFLRWGQGAFDDFKVVPPGTGIVHQVNIEYLARTVMVRDGVAYPDTCVGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQPVSMLIPRVVGFKLSGEIKPGVTATDVVLTVTDMLRRHGVVGKFVEFYGKGVAEVPLANRATLGNMSPEFGSTAAIFPIDEETINYLRLTGRTDEQLALVEAYAKAQGMWHDPEREPVFSEYLELDLSTVVPSISGPKRPQDRIELTDAKNAFRKDIHNYVEQNHPTPETKLDEAVEESFPASDPVSLSFADDGAPDMRPSAANGATGRPTNPVLVHSEERGDFVLDHGAVVVAGITSCTNTSNPSVMLGAALLAKKAVEKGLTTKPWVKTNMAPGSQVVTDYYNKAGLWPYLEKLGYYLGGYGCTTCIGNTGPLPEEISKAINDNDLAVTAVLSGNRNFEGRISPDVKMNYLASPPLVIAYGIAGTMDFDFESDPLGQDSEGNDVFLRDIWPSAAEIEETIASSINREMFTESYADVFKGDDRWRSLPTPEGDTFEWDPASTYVRKAPYFDGMPAEPEPVSDIKGARVLALLGDSVTTDHISPAGAIKPGTPAAQYLDANGVERKDYNSLGSRRGNHEVMIRGTFANIRLRNQLLDDVSGGYTRDFTQPGGPQAFIYDASENYKKAGIPLVVLGGKEYGSGSSRDWAAKGTVLLGVKAVITESFERIHRSNLIGMGVIPLQFPAGESAASLKLDGTETYDIEGIEELNSGKTPKTVHVTATKEDGSKVEFDAVVRIDTPGEADYYRNGGILQYVLRNMLKSSK | 4.2.1.3; 4.2.1.99 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P09339}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250|UniProtKB:P09339}; | citrate metabolic process [GO:0006101]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829] | 2-methylisocitrate dehydratase activity [GO:0047456]; 4 iron, 4 sulfur cluster binding [GO:0051539]; aconitate hydratase activity [GO:0003994]; iron-responsive element binding [GO:0030350]; metal ion binding [GO:0046872]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729] | PF00330;PF00694; | 6.10.190.10;3.30.499.10;3.20.19.10; | Aconitase/IPM isomerase family | null | null | CATALYTIC ACTIVITY: Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336, ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3; Evidence={ECO:0000250|UniProtKB:O53166}; CATALYTIC ACTIVITY: Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377, ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99; Evidence={ECO:0000250|UniProtKB:Q8ZP52}; | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2. {ECO:0000250|UniProtKB:O53166}.; PATHWAY: Organic acid metabolism; propanoate degradation. {ECO:0000250|UniProtKB:O53166}. | null | null | FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA-binding regulatory protein. Could catalyze the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. {ECO:0000250|UniProtKB:O53166, ECO:0000250|UniProtKB:Q8ZP52}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QX22 | RIPA_MYCS2 | MRRTVRALATRVHGRVCAVPLVVGMLLATALYGGGPAAADPAAPDNLATLVAKVASADQKLQELGAAIQTQQETVNKAIVDVQAARDAAAAAQRELEAGQRGVADANAAIEAAQKRFDSFAAATYMNGPSRSYLTATDPADIVNTTATGQALIASSQQVMAKLQRARTEQVNRESAARLAKEKADQAARDAESSQDNAVAALKQAQQTFNAQQGELERLAAERAAAQAELDSVRKVSATGNAAPAAAPAAAPAPAAAPAPVPNSAPAPVPGAQPNPQAAAGNWDRAPSGPASSGQNWAVWDPTLPAIPSAFVSGDPIAIINAVLGIASTSAQVTADMGRSFLQKLGILPTPTGFTNGAIPRVYGREAVEYVIRRGMSQIGVPYSWGGGNAAGPSRGIDSGAGTVGFDCSGLMLYMFAGVGIKLDHYSGSQYNAGRKIPSSQMRRGDMIFYGPNASQHVAMYLGNGQMLEAPYTGSHVKVSPVRTSGMTPYVTRLIEY | 3.4.-.- | null | cell division [GO:0051301]; cell wall macromolecule catabolic process [GO:0016998]; cell wall organization [GO:0071555]; cell wall organization or biogenesis [GO:0071554]; peptidoglycan catabolic process [GO:0009253]; proteolysis [GO:0006508]; regulation of cell shape [GO:0008360] | extracellular region [GO:0005576] | cysteine-type peptidase activity [GO:0008234] | PF00877; | 6.10.250.3150;3.90.1720.10; | Peptidase C40 family | null | SUBCELLULAR LOCATION: Secreted. Note=Localizes to the septa. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Peptidoglycan endopeptidase that cleaves the bond between D-glutamate and meso-diaminopimelate. Binds and degrades high-molecular weight peptidoglycan. Required for normal separation of daughter cells after cell division and for cell wall integrity (By similarity). {ECO:0000250, ECO:0000269|PubMed:18463693}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QXD8 | ELTD_MYCS2 | MSNQVPEKMQAVVCHGPHDYRLEEVAVPQRKPGEALIRVEAVGICASDLKCYHGAAKFWGDENRPAWAETMVIPGHEFVGRVVELDDEAAQRWGIAVGDRVVSEQIVPCWECLFCKRGQYHMCQPHDLYGFKRRTPGAMASYMVYPAEALVHKVSPDIPAQHAAFAEPLSCSLHAVERAQITFEDTVVVAGCGPIGLGMIAGAKAKSPMRVIALDMAPDKLKLAEKCGADLTINIAEQDAEKIIKDLTGGYGADVYIEGTGHTSAVPQGLNLLRKLGRYVEYGVFGSDVTVDWSIISDDKELDVLGAHLGPYCWPAAIKMIESGALPMDEICTHQFPLTEFQKGLDLVASGKESVKVSLIPA | 1.1.1.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O58389}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:O58389}; | carbohydrate catabolic process [GO:0016052]; carbohydrate utilization [GO:0009758]; cellular response to carbohydrate stimulus [GO:0071322] | null | carbohydrate binding [GO:0030246]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616] | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=erythritol + NAD(+) = D-erythrulose + H(+) + NADH; Xref=Rhea:RHEA:48756, ChEBI:CHEBI:15378, ChEBI:CHEBI:16023, ChEBI:CHEBI:17113, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:26560079}; CATALYTIC ACTIVITY: Reaction=L-threitol + NAD(+) = H(+) + L-erythrulose + NADH; Xref=Rhea:RHEA:48760, ChEBI:CHEBI:15378, ChEBI:CHEBI:27913, ChEBI:CHEBI:42090, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:26560079}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.64 mM for L-threitol {ECO:0000269|PubMed:26560079}; KM=1.5 mM for erythritol {ECO:0000269|PubMed:26560079}; KM=1.47 mM for L-arabitol {ECO:0000269|PubMed:26560079}; KM=2.76 mM for xylitol {ECO:0000269|PubMed:26560079}; KM=2.21 mM for ribitol {ECO:0000269|PubMed:26560079}; KM=0.026 mM for D-erythrulose {ECO:0000269|PubMed:26560079}; KM=0.066 mM for L-erythrulose {ECO:0000269|PubMed:26560079}; KM=0.73 mM for D-xylulose {ECO:0000269|PubMed:26560079}; KM=0.25 mM for L-xylulose {ECO:0000269|PubMed:26560079}; KM=1.23 mM for ribulose {ECO:0000269|PubMed:26560079}; Note=kcat is 10.2 sec(-1) with L-threitol as substrate. kcat is 8.46 sec(-1) with erythritol as substrate. kcat is 8.73 sec(-1) with L-arabitol as substrate. kcat is 8.20 sec(-1) with xylitol as substrate. kcat is 6.56 sec(-1) with ribitol as substrate. kcat is 9.88 sec(-1) with D-erythrulose as substrate. kcat is 13.3 sec(-1) with L-erythrulose as substrate. kcat is 19.3 sec(-1) with D-xylulose as substrate. kcat is 7.75 sec(-1) with L-xylulose as substrate. kcat is 21.0 sec(-1) with ribulose as substrate. {ECO:0000269|PubMed:26560079}; | PATHWAY: Carbohydrate metabolism; erythritol degradation. {ECO:0000269|PubMed:26560079}.; PATHWAY: Carbohydrate metabolism; L-threitol degradation. {ECO:0000269|PubMed:26560079}. | null | null | FUNCTION: Catalyzes the NAD-dependent reversible oxidation of erythritol and L-threitol. Involved in the degradation pathways of erythritol and L-threitol, that allow M.smegmatis to grow on these compounds as the sole carbon source. {ECO:0000269|PubMed:26560079}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QXE4 | DERK_MYCS2 | MTKLFNDPARFTEDMLVGFLDANSRYVVGVPGGVVRAQTTRPGKVAVVIGGGSGHYPAFCGTVGPGFADGAVVGNIFTSPSAEEAASVARAAHSDAGVLLTTGNYAGDVMNFNLAVDQLRSEGIEAQYFAVTDDVASAERGQEAKRRGIAGDFTVFKCASAAAEEGLDLAGVVRVAEAANAATRTLGVAFDGCTLPGADHPLFTVPEGHMGLGLGIHGEPGVSEEKMPTAAGLAATLVDGVLGDRPDAPEKRIAVILNGLGRTKYEELFVVWGEVSRLLRDRGYTIVEPEVGELVTSLDMAGCSLTVMWLDEELERYWAAPADTPAYKKGAAQQHVSGERRSEATARSASSGPKLAELSDEDGRAGARLVARAFDAMAEALADAEEELGRIDAVAGDGDHGRGMVKGSSAAREAAASALSEGAGQGSVLNAAGKAWAAKAGGTSGVLWGALLTALGARLGDTGRPDSSVIAAGVRDAYDALIRLGGAAPGDKTMLDAMLPFTEELERRVAQDESWQSAWRAAADVATEAARATADLRPKIGRARPLAERSVGTPDAGATSLALCARTVADCVTLSTQGEN | 2.7.1.210 | null | carbohydrate catabolic process [GO:0016052]; carbohydrate utilization [GO:0009758]; cellular response to carbohydrate stimulus [GO:0071322]; glycerol catabolic process [GO:0019563] | cytosol [GO:0005829] | ATP binding [GO:0005524]; carbohydrate binding [GO:0030246]; carbohydrate kinase activity [GO:0019200]; glycerone kinase activity [GO:0004371] | PF02733;PF02734; | 1.25.40.340; | null | null | null | CATALYTIC ACTIVITY: Reaction=ATP + D-erythrulose = ADP + D-erythrulose 4-phosphate + H(+); Xref=Rhea:RHEA:48768, ChEBI:CHEBI:15378, ChEBI:CHEBI:16023, ChEBI:CHEBI:30616, ChEBI:CHEBI:90796, ChEBI:CHEBI:456216; EC=2.7.1.210; Evidence={ECO:0000269|PubMed:26560079}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.6 uM for D-erythrulose {ECO:0000269|PubMed:26560079}; KM=396 uM for L-erythrulose {ECO:0000269|PubMed:26560079}; KM=339 uM for dihydroxyacetone {ECO:0000269|PubMed:26560079}; Note=kcat is 2.88 sec(-1) with D-erythrulose as substrate. kcat is 0.091 sec(-1) with L-erythrulose as substrate. kcat is 0.063 sec(-1) with dihydroxyacetone as substrate. {ECO:0000269|PubMed:26560079}; | PATHWAY: Carbohydrate metabolism; erythritol degradation. {ECO:0000269|PubMed:26560079}.; PATHWAY: Carbohydrate metabolism; D-threitol degradation. {ECO:0000269|PubMed:26560079}. | null | null | FUNCTION: Catalyzes the phosphorylation of D-erythrulose to D-erythrulose-4P. Involved in the degradation pathways of erythritol and D-threitol, that allow M.smegmatis to grow on these compounds as the sole carbon source. {ECO:0000269|PubMed:26560079}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QXX7 | KATG2_MYCS2 | MSSDTSDSRPPNPDTKTASTSESENPAIPSPKPKSGAPLRNQDWWPNQIDVSRLHPHPPQGNPLGEDFDYAEEFAKLDVNALKADLTALMTQSQDWWPADYGHYGGLFIRMSWHSAGTYRIHDGRGGGGQGAQRFAPINSWPDNVSLDKARRLLWPIKQKYGNKISWADLLVFTGNVALESMGFKTFGFGFGREDIWEPEEILFGEEDEWLGTDKRYGGGEQRQLAEPYGATTMGLIYVNPEGPEGQPDPLAAAHDIRETFGRMAMNDEETAALIVGGHTFGKTHGAGDASLVGPEPEAAPIEQQGLGWKSSYGTGKGPDTITSGLEVVWTNTPTKWDNSFLEILYGYEWELTKSPAGAWQFTAKDGAGAGTIPDPFGGPGRNPTMLVTDISMRVDPIYGKITRRWLDHPEELSEAFAKAWYKLLHRDMGPISRYLGPWVAEPQLWQDPVPAVDHPLVDDQDIAALKSTVLDSGLSTGQLIKTAWASAASYRNTDKRGGANGARVRLEPQKNWDVNEPAELATVLPVLERIQQDFNASASGGKKVSLADLIVLAGSAAIEKAAKDGGYNVTVPFAPGRTDASQENTDVESFAVLEPRADGFRNYVRPGEKVQLEKMLLERAYFLGVTAPQLTALVGGLRALDVNHGGTKHGVFTDRPGALTNDFFVNLLDMGTEWKTSETTENVYEGVDRKTGQLKWTATANDLVFGSHSVLRAVAEVYAQSDNGERFVNDFVKAWVKVMNNDRFDLK | 1.11.1.21 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 2 heme B (iron-protoporphyrin IX) groups per tetramer.; | cellular response to hydrogen peroxide [GO:0070301]; hydrogen peroxide catabolic process [GO:0042744] | cytosol [GO:0005829] | catalase activity [GO:0004096]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00141; | 1.10.520.10;1.10.420.10; | Peroxidase family, Peroxidase/catalase subfamily | PTM: Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme. {ECO:0000255|HAMAP-Rule:MF_01961}. | null | CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01961}; CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01961}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 mM for H(2)O(2) for the catalase reaction {ECO:0000269|PubMed:7673210}; KM=0.19 mM for o-dianisidine for the peroxidase reaction {ECO:0000269|PubMed:7673210}; KM=0.17 mM for NADPH for the peroxidase reaction {ECO:0000269|PubMed:7673210}; KM=0.23 mM for NADH for the peroxidase reaction {ECO:0000269|PubMed:7673210}; KM=0.31 mM for pyrogallol for the peroxidase reaction {ECO:0000269|PubMed:7673210}; KM=0.11 mM for 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) for the peroxidase reaction {ECO:0000269|PubMed:7673210}; | null | null | null | FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. May play a role in the intracellular survival of mycobacteria. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QYC2 | DTHD_MYCS2 | MTQAQELSVDFDFRLDGKVALVTGAASGIGAAIASAYATKGARIAAVDLNAEGAEALAAQLGGDRGAHRGFACDVADAASVQAAADAVAAEFGRIDILVNSAGVARLAPAEELSLQDWDSTLAINLSGTFLMCQAVGKRMLEAGGGAIVNMASQAATVALDQHVAYCASKFGVVGVSKVLAAEWGGRGVRVNTISPTVVLTELGHKAWDGPRGDALKKLIPTGRFAYPDEIAAAAVFLASDAAAMINGADLVIDGGYTIK | 1.1.1.403 | null | carbohydrate catabolic process [GO:0016052]; carbohydrate utilization [GO:0009758]; cellular response to carbohydrate stimulus [GO:0071322] | null | carbohydrate binding [GO:0030246]; erythrulose reductase activity [GO:0047880] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=D-threitol + NAD(+) = D-erythrulose + H(+) + NADH; Xref=Rhea:RHEA:48748, ChEBI:CHEBI:15378, ChEBI:CHEBI:16023, ChEBI:CHEBI:48300, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.403; Evidence={ECO:0000269|PubMed:26560079}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.52 mM for D-threitol {ECO:0000269|PubMed:26560079}; KM=1.2 mM for D-threose {ECO:0000269|PubMed:26560079}; KM=0.048 mM for D-erythrulose {ECO:0000269|PubMed:26560079}; Note=kcat is 6.97 sec(-1) with D-threitol as substrate. kcat is 0.71 sec(-1) with D-threose as substrate. kcat is 7.32 sec(-1) with D-erythrulose as substrate. {ECO:0000269|PubMed:26560079}; | PATHWAY: Carbohydrate metabolism; D-threitol degradation. {ECO:0000269|PubMed:26560079}. | null | null | FUNCTION: Catalyzes the NAD-dependent reversible oxidation of D-threitol. Involved in the degradation pathway of D-threitol, that allows M.smegmatis to grow on this compound as the sole carbon source. Does not catalyze the oxidation of xylitol, L-sorbitol, and L-sorbose. {ECO:0000269|PubMed:26560079}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QYE8 | GUAB1_MYCS2 | MRFLDGHTPAYDLTYNDVFVVPGRSDVASRFDVDLSTVDGSGTTIPVVVANMTAVAGRRMAETVARRGGIVVLPQDLPITAVSETVDFVKSRDLVVDTPVTLSPEDSVSDANALLHKRAHGAAVVVFEGRPIGLVTEANCAGVDRFARVRDIALSDFVTAPVGTDPREVFDLLEHAPIDVAVMTAPDGTLAGVLTRTGAIRAGIYTPAVDAKGRLRIAAAVGINGDVGAKAQALAEAGADLLVIDTAHGHQAKMLDAIKAVASLDLGLPLVAGNVVSAEGTRDLIEAGASIVKVGVGPGAMCTTRMMTGVGRPQFSAVVECAAAARQLGGHVWADGGVRHPRDVALALAAGASNVMIGSWFAGTYESPGDLLFDRDDRPYKESYGMASKRAVAARTAGDSSFDRARKGLFEEGISTSRMSLDPARGGVEDLLDHITSGVRSTCTYVGAANLPELHEKVVLGVQSAAGFAEGHPLPAGW | 1.7.1.7 | COFACTOR: Name=a monovalent cation; Xref=ChEBI:CHEBI:60242; Evidence={ECO:0000255|HAMAP-Rule:MF_02250, ECO:0000269|PubMed:35338694}; Note=Activity is highest with Rb(+), followed by K(+), NH4(+) and Cs(+). {ECO:0000269|PubMed:35338694}; | IMP salvage [GO:0032264]; purine ribonucleoside salvage [GO:0006166] | cytosol [GO:0005829] | GMP reductase activity [GO:0003920]; IMP dehydrogenase activity [GO:0003938] | PF00571;PF00478; | 3.20.20.70; | IMPDH/GMPR family, GuaB1 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=IMP + NADP(+) + NH4(+) = GMP + 2 H(+) + NADPH; Xref=Rhea:RHEA:17185, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57783, ChEBI:CHEBI:58053, ChEBI:CHEBI:58115, ChEBI:CHEBI:58349; EC=1.7.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_02250, ECO:0000269|PubMed:35338694}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17187; Evidence={ECO:0000255|HAMAP-Rule:MF_02250, ECO:0000269|PubMed:35338694}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=30 uM for NADPH (at pH 7.8) {ECO:0000269|PubMed:35338694}; KM=63 uM for NADPH (at pH 6.6) {ECO:0000269|PubMed:35338694}; | PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway. {ECO:0000255|HAMAP-Rule:MF_02250, ECO:0000305|PubMed:35338694}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4-7.8. {ECO:0000269|PubMed:35338694}; | null | FUNCTION: Involved in the purine-salvage pathway (PubMed:35338694). Catalyzes the NADPH-dependent conversion of GMP to IMP (PubMed:35338694). Is not essential for viability, but may contribute to the regulation of the purine nucleotide pool by recycling GMP to IMP (PubMed:35338694). {ECO:0000269|PubMed:35338694}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QYV1 | LYSX_MYCS2 | MTVISRVEHLPARPASRVAWVPAAAGWTVGVIATLSLIASVSPLVRSLIRVPREFVNDFIFNFPDTSFAWAFVLALLAAALAARKRIAWWVLVLYLVGAIGWNVGDLAAGGDTVADDIGELIGIAFHVAAIVFLVVARKEFWAKVRRGALLKSAAVLVAGNLIGIVVAWGLLQAFPGTLDPEWRLPYAVNRVSGFATVPTEVFEGYSHTFLNAIFGLFGALALMAAAIVLFQSQRASNALTGEDESAIRGLLELYGKNDSLGYFATRRDKSVVFAPNGRAAITYRVEVGVCLASGDPVGDPKSWPQAIAAWLQLCQAYGWAPGVMGASLAGAEAYRAAGLNALQLGDEAILHPDRFRLSGPDMRAVRQAVTRARRAGTSVRIRRHRELSPEEMAAVIRRADAWRDTETERGFSMALGRLGDPADDDCLLVEAVQGDEVVAMLSLVPWGSNGVSLDVMRRSPRSPNGTIELMVSELCMQAEDIGISRISLNFAMFRSAFEQGAQLGAGPVARLWRALLVFFSKWWQLESLYRSNMKYQPEWVPRYACYEDARLVPRVGVASVIAEGFLVLPFSRRNKQHTGEHIAAPDTLVQSGRLHRDGSAPDVTGLQGELPDADDEPRLPEQVRVRMAKLKALQGNGVDAYPVGQPPSHTVAQALGATDGETLSVAGRVMRIRDYGGVLFAQLRDWSGEVQLLLDNAALTEGETADFTATIDLGDLVEVTGSMGFSRNGTRSLLVERWRLIGKCLRPLPDKWKGLTDQEARVRARYVDLAVNTEARDLIRARSGALHAIRETLYSKGFLEVETPILQQIHGGANARPFLTHINAYDLDLYLRIAPELYLKRLCVGGVERVFELGRAFRNEGVDFSHNPEFTLLEAYQAHADYNVWIDGCRELIQNAAQAANGAQVFLRPRPNDPAGTLEPVDISGQWAVKTVHDAVSEAIGEHITPETELGELRRLCDSAGIPYLTHWDAGAVVLEMYEHLVEDRTTEPTFYKDFPTSVSPLTRPHRSIPGVAERWDLVAWGVELGTAYSELTDPVEQRRRLQEQSLLAAGGDPEAMELDEDFLQAMEYAMPPTGGLGMGVDRVVMMITGRSIRETLPFPLAKPR | 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]; 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}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QZ13 | LNT_MYCS2 | MIPAVTDDDPLEDPLDDDVAPGLDDAEPEPEPRDEHDEPSRPATGSRIGGWVARRGSRFGKGVLDRCAPLSAAIGGGLALWLSFPPIGWWFTAFPGLALLGWVLTRTATTKAGGFGYGVLFGLAFYVPLLPWISGLVGAVPWLALAFAESLFCGLFGLGAVVVVRLPGWPLWFATLWVAAEWAKSTFPFGGFPWGASSYGQTNGPLLALARIGGAPLVSFAVALIGFSLTLLTAQIVWWWRHGHKPGVPAPAVMLPGVAIAASLLVTALVWPQVRQSGTGAGDDTAVTVAAVQGNVPRLGLEFNAQRRAVLDNHVKETLRLADDVKAGRAAQPMFVIWPENSSDIDPLLNADASAQITTAAEAIDAPILVGGVVRADGYTPDNPVANNTVIVWEPTDGPGERHDKQIVQPFGEYLPWRGFFKHLSSYADRAGYFVPGTGTGVVHAAGVPIGITTCWEVIFDRAARESVLNGAQVLAVPSNNATFDEAMSAQQLAFGKLRAVEHDRYVVVAGTTGISAVIAPDGHEISRTEWFQPAYLDNQIRLKTDLTPATKWGPIVQAVLVIAGVAVLLIAILHNGRFAPRMLRRRSATTVKR | 2.3.1.269 | null | lipoprotein biosynthetic process [GO:0042158] | plasma membrane [GO:0005886] | N-acyltransferase activity [GO:0016410] | PF00795;PF20154; | 3.60.110.10; | CN hydrolase family, Apolipoprotein N-acyltransferase subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000269|PubMed:12427759}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000269|PubMed:12427759}. | CATALYTIC ACTIVITY: Reaction=a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]; Xref=Rhea:RHEA:48228, Rhea:RHEA-COMP:14681, Rhea:RHEA-COMP:14684, ChEBI:CHEBI:15378, ChEBI:CHEBI:136912, ChEBI:CHEBI:140656, ChEBI:CHEBI:140657, ChEBI:CHEBI:140660; EC=2.3.1.269; Evidence={ECO:0000255|HAMAP-Rule:MF_01148}; | null | PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl transfer). {ECO:0000255|HAMAP-Rule:MF_01148}. | null | null | FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. Can transfer a number of fatty acids (C16 and C19, palmitic and probably tuberculostearic acids respectively are shown) (PubMed:19661058). Enhances the polyprenol monophosphomannose (PPM) synthase activity of Ppm1 (AC A0QZ12) without itself having PPM synthase catalytic activity (PubMed:12427759). {ECO:0000269|PubMed:12427759, ECO:0000269|PubMed:19661058}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QZ48 | PUP_MYCS2 | MAQEQTKRGGGGGEDDDLPGASAAGQERREKLTEETDDLLDEIDDVLEENAEDFVRAYVQKGGQ | null | null | modification-dependent protein catabolic process [GO:0019941]; proteasomal protein catabolic process [GO:0010498]; protein pupylation [GO:0070490] | null | proteasome binding [GO:0070628]; protein tag activity [GO:0031386] | PF05639; | null | Prokaryotic ubiquitin-like protein family | PTM: Is modified by deamidation of its C-terminal glutamine to glutamate probably by the deamidase Dop, a prerequisite to the subsequent pupylation process. {ECO:0000269|PubMed:19028679}. | null | null | null | PATHWAY: Protein degradation; proteasomal Pup-dependent pathway. | null | null | FUNCTION: Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation. Among the identified substrates are the SodA and Ino1 proteins. {ECO:0000269|PubMed:19028679}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QZ49 | DOP_MYCS2 | MQRIIGTEVEYGISSPSDPTANPILTSTQAVLAYAAAAGIQRAKRTRWDYEVESPLRDARGFDLSRSSGPPPIVDADEVGAANMILTNGARLYVDHAHPEYSAPECTDPMDAVIWDKAGERVMEAAARHVASVPGAAKLQLYKNNVDGKGASYGSHENYLMSRQTPFSAVIAGLTPFMVSRQVVTGSGRVGIGPSGDEPGFQLSQRADYIEVEVGLETTLKRGIINTRDEPHADADKYRRLHVIIGDANLAETSTYLKLGTTSLVLDLIEEGVDLSDLALARPVHAVHVISRDPSLRATVALADGRELTALALQRIYLDRVAKLVDSRDPDPRASHVIETWANVLDLLERDPMECAEILDWPAKLRLLEGFRQRENLTWQAPRLHLVDLQYSDVRLDKGLYNRLVARGSMKRLVTEQQVLDAVENPPTDTRAYFRGECLRRFGADIAAASWDSVIFDLGGDSLVRIPTLEPLRGSKAHVGALLDSVDSAVELVEQLTN | 3.4.-.-; 3.5.1.119 | COFACTOR: Name=ATP; Xref=ChEBI:CHEBI:30616; Evidence={ECO:0000269|PubMed:20025664}; Note=ATP is required for the deamidation reaction but is not hydrolyzed during this reaction. {ECO:0000269|PubMed:20025664}; | modification-dependent protein catabolic process [GO:0019941]; proteasomal protein catabolic process [GO:0010498]; protein pupylation [GO:0070490] | null | ATP binding [GO:0005524]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides [GO:0016811]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233] | PF03136; | null | Pup ligase/Pup deamidase family, Pup deamidase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=[prokaryotic ubiquitin-like protein]-C-terminal-L-glutamine + H2O = [prokaryotic ubiquitin-like protein]-C-terminal-L-glutamate + NH4(+); Xref=Rhea:RHEA:47952, Rhea:RHEA-COMP:11959, Rhea:RHEA-COMP:11960, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:78525, ChEBI:CHEBI:88115; EC=3.5.1.119; Evidence={ECO:0000269|PubMed:20025664}; | null | PATHWAY: Protein degradation; proteasomal Pup-dependent pathway. | null | null | FUNCTION: Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Probably also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; thus may be involved in the recycling of Pup and may function similarly to deubiquitinases (DUBs) in eukaryotes to prevent or promote proteasomal degradation of certain proteins. {ECO:0000269|PubMed:20025664}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QZY0 | MSHC_MYCS2 | MQSWSAPAIPVVPGRGPALRLFDSADRQVRPVTPGPTATMYVCGITPYDATHLGHAATYLTFDLVHRLWLDAGHTVQYVQNVTDVDDPLFERAERDGIDWRTLGDRETQLFREDMAALRVLPPHDYVAATDAIAEVVEMVEKLLASGAAYIVEDAEYPDVYFRADATAQFGYESGYDRDTMLTLFAERGGDPDRPGKSDQLDALLWRAERPGEPSWPSPFGRGRPGWHVECSAIALTRIGTGLDIQGGGSDLIFPHHEYSAAHAESVTGERRFARHYVHTGMIGWDGHKMSKSRGNLVLVSQLRAQGVDPSAIRLGLFSGHYREDRFWSNEVLDEANARLARWRSATALPEAPDATDVIARVRQYLADDLDTPKALAALDGWCTDALSYGGHDTESPRLVATTVDALLGVDL | 6.3.1.13 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; | cysteinyl-tRNA aminoacylation [GO:0006423]; mycothiol biosynthetic process [GO:0010125] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; cysteine-glucosaminylinositol ligase activity [GO:0035446]; cysteine-tRNA ligase activity [GO:0004817]; zinc ion binding [GO:0008270] | PF01406; | 1.20.120.640;3.40.50.620; | Class-I aminoacyl-tRNA synthetase family, MshC subfamily | null | null | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + ATP + L-cysteine = 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + AMP + diphosphate + H(+); Xref=Rhea:RHEA:26176, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:35235, ChEBI:CHEBI:58886, ChEBI:CHEBI:58887, ChEBI:CHEBI:456215; EC=6.3.1.13; Evidence={ECO:0000269|PubMed:12033919}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40 uM for L-cysteine {ECO:0000269|PubMed:12033919, ECO:0000269|PubMed:17848100}; KM=72 uM for GlcN-Ins {ECO:0000269|PubMed:12033919, ECO:0000269|PubMed:17848100}; KM=1.84 mM for ATP {ECO:0000269|PubMed:12033919, ECO:0000269|PubMed:17848100}; Vmax=83 nmol/min/mg enzyme {ECO:0000269|PubMed:12033919, ECO:0000269|PubMed:17848100}; | null | null | null | FUNCTION: Catalyzes the ATP-dependent condensation of GlcN-Ins and L-cysteine to form L-Cys-GlcN-Ins. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R066 | ILVE_MYCS2 | MNSGPLEFTVSANTNPATDAVRESILANPGFGKYYTDHMVSIDYTVDEGWHNAQVIPYGPIQLDPSAIVLHYGQEIFEGLKAYRWADGSIVSFRPEANAARLQSSARRLAIPELPEEVFIESLRQLIAVDEKWVPPAGGEESLYLRPFVIATEPGLGVRPSNEYRYLLIASPAGAYFKGGIKPVSVWLSHEYVRASPGGTGAAKFGGNYAASLLAQAQAAEMGCDQVVWLDAIERRYVEEMGGMNLFFVFGSGGSARLVTPELSGSLLPGITRDSLLQLATDAGFAVEERKIDVDEWQKKAGAGEITEVFACGTAAVITPVSHVKHHDGEFTIADGQPGEITMALRDTLTGIQRGTFADTHGWMARLN | 2.6.1.42 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:20445230}; | amino acid biosynthetic process [GO:0008652]; branched-chain amino acid metabolic process [GO:0009081]; isoleucine biosynthetic process [GO:0009097]; leucine biosynthetic process [GO:0009098]; protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine [GO:0018272]; valine biosynthetic process [GO:0009099] | null | branched-chain-amino-acid transaminase activity [GO:0004084]; L-isoleucine transaminase activity [GO:0052656]; L-leucine transaminase activity [GO:0052654]; L-leucine:2-oxoglutarate aminotransferase activity [GO:0050048]; L-valine transaminase activity [GO:0052655]; pyridoxal phosphate binding [GO:0030170] | PF01063; | 3.30.470.10;3.20.10.10; | Class-IV pyridoxal-phosphate-dependent aminotransferase family | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; | null | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.; PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. | null | null | FUNCTION: Catalyzes the reversible transfers of an amino group from glutamate to the alpha-ketoacid of the respective amino acid in the final step in the biosynthesis of branchedchain amino acids. The amino acids can be ranked in the following order with respect to their efficiency as amino donor: Leu > Ile > Val. {ECO:0000269|PubMed:20445230}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R0S4 | DPDS_MYCS2 | MATTRGKKTYPQLPPAPDDYPTFPDKSTWPVVFPEIPAGTNGRFARPPQHTSKAAAPKIPADQVPNHVAVVMDGNGRWATQRGLGRTEGHKMGEAVLIDITCGAIEIGIKHLTVYAFSTENWKRSTEEVRFLMGFNREVVRRRRENLNDMGVRMRWVGSRPRMWRSVIKEFDIAEQMTVDNDVITINYCVNYGGRTEIVEAARALAQEAVDGKINPARISEAMFAKHLHRADIPDVDLFIRTSGEQRASNFLLWQAAYAEYVFQDKLWPDYDRRDLWAACEEYVNRNRRFGRA | 2.5.1.86; 2.5.1.87 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250}; | polyprenol biosynthetic process [GO:0016094] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | dehydrodolichyl diphosphate synthase activity [GO:0045547]; di-trans,poly-cis-undecaprenyl-diphosphate synthase activity [GO:0008834]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; polyprenyltransferase activity [GO:0002094]; Z-farnesyl diphosphate synthase activity [GO:0033850] | PF01255; | 3.40.1180.10; | UPP synthase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11004176}. | CATALYTIC ACTIVITY: Reaction=(2Z,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate = (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E)-decaprenyl diphosphate + 7 diphosphate; Xref=Rhea:RHEA:47096, ChEBI:CHEBI:33019, ChEBI:CHEBI:87356, ChEBI:CHEBI:128769, ChEBI:CHEBI:162247; EC=2.5.1.86; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-trans,poly-cis-polyprenyl diphosphate + n diphosphate; Xref=Rhea:RHEA:53008, Rhea:RHEA-COMP:13431, ChEBI:CHEBI:33019, ChEBI:CHEBI:128769, ChEBI:CHEBI:136960, ChEBI:CHEBI:175763; EC=2.5.1.87; | null | null | null | null | FUNCTION: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) in the cis configuration with (2Z,6E)-farnesyl diphosphate (Z-FPP or EZ-FPP) generating the 50 carbon product trans,polycis-decaprenyl diphosphate. When (2E,6E)-farnesyl diphosphate (E-FPP or EE-FPP) is used in vitro, both primary products decaprenyl diphosphate and heptaprenyl diphosphate are synthesized. It is probably due to the fact that M.smegmatis synthesizes both (2E,6E,10E)-geranylgeranyl diphosphate (EEE-GGPP) and (2E,6E,10Z)-geranylgeranyl diphosphate (EEZ-GGPP). Can also accept many different allylic substrates, including E-geranyl diphosphate (E-GPP), neryl diphosphate (NPP), and all-trans-geranyl-geranyl diphosphate. {ECO:0000269|PubMed:11004176}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R0S7 | ERA_MYCS2 | MTEFRSGFVCFVGRPNTGKSTLTNALVGQKVAITSNRPQTTRHTIRGIVHREDFQIILVDTPGLHRPRTLLGQRLNDLVKDTYSEVDVIGMCIPADEAIGPGDRWIYQQIRAVAPRTTLIGIVTKIDKVPKDRVAAQLLAVSELMGPDAEIVPVSATSGEQLDVLTNVLVSQLPPGPAYYPDGELTDEPEEVLMAELIREAALEGVRDELPHSLAVVIDEVSQREDRDDLIDVHAILYVERDSQKGIVIGKGGARLREVGTAARKQIEKLLGTKVYLDLRVKIAKNWQRDPKQLGKLGF | null | null | ribosomal small subunit assembly [GO:0000028] | cytosol [GO:0005829]; envelope [GO:0031975]; extracellular region [GO:0005576] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; ribosomal small subunit binding [GO:0043024]; rRNA binding [GO:0019843] | PF07650;PF01926; | 3.30.300.20;3.40.50.300; | TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Era GTPase family | null | SUBCELLULAR LOCATION: Cell envelope {ECO:0000255|HAMAP-Rule:MF_00367}. Secreted, cell wall {ECO:0000255|HAMAP-Rule:MF_00367}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=285 uM for GTP {ECO:0000269|PubMed:35917161}; | null | null | null | FUNCTION: Exhibits GTPase activity (PubMed:35917161). Binds RNA but is probably not involved in ribosome assembly in mycobacteria (PubMed:35917161). Cannot use ATP (PubMed:35917161). {ECO:0000269|PubMed:35917161}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R152 | RNE_MYCS2 | MAEDAHTEDLSTQTPQQEGLPERLRVHSLARVLGTTSRRVLDALAEFDGRQRSAHSTVDKADAERVRAALTESPAAETPPEEAPAAETPVADLVVVQAEQVEVVTVSEAGPAEPAEPAEPEAPAAEAEAEAETEVADEAETPEPTFRGAVLVGDEPESRLILEHANIPPARETQTERPDYLPLFVAPQPVSFEPAVVDDEDEDDDTETGAESDFDSGADSDSDDDQADRPRRRRRGRRGRGRGRGEQNDDATSDADTDSTEDQTDGDEQESGEDSDDSGDEDSTTTEGGTRRRRRRRRRKSGSGDSDDAVSPDDPPNTVVHERAPRTERSDKSDDSEIQGISGSTRLEAKRQRRRDGRDAGRRRPPILSEAEFLARREAVERTMIVRDKVRTEPPHEGARYTQIAVLEDGVVVEHFVTSAASASLVGNIYLGIVQNVLPSMEAAFVDIGRGRNGVLYAGEVNWEAAGLGGQNRKIEQALKPGDYVVVQVSKDPVGHKGARLTTQVSLAGRYLVYVPGASSTGISRKLPDTERQRLKEILREVVPSDAGVIIRTASEGVKEEDIRSDVERLQKRWSEIEAKAAEVTEKKAGAAVALYEEPDVLVKVIRDLFNEDFSSLIVSGDEAWNTINSYVEAVAPDLMPRLTKYEPAGPDAPDVFAVHRIDEQLAKAMDRKVWLPSGGTLVIDRTEAMTVVDVNTGKFTGSGGNLEQTVTRNNLEAAEEIVRQLRLRDIGGIVVIDFIDMVLESNRDLVLRRLTEALARDRTRHQVSEVTSLGLVQLTRKRLGTGLVEAFSTACTHCGGRGIVLHGDPIDSASSNGGRKSDSSGGGGSGGGRRGKRGKKGAARTEEVHVAKVPDHTPGEHPMFKAMAAANGKHEGDEDHEDHEDHETAEDTTAAEVRDDTRDEHDADERAHVVTAAVGAAGDEDLDDSDEDSDLDSDEESDDESDEDEIELDDDEDELDEDIEVIGDSDDSDDSDDSDEDDDSDDSDDDSDEDEDSDSDEDEEPVREVYEPPVTAPRARVRRRAAARPAGPPSHD | 3.1.26.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P21513}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P21513}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P21513}; Note=Binds 2 Zn(2+) ions per homotetramer. Zinc ions are bound between subunits. {ECO:0000250|UniProtKB:P21513}; | mRNA processing [GO:0006397]; rRNA processing [GO:0006364]; tRNA processing [GO:0008033] | cytoplasm [GO:0005737] | metal ion binding [GO:0046872]; RNA nuclease activity [GO:0004540]; rRNA binding [GO:0019843]; tRNA binding [GO:0000049] | PF10150; | 1.10.10.2480;2.40.50.140; | RNase E/G family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:35521527}. Note=Has dynamic expression patterns, often present as foci near the mid-cell or new cell pole in addition to a weaker overall cytoplasmic distribution. Colocalizes with HupB (PubMed:35521527). {ECO:0000269|PubMed:35521527}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions.; EC=3.1.26.12; | null | null | null | null | FUNCTION: Endoribonuclease that plays a central role in RNA processing and decay. Plays a major role in pre-16S rRNA maturation, probably generating the mature 5'-end, and a minor role in pre-5S and pre-23S rRNA maturation (PubMed:22014150). Probably also processes tRNA (By similarity). RNase E and HupB jointly contribute to cellular adaptation to changing growth conditions and survival during antibiotic treatment. Overexpression or depletion leads to changes in gene expression; overexpression induces metabolic slowdown and cell stress while depleted strains grow less well than induced strains (PubMed:35521527). {ECO:0000250|UniProtKB:P21513, ECO:0000269|PubMed:22014150, ECO:0000269|PubMed:35521527}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R1E8 | PKS5_MYCS2 | MTQNCVAPVAIIGMACRLPGAINSPQQLWEALLRGDDFVTEIPTGRWDAEEYYDPEPGVPGRSVSKWGAFLDDPAAFDPEFFGITEREAAAIDPQHRLLLETAWEAVEHSGLNPAGLAGSATGVFMGLTHNDYAHLAADAKALEGPYGFTGTSFSLASGRIAYALGVHGPAITVDTACSSSLSAIHMACRSLHDGESDVALAGGVSVLLEPRKAAGGSAAGMLSPTGHCHAFDTAADGFVSAEGCVVLTLKRLDDAVADGDRILAVIRGTATNQDGRTVNIATPSADAQAKVYRMALKAAGVEPGTVGLVEAHGTGTPVGDPLEFSSLAEVYGTDGPCALGSIKTNFGHTQSAAGALGVMKAVLALQHNVIPQNLHFTRLPDQMAEIETGLFVPETITPWPVREGQPRRAAVSAYGLSGTNVHAVLEQAPESPAETAAEAISPKAGNALVFPVSASSADALRSTAQHLADWLLRSGDGNGRGPAIDLGDLAYTLARRRGFRAARSAVLAGDRGTLVEGLRQIADGEAMPQQAVTNDDRGPVWVFSGQGSQWASMGAELLDREPAFAAAIAELEPLIAAESDFSVTEALTASETVTGIDRVQPTIFAVQVALAAAMRSHGVVPGAVIGHSMGEVAASVVSGALSLEDGVKVICRRTRLMTRIAGSGAMAMVELPAQQVLSELASRGVDDVVLSVVASPQSTVVGGATASVRELIEMWESRGVMAREIAVDVASHSPQVDPILDDLIEALADLDPAEPEIPYYSATLYDPRDYADYDAYYWADNLRHTVRFSAAVQAALEDGHRVFAELSPHPLLTHPVEQTARSLDMPLAVFAAMRRQQEMPHGLLGFVADLHSAGAAVDFSVLYPTGRLLDAPLPAWTHSTLLLDRELESSAPGVPSVSVHPLLGSHVVLPQEPEEHLWQGDVGTEAHPWLSDHRVHQVAVLPGAAYCEMALAAVTPVLGDTGEVHDLKFHDMLLLDDATPVWVSAAVTAPGTAEFGVETHQSGDRTQRATAVLRGDVDAERPAAHSIDALLAAHPNRVDGDELRAGFGTVGIGHGAAFAGLSEAYVATAAEPTVVAAVALPGPLRSGQRGYTVHPALLDACFQSVIAHPEVQNIASGMLLPLGVRRLRAYGSTRNVRYCLSRIVKADSFGVEADLELLDADGTVLLSAMGLQLGTGNSDKAEEERLLDERLLTIEWQQRELPRPEGSETVDAGSWLVILAGDDDENPRAAGVVSALIGAGMPTTTMAWSHDADHDAQAAALTARLDEQPLAGVAVIVGDSETGTDAHDVGADARRGADHVRHLVRIARTLADAVGEPPRLYVVTHRSQHVLDTDEPYLEHSGLRGLIRVVGMEHPRLRATQIDVDDSTAHEALVRQLLSGSPEDETAWRDGQWYAARLCPSPLRAAERRTAVADNASEGMRLVVRNPGDLESMELVTFERGTPGPGQIEVAVKASSINFADVLVAFGRCPSFDGRLPELGSEFGGVVTAVGPGVTTHRVGDRVGGVSANGCWSNFVTCEADLATKLPEGISEHEAAAVGLAYGTVWLGLTELARMSAGDKILIHSATGGVGQAAIAVARAAGAEIYATAGSEKRRQLLRDWGIEHVYDSRTTAFADQIRTDTDGYGVDIVLNSVTGPAQRAGLELLAFGGRFVEIGKRDIYADTRLGLFPFRRNLSFYAVDLALMTVTHPQKIRDLLATVYRLIADGTLPLPEITHYPLEEAATAIRIMGGAQHTGKLVIDIPDTGQSQVVVPPEQVPVFRGDGAYVITGGLGGLGLFLAERMAAAGCGRIVVNSRSAPSTRSSEIIELIRATGADIVVECGDIAEPDTALRLVAAATQTGLPLRGVLHAAAVVEDATLANITDELVEHDWAPKVYGAWNLHQAVQSGGPATSELDWFCAFSSAAALVGSPGQGAYAAANSWLDAFMQWRRAQGLPATSIAWGAWGEIGRGTAMAEGDNAIAPDEGAYAFEAILRHDRVYNGYAPVLGASWLTAFAQRSPFAELFLADTQGASETRKLRSELAALPREEWPTHLRRLIAEQVGLLLRRTVDPDRPLSEYGLDSLGHLELRTRIETETGVRVSAMDMTTIRGLAQRLCEMLDTDDAVSAPS | 2.3.1.- | null | DIM/DIP cell wall layer assembly [GO:0071770]; fatty acid biosynthetic process [GO:0006633]; secondary metabolite biosynthetic process [GO:0044550] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF08240;PF13602;PF16197;PF00109;PF02801;PF08659;PF21089;PF00550;PF14765; | 3.40.47.10;1.10.1200.10;3.30.70.250;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. | null | null | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000269|PubMed:19181796}. | null | null | FUNCTION: Polyketide synthase involved in the biosynthesis of 2,4-dimethyl-2-eicosenoic acid, a lipid component of the lipooligosaccharides (LOS) which are not located at the bacterial surface but rather in deeper compartments of the cell envelope of M.smegmatis. {ECO:0000269|PubMed:19181796}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R2B1 | KGD_MYCS2 | MSSSPSPFGQNEWLVEEMYRKFRDDPSSVDPSWHEFLVDYSPEPTTDSASNGRTTTAAPVTPPTPAPAPAPEPKAAPKPAAKTEAKPAKPAKSATPAKGDESQILRGAAAAVVKNMNASLEVPTATSVRAIPAKLMIDNRVVINNHLKRTRGGKISFTHLLGYAIVQAVKKFPNMNRHFAVVDGKPTAITPAHTNLGLAIDLQGKDGNRSLVVAAIKRCETMRFGQFIAAYEDIVRRARDGKLTAEDFSGVTISLTNPGTLGTVHSVPRLMQGQGAIIGAGAMEYPAEFQGASEERIADLGIGKLITLTSTYDHRIIQGAESGDFLRTIHQLLLDDDFFDEIFRELGIPYEPVRWRTDNPDSIEDKNARVIELIAAYRNRGHLMADIDPLRLDNTRFRSHPDLDVNSHGLTLWDLDREFKVDGFAGVQRKKLRDILSVLRDAYCRHVGVEYTHILEPEQQRWIQERVETKHDKPTVAEQKYILSKLNAAEAFETFLQTKYVGQKRFSLEGAETVIPMMDAVIDQCAEHGLDEVVIAMPHRGRLNVLANIVGKPYSQIFSEFEGNLNPSQAHGSGDVKYHLGATGTYIQMFGDNDIEVSLTANPSHLEAVDPVLEGLVRAKQDLLDTGEEGSDNRFSVVPLMLHGDAAFAGQGVVAETLNLALLRGYRTGGTIHIVVNNQIGFTTAPTDSRSSEYCTDVAKMIGAPIFHVNGDDPEACAWVARLAVDFRQAFKKDVVIDMLCYRRRGHNEGDDPSMTQPYMYDVIDTKRGSRKAYTEALIGRGDISMKEAEDALRDYQGQLERVFNEVRELEKHEIEPSESVEADQQIPSKLATAVDKAMLQRIGDAHLALPEGFTVHPRVRPVLEKRREMAYEGRIDWAFAELLALGSLIAEGKLVRLSGQDTQRGTFTQRHAVIVDRKTGEEFTPLQLLATNPDGTPTGGKFLVYNSALSEFAAVGFEYGYSVGNPDAMVLWEAQFGDFVNGAQSIIDEFISSGEAKWGQLSDVVLLLPHGHEGQGPDHTSGRIERFLQLWAEGSMTIAMPSTPANYFHLLRRHGKDGIQRPLIVFTPKSMLRNKAAVSDIRDFTESKFRSVLEEPMYTDGEGDRNKVTRLLLTSGKIYYELAARKAKENREDVAIVRIEQLAPLPRRRLAETLDRYPNVKEKFWVQEEPANQGAWPSFGLTLPEILPDHFTGLKRISRRAMSAPSSGSSKVHAVEQQEILDTAFG | 1.2.4.2; 2.2.1.5; 2.3.1.61; 4.1.1.71 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21867916}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000269|PubMed:21867916}; | tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; oxoglutarate dehydrogenase complex [GO:0045252] | 2-hydroxy-3-oxoadipate synthase activity [GO:0050439]; 2-oxoglutarate decarboxylase activity [GO:0008683]; dihydrolipoyllysine-residue succinyltransferase activity [GO:0004149]; magnesium ion binding [GO:0000287]; oxoglutarate dehydrogenase (succinyl-transferring) activity [GO:0004591]; thiamine pyrophosphate binding [GO:0030976] | PF00198;PF16078;PF00676;PF16870;PF02779; | 3.40.50.12470;3.40.50.970;3.30.559.10;3.40.50.11610;1.10.287.1150; | 2-oxoacid dehydrogenase family, Kgd subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + glyoxylate + H(+) = 2-hydroxy-3-oxoadipate + CO2; Xref=Rhea:RHEA:14341, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:36655, ChEBI:CHEBI:57712; EC=2.2.1.5; Evidence={ECO:0000269|PubMed:21867916}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) = CO2 + succinate semialdehyde; Xref=Rhea:RHEA:10524, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:57706; EC=4.1.1.71; Evidence={ECO:0000269|PubMed:21867916}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2; Evidence={ECO:0000269|PubMed:21867916}; CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61; Evidence={ECO:0000269|PubMed:21867916}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.54 mM for alpha-ketoglutarate {ECO:0000269|PubMed:19019160}; | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from 2-oxoglutarate (transferase route): step 1/2. {ECO:0000269|PubMed:21867916}.; PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1. {ECO:0000269|PubMed:21867916}. | null | null | FUNCTION: Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutarate to four-carbon succinate semialdehyde (SSA). Also catalyzes C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate dehydrogenase (ODH) complex, that catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The KG decarboxylase and KG dehydrogenase reactions provide two alternative, tightly regulated, pathways connecting the oxidative and reductive branches of the TCA cycle. {ECO:0000269|PubMed:19019160, ECO:0000269|PubMed:21867916}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R2E6 | GPGS_MYCS2 | MGHRWLTDHSWNRPSWTVADLEAAKAGRTVSVVLPALNEEETVGSVVETIKPLLGGLVDELIVLDSGSTDETEIRAVAAGAKVVSREAALPEVPPQPGKGEVLWRSLAATTGDIIAFVDSDLIDPDPMFVPKLLGPLLTCDGVHLVKGFYRRPLKVSGAEDANGGGRVTELVARPLLASLRPELNCVLQPLGGEYAGTRELLTSVPFAPGYGVEIGLLVDTYDRLGLDGIAQVNLGVRAHRNRPLTELASMSRQVIATLLSRCGISDSGVGLTQFFADGDDFTPRVSSVSLADRPPMTTLRPR | 2.4.1.266 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:18221489}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P9WMW9}; Note=Requires divalent cations for activity. The maximum activity is observed at 20 mM of MgCl(2). {ECO:0000269|PubMed:18221489}; | null | null | glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872] | PF00535; | 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:18221489}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47245; Evidence={ECO:0000305|PubMed:18221489}; CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + UDP-alpha-D-glucose = (2R)-2-O-(alpha-D-glucopyranosyl)-3-phospho-glycerate + H(+) + UDP; Xref=Rhea:RHEA:31319, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58272, ChEBI:CHEBI:58885, ChEBI:CHEBI:62600; EC=2.4.1.266; Evidence={ECO:0000269|PubMed:18221489}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31320; Evidence={ECO:0000305|PubMed:18221489}; CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + ADP-alpha-D-glucose = (2R)-2-O-(alpha-D-glucopyranosyl)-3-phospho-glycerate + ADP + H(+); Xref=Rhea:RHEA:31311, ChEBI:CHEBI:15378, ChEBI:CHEBI:57498, ChEBI:CHEBI:58272, ChEBI:CHEBI:62600, ChEBI:CHEBI:456216; EC=2.4.1.266; Evidence={ECO:0000269|PubMed:18221489}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31312; Evidence={ECO:0000305|PubMed:18221489}; CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + GDP-D-glucose = (2R)-2-O-(alpha-D-glucopyranosyl)-3-phospho-glycerate + GDP + H(+); Xref=Rhea:RHEA:31315, ChEBI:CHEBI:15378, ChEBI:CHEBI:58127, ChEBI:CHEBI:58189, ChEBI:CHEBI:58272, ChEBI:CHEBI:62600; EC=2.4.1.266; Evidence={ECO:0000269|PubMed:18221489}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31316; Evidence={ECO:0000305|PubMed:18221489}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.24 mM for 3-PGA (at 37 degrees Celsius) {ECO:0000269|PubMed:18221489}; KM=1.28 mM for UDP-glucose (at 37 degrees Celsius) {ECO:0000269|PubMed:18221489}; KM=6.08 mM for ADP-glucose (at 37 degrees Celsius) {ECO:0000269|PubMed:18221489}; KM=32.04 mM for GDP-glucose (at 37 degrees Celsius) {ECO:0000269|PubMed:18221489}; Vmax=2.45 umol/min/mg enzyme towards GDP-glucose {ECO:0000269|PubMed:18221489}; Vmax=25.91 umol/min/mg enzyme towards 3-PGA {ECO:0000269|PubMed:18221489}; Vmax=26.23 umol/min/mg enzyme towards ADP-glucose {ECO:0000269|PubMed:18221489}; Vmax=27.51 umol/min/mg enzyme towards UDP-glucose {ECO:0000269|PubMed:18221489}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:18221489}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. The activity is undetectable below 20 and above 55 degrees Celsius. {ECO:0000269|PubMed:18221489}; | FUNCTION: Involved in the biosynthesis of 6-O-methylglucose lipopolysaccarides (MGLPs) (PubMed:18221489, PubMed:19421329). Catalyzes the transfer of the glucose moiety from a nuleotide sugar such as UDP-alpha-D-glucose to the position 2 of 3-phospho-D-glycerate (3-PGA) to form glucosyl-3-phosphoglycerate (GPG). It can use UDP-glucose, ADP-glucose and GDP-glucose as sugar donor substrates with decreasing affinity and with 3-PGA as an acceptor. D-glycerate can only be an acceptor with ADP-glucose and at a very low rate (PubMed:18221489). {ECO:0000269|PubMed:18221489, ECO:0000269|PubMed:19421329}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R2K8 | PIME_MYCS2 | MRVNGYRGAKVGAVDTTSPPEVPASARLQRLAPMLLVVSILARLAWTYLVPNGANFVDLHVYVGGADALDGPGALYDYVYADQTPDFPLPFTYPPFAAIVFYPLHLLPFGVVAFIWQIGIIAALYGVVRVSQRLMGLQSQRRVAMLWTALGIWTEPLRSTFDYGQVNVVLVLAVLCAVSTTRWWLSGLLVGLAAGIKLTPAVAGLYFLGARRWAAVACSAAVFFATVGVSWLVVGAQARRYFTELLGDADRIGPIGTSFNQSWRGGISRILGHDAGFGPLVLIGIGITAVLALLAWRAIGGAQDRLGGILVVSLFGLVLSPISWTHHWVWLIPLMMWLLHGPLSALRGARILGWGWLALTLLGVPWLLSFAQPTIWEIGRPWYLAWAGLVYIVATLATLGWIAFSRKGSG | 2.4.1.- | null | glycolipid biosynthetic process [GO:0009247]; phosphatidylinositol metabolic process [GO:0046488]; phospholipid biosynthetic process [GO:0008654] | plasma membrane [GO:0005886] | GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity [GO:0004377]; phosphatidylinositol alpha-mannosyltransferase activity [GO:0043750] | PF09594; | null | Glycosyltransferase 87 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16803893}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in the plasma membrane-cell wall (PM-CW) fraction. {ECO:0000269|PubMed:16803893}. | null | null | PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism. {ECO:0000269|PubMed:16803893}. | null | null | FUNCTION: Catalyzes the alpha-1,2 addition of a mannose residue from polyprenol-phosphate-mannose (PPM) to a monoacyl phosphatidylinositol tetramannoside (AcPIM4) to generate a monoacyl phosphatidylinositol pentamannoside (AcPIM5). {ECO:0000269|PubMed:16803893}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R2N3 | NDP_MYCS2 | MQVTVLSGAGISAESGVPTFRDAETGLWAQVDPYEISSTDGWQRNPEKVWAWYLWRHYMMARVAPNEAHRTVAAWEDHLDVRVVTQNIDDLHERAGSTNVYHLHGSLFEFRCDACGSAFEGNLPEMPEPVETIDPPVCPCSGLIRPSVVWFGEPLPDAAWNRSVLAVSSADVVIVVGTSSIVYPAAGLPEAALAAGKPVIEVNPERTPLSDSATVSLRETASEALPTLLQRLPELLNRSA | 2.3.1.286 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01121}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01121}; | cellular response to ionizing radiation [GO:0071479]; double-strand break repair via nonhomologous end joining [GO:0006303] | cytoplasm [GO:0005737] | NAD+ binding [GO:0070403]; NAD-dependent histone deacetylase activity [GO:0017136]; protein-malonyllysine demalonylase activity [GO:0036054]; protein-succinyllysine desuccinylase activity [GO:0036055]; transferase activity [GO:0016740]; zinc ion binding [GO:0008270] | PF02146; | 3.30.1600.10;3.40.50.1220; | Sirtuin family, Class III subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01121}. | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-succinyl-L-lysyl-[protein] + NAD(+) = 2''-O-succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:47668, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11877, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:87830, ChEBI:CHEBI:87832; Evidence={ECO:0000255|HAMAP-Rule:MF_01121}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=2.3.1.286; Evidence={ECO:0000255|HAMAP-Rule:MF_01121}; | null | null | null | null | FUNCTION: NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. {ECO:0000255|HAMAP-Rule:MF_01121}.; FUNCTION: Involved in non-homologous end joining (NHEJ) repair of blunt, 5' overhang and 3' overhang DNA double strand breaks (DSB). Overexpression increases the efficiency of NHEJ of the above DSBs 2-fold with no effect on repair fidelity. {ECO:0000269|PubMed:21637345}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R3C4 | MAZG_MYCS2 | MIVVLVDPRRPALVPVDAVEFLTGDVQYTEEMPVKVPWSLPSARPAYDGEDAPVLLSSDPEHPVVKARLAAGDRLIAAPEPQPGERLVDAVALMDKLRTSGPWESEQTHDSLRRYLLEETYELFDAVRSGNADELREELGDVLLQVLFHARIAEDAPHHPFSIDDVADALVRKLGNRVPAVLAGESISLDEQLAQWEERKAQEKKVKARASSMDDVPTGQPALALAQKVLARVSQAGLPAELIPASLTSVSVSADTDSENELRTAVLEFMDTVREVEAAVAAGRRGEDVPEELDVAPLGVISEDEWRAYWPGAESSASEAEPEE | 3.6.1.8 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | dATP catabolic process [GO:0046061]; dGTP catabolic process [GO:0006203]; dTTP catabolic process [GO:0046076]; dUTP catabolic process [GO:0046081]; TTP catabolic process [GO:0046047]; UTP catabolic process [GO:0046052] | null | ATP binding [GO:0005524]; ATP diphosphatase activity [GO:0047693]; metal ion binding [GO:0046872] | PF03819; | 1.10.287.1080; | Nucleoside triphosphate pyrophosphohydrolase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + H2O = AMP + diphosphate + H(+); Xref=Rhea:RHEA:14245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:456215; EC=3.6.1.8; Evidence={ECO:0000269|PubMed:20529853}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.16 mM for 8-oxo-dGTP (at pH 9.6 and at 37 degrees Celsius in the presence of 5 mM magnesium) {ECO:0000269|PubMed:20529853}; KM=0.9 mM for GTP (at pH 9.6 and at 37 degrees Celsius in the presence of 5 mM magnesium) {ECO:0000269|PubMed:20529853}; Vmax=0.16 nmol/min/ug enzyme for 8-oxo-dGTP (at pH 9.6 and at 37 degrees Celsius in the presence of 5 mM magnesium) {ECO:0000269|PubMed:20529853}; Vmax=3.1 nmol/min/ug enzyme for GTP (at pH 9.6 and at 37 degrees Celsius in the presence of 5 mM magnesium) {ECO:0000269|PubMed:20529853}; | null | null | null | FUNCTION: Required to maintain the full capacity of the mycobacteria to respond to oxidative stress via the degradation of the oxidation-induced damaged nucleotides. It hydrolyzes all canonical (d)NTPs, as well as the mutagenic dUTP and 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate (8-oxo-dGTP). Also involved in the transcriptional activation of RelA in response to oxidative stress. {ECO:0000269|PubMed:20529853}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R3F9 | PAT_MYCS2 | MAELTEVRAADLAALEFFTGCRPSALEPLATQLRPLKAEPGQVLIRQGDPALTFMLIESGRVQVSHAVADGPPIVLDIEPGLIIGEIALLRDAPRTATVVAAEPVIGWVGDRDAFDTILHLPGMFDRLVRIARQRLAAFITPIPVQVRTGEWFYLRPVLPGDVERTLNGPVEFSSETLYRRFQSVRKPTRALLEYLFEVDYADHFVWVMTEGALGPVIADARFVREGHNATMAEVAFTVGDDYQGRGIGSFLMGALIVSANYVGVQRFNARVLTDNMAMRKIMDRLGAVWVREDLGVVMTEVDVPPVDTVPFEPELIDQIRDATRKVIRAVSQ | 2.3.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | cGMP-mediated signaling [GO:0019934] | null | 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; metal ion binding [GO:0046872]; N-acetyltransferase activity [GO:0008080] | PF13302;PF00027; | 3.40.630.30;2.60.120.10; | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.1 uM for acetyl-CoA (with ACS as substrate) {ECO:0000269|PubMed:20507997, ECO:0000269|PubMed:21627103}; KM=10 uM for acetyl-CoA (with USP as substrate) {ECO:0000269|PubMed:20507997, ECO:0000269|PubMed:21627103}; KM=10.2 uM for ACS {ECO:0000269|PubMed:20507997, ECO:0000269|PubMed:21627103}; KM=335 uM for USP {ECO:0000269|PubMed:20507997, ECO:0000269|PubMed:21627103}; | null | null | null | FUNCTION: Catalyzes specifically the acetylation of the epsilon-amino group of a highly conserved lysine residue in acetyl-CoA synthetase (ACS) and of the universal stress protein (USP) MSMEG_4207. Acetylation results in the inactivation of ACS activity and could be important for mycobacteria to adjust to environmental changes. {ECO:0000269|PubMed:20507997, ECO:0000269|PubMed:21627103}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R3R7 | LIGD_MYCS2 | MARHPWGMERYERVRLTNPDKVLYPATGTTKAEVFDYYLSIAQVMVPHIAGRPVTRKRWPNGVAEEAFFEKQLASSAPSWLERGSITHKSGTTTYPIINTREGLAWVAQQASLEVHVPQWRFEDGDQGPATRIVFDLDPGEGVTMTQLCEIAHEVRALMTDLDLETYPLTSGSKGLHLYVPLAEPISSRGASVLARRVAQQLEQAMPKLVTATMTKSLRAGKVFLDWSQNNAAKTTIAPYSLRGRDHPTVAAPRTWDEIADPELRHLRFDEVLDRLDEYGDLLAPLDADAPIADKLTTYRSMRDASKTPEPVPKEIPKTGNNDKFVIQEHHARRLHYDLRLERDGVLVSFAVPKNLPETTAENRLAVHTEDHPIEYLAFHGSIPKGEYGAGDMVIWDSGSYETEKFRVPEELDNPDDSHGEIIVTLHGEKVDGRYALIQTKGKNWLAHRMKDQKNARPEDFAPMLATEGSVAKYKAKQWAFEGKWDGYRVIIDADHGQLQIRSRTGREVTGEYPQFKALAADLAEHHVVLDGEAVALDESGVPSFGQMQNRARSTRVEFWAFDILWLDGRSLLRAKYSDRRKILEALADGGGLIVPDQLPGDGPEAMEHVRKKRFEGVVAKKWDSTYQPGRRSSSWIKDKIWNTQEVVIGGWRQGEGGRSSGIGALVLGIPGPEGLQFVGRVGTGFTEKELSKLKDMLKPLHTDESPFNAPLPKVDARGVTFVRPELVGEVRYSERTSDGRLRQPSWRGLRPDKTPDEVVWE | 6.5.1.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 4 Mn(2+); 2 Mn(2+) for polymerase/primase activity, 1 each for 3-phosphoesterase and ligase. {ECO:0000250}; | DNA recombination [GO:0006310]; double-strand break repair via nonhomologous end joining [GO:0006303] | null | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA ligase (ATP) activity [GO:0003910]; DNA-directed DNA polymerase activity [GO:0003887]; exonuclease activity [GO:0004527]; metal ion binding [GO:0046872] | PF04679;PF01068;PF13298;PF21686; | 3.30.1490.70;3.30.470.30;3.90.920.10;2.40.50.140; | LigD polymerase family; LigD 3'-phosphoesterase family; ATP-dependent DNA ligase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.1; | null | null | null | null | FUNCTION: With Ku forms a non-homologous end joining (NHEJ) repair enzyme which repairs blunt-end and 5'-overhang DNA double strand breaks (DSB) with about 50% fidelity, and DSB with non-complementary 3' ends. Plays a partial role in NHEJ during 3'-overhang repair. NHEJ repairs DSB with blunt ends and 5' overhangs with a high level of nucleotide insertion/deletion, without a need for microhomology. Acts as a DNA ligase on singly nicked dsDNA, as a DNA-directed DNA polymerase on 5' overhangs, and adds non-templated nucleotides to 3' overhangs (terminal transferase). Fills in gaps in dsDNA, prefers a 5'-phosphate in the gap. Site-directed mutations leading to ligase loss alter the bias from insertion to deletion mutations, and indicate another ligase (LigC1 and/or LigC2) can compensate.; FUNCTION: The preference of the polymerase domain for rNTPs over dNTPs may be advantageous in dormant cells, where the dNTP pool may be limiting. {ECO:0000250, ECO:0000269|PubMed:15778718, ECO:0000269|PubMed:16446439, ECO:0000269|PubMed:16476729, ECO:0000269|PubMed:16949369, ECO:0000269|PubMed:17174332, ECO:0000269|PubMed:17360246, ECO:0000269|PubMed:18281464}.; FUNCTION: The ligase activity is required for replication of viruses with short cos ends (4 bases) such as Mycobacterium phage Omega and Corndog, but not D29 which has a 9 base cos end. Stimulates dsDNA end joining by LigD; when expressed with endogenous or Mycobacterium phage Omega Ku, can reconstitute NHEJ in S.cerevisiae. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R4M9 | OTSA_MYCS2 | MSPESGHETISGTSDFVVVANRLPVDLERLPDGTTRWKRSPGGLVTALEPLLRKRRGSWIGWAGVADSDEEPIVQDGLQLHPVRLSADDVAKYYEGFSNATLWPLYHDLIVKPEYHREWWDRYVEVNRRFAEATARAAAEGATVWIQDYQLQLVPKMLRMLRPDVTIGFFLHIPFPPVELFMQMPWRTEIVEGLLGADLVGFHLPGGAQNFLVLSRRLVGANTSRASIGVRSRFGEVQVGFRTVKVGAFPISIDSAELDGKARNRAIRQRARQIRAELGNPRKIMLGVDRLDYTKGIDVRLRALSELLEEKRIKRDDTVLVQLATPSRERVESYIAMREDIERQVGHINGEYGEVGHPIVHYLHRPIPRDELIAFFVAADVMLVTPLRDGMNLVAKEYVACRSDLGGALVLSEFTGAAAELRQAYLVNPHDLEGVKDKIEAAVNQNPEEGKRRMRALRRQVLAHDVDRWARSFLDALAATGETGDSGVTGESTPAPESDSGSF | 2.4.1.15; 2.4.1.347 | null | cellular response to heat [GO:0034605]; trehalose biosynthetic process [GO:0005992]; trehalose metabolism in response to stress [GO:0070413] | alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) [GO:0005946]; cytosol [GO:0005829] | alpha,alpha-trehalose-phosphate synthase (GDP-forming) activity [GO:0047260]; alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity [GO:0003825]; trehalose-phosphatase activity [GO:0004805] | PF00982; | 3.40.50.2000; | Glycosyltransferase 20 family | null | null | CATALYTIC ACTIVITY: Reaction=ADP-alpha-D-glucose + D-glucose 6-phosphate = ADP + alpha,alpha-trehalose 6-phosphate + H(+); Xref=Rhea:RHEA:53880, ChEBI:CHEBI:15378, ChEBI:CHEBI:57498, ChEBI:CHEBI:58429, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.4.1.347; Evidence={ECO:0000269|Ref.4}; CATALYTIC ACTIVITY: Reaction=CDP-alpha-D-glucose + D-glucose 6-phosphate = alpha,alpha-trehalose 6-phosphate + CDP + H(+); Xref=Rhea:RHEA:53884, ChEBI:CHEBI:15378, ChEBI:CHEBI:58069, ChEBI:CHEBI:58429, ChEBI:CHEBI:61548, ChEBI:CHEBI:137927; Evidence={ECO:0000269|Ref.4}; CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + GDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + GDP + H(+); Xref=Rhea:RHEA:14605, ChEBI:CHEBI:15378, ChEBI:CHEBI:58189, ChEBI:CHEBI:58429, ChEBI:CHEBI:61548, ChEBI:CHEBI:62230; Evidence={ECO:0000269|Ref.4}; CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + TDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + H(+) + TDP; Xref=Rhea:RHEA:53888, ChEBI:CHEBI:15378, ChEBI:CHEBI:58429, ChEBI:CHEBI:61417, ChEBI:CHEBI:61548, ChEBI:CHEBI:137931; Evidence={ECO:0000269|Ref.4}; CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + H(+) + UDP; Xref=Rhea:RHEA:18889, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58429, ChEBI:CHEBI:58885, ChEBI:CHEBI:61548; EC=2.4.1.15; Evidence={ECO:0000269|Ref.4}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40 uM for UDP-Glc (in the presence of polyanion) {ECO:0000269|Ref.4}; KM=1 mM for Glc-6-P (with UDP-Glc in the presence of polyanion) {ECO:0000269|Ref.4}; KM=2 mM for Glc-6-P (with GDP-Glc in the presence of polyanion) {ECO:0000269|Ref.4}; | PATHWAY: Glycan biosynthesis; trehalose biosynthesis. {ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|Ref.4}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: About 60% of the activity is lost in the absence of FII after 10 minutes at 40 degrees Celsius, but only 35% in the presence of FII. {ECO:0000269|Ref.4}; | FUNCTION: Involved in the production of glycogen and alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate (M1P), and probably in the osmoprotection via the biosynthesis of trehalose (PubMed:27513637, Ref.4). Catalyzes the transfer of glucose from UDP-glucose (UDP-Glc) to glucose-6-phosphate (Glc-6-P) to form trehalose-6-phosphate (Ref.4). ADP-Glc, CDP-Glc, GDP-Glc and TDP-Glc are also glucosyl donors, however, when the pyrimidine sugar nucleotides (CDP-Glc, TDP-Glc and UDP-Glc) are used as substrates, there is an absolute requirement for a high molecular weight polyanion for activity (Ref.4). {ECO:0000269|PubMed:27513637, ECO:0000269|Ref.4}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R4Q6 | CP142_MYCS2 | MTQMLTRPDVDLVNGMFYADGGAREAYRWMRANEPVFRDRNGLAAATTYQAVLDAERNPELFSSTGGIRPDQPGMPYMIDMDDPQHLLRRKLVNAGFTRKRVMDKVDSIGRLCDTLIDAVCERGECDFVRDIAAPLPMAVIGDMLGVLPTERDMLLKWSDDLVCGLSSHVDEAAIQKLMDTFAAYTEFTKDVITKRRAEPTDDLFSVLVNSEVEGQRMSDDEIVFETLLILIGGDETTRHTLSGGTEQLLRHRDQWDALVADVDLLPGAIEEMLRWTSPVKNMCRTLTADTVFHGTELRAGEKIMLMFESANFDESVFGDPDNFRIDRNPNSHVAFGFGTHFCLGNQLARLELRLMTERVLRRLPDLRLADDAPVPLRPANFVSGPESMPVVFTPSAPVLA | 1.14.15.28 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:23489718, ECO:0000269|PubMed:25210044}; | cholesterol catabolic process [GO:0006707] | null | cholest-4-en-3-one 26-monooxygenase activity [GO:0036199]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; steroid hydroxylase activity [GO:0008395] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | null | CATALYTIC ACTIVITY: Reaction=cholest-4-en-3-one + 5 H(+) + 3 O2 + 6 reduced [2Fe-2S]-[ferredoxin] = (25R)-3-oxocholest-4-en-26-oate + 4 H2O + 6 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:49996, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16175, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:71570; EC=1.14.15.28; Evidence={ECO:0000269|PubMed:23489718, ECO:0000305|PubMed:25210044}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.3 uM for cholest-4-en-3-one {ECO:0000269|PubMed:23489718}; KM=39.8 uM for cholesteryl sulfate {ECO:0000269|PubMed:25210044}; | PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000303|PubMed:23489718}. | null | null | FUNCTION: Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25R)-26-hydroxycholest-4-en-3-one (alcohol), (25R)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25R)-3-oxocholest-4-en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en-3-one. {ECO:0000269|PubMed:23489718, ECO:0000269|PubMed:25210044}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R4Y3 | CP125_MYCS2 | MPTPNIPSDFDFLDATLNLERLPVEELAELRKSEPIHWVDVPGGTGGFGDKGYWLVTKHADVKEVSRRSDVFGSSPDGAIPVWPQDMTREAVDLQRAVLLNMDAPQHTRLRKIISRGFTPRAIGRLEDELRSRAQKIAQTAAAQGAGDFVEQVSCELPLQAIAELLGVPQDDRDKLFRWSNEMTAGEDPEYADVDPAMSSFELISYAMKMAEERAVNPTEDIVTKLIEADIDGEKLSDDEFGFFVVMLAVAGNETTRNSITHGMIAFAQNPDQWELYKKERPETAADEIVRWATPVSAFQRTALEDVELGGVQIKKGQRVVMSYRSANFDEEVFEDPHTFNILRSPNPHVGFGGTGAHYCIGANLARMTINLIFNAIADNMPDLKPIGAPERLKSGWLNGIKHWQVDYTGAGKASVSGAPGTCPVAH | 1.14.15.29 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:23489718, ECO:0000269|PubMed:26522442}; | cholesterol catabolic process [GO:0006707] | null | cholest-4-en-3-one 26-monooxygenase activity [GO:0036199]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; steroid hydroxylase activity [GO:0008395] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | null | CATALYTIC ACTIVITY: Reaction=cholest-4-en-3-one + 5 H(+) + 3 O2 + 6 reduced [2Fe-2S]-[ferredoxin] = (25S)-3-oxocholest-4-en-26-oate + 4 H2O + 6 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:51564, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16175, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:71541; EC=1.14.15.29; Evidence={ECO:0000250|UniProtKB:P9WPP1, ECO:0000305|PubMed:23489718}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14 uM for cholest-4-en-3-one {ECO:0000269|PubMed:23489718}; | PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000303|PubMed:23489718}. | null | null | FUNCTION: Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25S)-26-hydroxycholest-4-en-3-one (alcohol), (25S)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25S)-3-oxocholest-4-en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en-3-one. {ECO:0000269|PubMed:23489718}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R564 | DISA_MYCS2 | MAVKSGARSGRNVVHLARPTLRETLGRLAPGTPLRDGLERILRGRTGALIVLGYDDSVEAICDGGFVLDVRYAPTRLRELSKMDGAVVLSSDGSRILRANVQLVPDPSIPTDESGTRHRSAERTAIQTGYPVISVSHSMSIVTVYVAGERHVVPDSATILSRANQTIATLERYKGRLDEVSRQLSTAEIEDFVTLRDVMTVVQRLEMVRRISLEIDADVVELGTDGRQLKLQLDELVGDNETARELIVRDYHANPDPPTAAQVAATLEELDSLSDSELLDFTVLARVFGYPSTAEAQDSAMSSRGYRAMAAIPRLQFAHVDLLVRSFGSLQNLLAASADDLQSVDGIGSMWARHIREGLSLLAESTIADRLA | 2.7.7.85 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01438}; | DNA repair [GO:0006281] | null | adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; diadenylate cyclase activity [GO:0106408]; DNA binding [GO:0003677] | PF02457;PF10635;PF12826; | 1.10.150.20;1.20.1260.110;3.40.1700.10; | DisA family | null | null | CATALYTIC ACTIVITY: Reaction=2 ATP = 3',3'-c-di-AMP + 2 diphosphate; Xref=Rhea:RHEA:35655, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:71500; EC=2.7.7.85; Evidence={ECO:0000255|HAMAP-Rule:MF_01438, ECO:0000269|PubMed:23760274}; | null | null | null | null | FUNCTION: Participates in a DNA-damage check-point. DisA forms globular foci that rapidly scan along the chromosomes searching for lesions. {ECO:0000255|HAMAP-Rule:MF_01438}.; FUNCTION: Has also diadenylate cyclase activity, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP likely acts as a signaling molecule that may couple DNA integrity with a cellular process. {ECO:0000255|HAMAP-Rule:MF_01438, ECO:0000269|PubMed:23760274}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R5D9 | TOP1_MYCS2 | MAGGDRGSGGTGNVRRLVIVESPTKARKIAGYLGSNYVVESSRGHIRDLPRNAADVPAKFKSEPWARLGVNVDQNFEPLYIVSPEKKSTVTELKGLLKDVDELYLATDGDREGEAIAWHLLETLKPRVPVKRMVFHEITEPAIRNAAENPRDLDIALVDAQETRRILDRLYGYEVSPVLWKKVAPKLSAGRVQSVATRIIVQRERERMAFHSASYWDVTAELDASVSDPSASPPKFTAKLNTVDGRRVATGRDFDSLGQLKRPDEVLVLDEASAGALASGLRGAQLAVTSVEQKPYTRRPYAPFMTSTLQQEAARKLRFSSERTMSIAQRLYENGYITYMRTDSTTLSESAINAARTQARQLYGEEYVHPSPRQYTRKVKNAQEAHEAIRPAGDVFQTPGQLHSALDTDEFRLYELIWQRTVASQMADARGTTLSLRIGGSASSGEQVVFNASGRTITFPGFLKAYVESIDELAGGESDDAESRLPNLTQGQRVDAADLSADGHQTSPPARYTEASLIKALEELGIGRPSTYSSIIKTIQDRGYVQKKGSALVPSWVAFAVVGLLEQHFGRLVDYDFTAAMEDELDEIANGQEQRTNWLNNFYFGGEHGVEGSIARAGGLKQLVGGNLEGIDAREVNSIKVFDDSEGRPVYVRVGRNGPYLERMVDDPDNPGEQKPQRANLKEDLTPDELTPELAEKLFATPQEGRSLGIDPETGHEIVAKDGRFGPYVTEVLPEPEDGGDDGTAGTPAKKGKKPTGPKPRTGSLFRSMDLETVTLEDALKLLSLPRVVGVDPTTNEEITAQNGRYGPYLKRGTDSRSLATEDQIFTITLDEALKIYAEPKRRGRQAASAPPLRELGNDPVSGKPMVIKDGRFGPYVTDGETNASLRKGDDVLTITDERASELLADRRARGPVKKKAPAKKAAKKAPAKKAAAKKA | 5.6.2.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00952, ECO:0000269|PubMed:9593741}; | DNA topological change [GO:0006265] | null | DNA binding [GO:0003677]; DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917]; metal ion binding [GO:0046872] | PF01131;PF01751;PF13368; | 3.40.50.140;1.10.460.10;2.70.20.10;1.10.290.10; | Type IA topoisomerase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00952}; | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-42 degrees Celsius. Partially active up to 65 degrees Celsius (PubMed:9593741). {ECO:0000269|PubMed:9593741}; | FUNCTION: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate (PubMed:9593741) and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). {ECO:0000255|HAMAP-Rule:MF_00952, ECO:0000269|PubMed:9593741}.; FUNCTION: Relaxes negatively (but not positively) supercoiled DNA, concatanates and knots circular ssDNA at 52 but not 37 degrees Celsius (PubMed:9593741). Preferentially nicks supercoiled DNA at C(G/T)CTT, cutting between the TT residues, binds ss and dsDNA with the recognition site (PubMed:10734203). {ECO:0000269|PubMed:10734203, ECO:0000269|PubMed:9593741}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R5M8 | EGTD_MYCS2 | MTLSLANYLAADSAAEALRRDVRAGLTAAPKSLPPKWFYDAVGSDLFDQITRLPEYYPTRTEAQILRTRSAEIIAAAGADTLVELGSGTSEKTRMLLDAMRDAELLRRFIPFDVDAGVLRSAGAAIGAEYPGIEIDAVCGDFEEHLGKIPHVGRRLVVFLGSTIGNLTPAPRAEFLSTLADTLQPGDSLLLGTDLVKDTGRLVRAYDDAAGVTAAFNRNVLAVVNRELSADFDLDAFEHVAKWNSDEERIEMWLRARTAQHVRVAALDLEVDFAAGEEMLTEVSCKFRPENVVAELAEAGLRQTHWWTDPAGDFGLSLAVR | 2.1.1.44 | null | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide [GO:0052704]; methylation [GO:0032259]; N-alpha,N-alpha,N-alpha-trimethyl-L-histidine biosynthesis from histidine [GO:0052707] | null | dimethylhistidine N-methyltransferase activity [GO:0030745]; protein methyltransferase activity [GO:0008276] | PF10017; | 3.40.50.150; | Methyltransferase superfamily, EgtD family | null | null | CATALYTIC ACTIVITY: Reaction=L-histidine + 3 S-adenosyl-L-methionine = 3 H(+) + hercynine + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:38471, ChEBI:CHEBI:15378, ChEBI:CHEBI:15781, ChEBI:CHEBI:57595, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.44; Evidence={ECO:0000269|PubMed:20420449, ECO:0000269|PubMed:25404173}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=109 uM for L-histidine {ECO:0000269|PubMed:25404173}; KM=17.7 uM for N-alpha-methyl-L-histidine {ECO:0000269|PubMed:25404173}; KM=25.3 uM for N-alpha,N-alpha-dimethyl-L-histidine {ECO:0000269|PubMed:25404173}; Note=kcat is 0.58 sec(-1) for the methylation of L-histidine. kcat is 0.23 sec(-1) for the methylation of N-alpha-methyl-L-histidine. kcat is 0.23 sec(-1) for the methylation of N-alpha,N-alpha-dimethyl-L-histidine. {ECO:0000269|PubMed:25404173}; | PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis. {ECO:0000269|PubMed:23629716, ECO:0000305|PubMed:20420449}. | null | null | FUNCTION: Catalyzes the SAM-dependent triple methylation of the alpha-amino group of histidine to form hercynine, a step in the biosynthesis pathway of ergothioneine. Among all the proteinogenic amino acids, only L-histidine is a substrate. {ECO:0000269|PubMed:20420449, ECO:0000269|PubMed:25404173}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R607 | DPRE1_MYCS2 | MSTTEFPTTTKRLMGWGRTAPTVASVLSTSDPEVIVRAVTRAAEEGGRGVIARGLGRSYGDNAQNGGGLVIDMPALNRIHSIDSGTRLVDVDAGVSLDQLMKAALPHGLWVPVLPGTRQVTVGGAIGCDIHGKNHHSAGSFGNHVRSMELLTANGEVRHLTPAGPDSDLFWATVGGNGLTGIILRATIEMTPTETAYFIADGDVTGSLDETIAFHSDGSEANYTYSSAWFDAISKPPKLGRAAISRGSLAKLDQLPSKLQKDPLKFDAPQLLTLPDIFPNGLANKFTFMPIGELWYRKSGTYRNKVQNLTQFYHPLDMFGEWNRAYGSAGFLQYQFVVPTEAVEEFKSIIVDIQRSGHYSFLNVFKLFGPGNQAPLSFPIPGWNVCVDFPIKAGLHEFVTELDRRVLEFGGRLYTAKDSRTTAETFHAMYPRIDEWIRIRRSVDPDGVFASDMARRLQLL | 1.1.98.3 | null | capsule polysaccharide biosynthetic process [GO:0045227]; cell wall organization [GO:0071555]; response to antibiotic [GO:0046677] | membrane [GO:0016020]; periplasmic space [GO:0042597] | D-arabinono-1,4-lactone oxidase activity [GO:0003885]; FAD binding [GO:0071949] | PF04030;PF01565; | 3.30.465.10;3.30.43.10; | DprE1 family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P9WJF1}. | CATALYTIC ACTIVITY: Reaction=FAD + H(+) + trans,octa-cis-decaprenylphospho-beta-D-ribofuranose = FADH2 + trans,octa-cis-decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose; Xref=Rhea:RHEA:33899, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:65067, ChEBI:CHEBI:66881; EC=1.1.98.3; Evidence={ECO:0000269|PubMed:22188377}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.11 mM for FPR (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22956199}; Note=kcat is 12.7 min(-1) for epimerase activity with FPR as substrate (at pH 8.5 and 25 degrees Celsius). {ECO:0000269|PubMed:22956199}; | PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis. {ECO:0000305|PubMed:21346818}. | null | null | FUNCTION: Component of the DprE1-DprE2 complex that catalyzes the 2-step epimerization of decaprenyl-phospho-ribose (DPR) to decaprenyl-phospho-arabinose (DPA), a key precursor that serves as the arabinose donor required for the synthesis of cell-wall arabinans (PubMed:22188377). DprE1 catalyzes the first step of epimerization, namely FAD-dependent oxidation of the C2' hydroxyl of DPR to yield the keto intermediate decaprenyl-phospho-2'-keto-D-arabinose (DPX) (PubMed:22188377). The intermediate DPX is then transferred to DprE2 subunit of the epimerase complex, most probably through a 'substrate channel' at the interface of DprE1-DprE2 complex (By similarity). Can also use farnesyl-phosphoryl-beta-D-ribofuranose (FPR) as substrate in vitro (PubMed:22188377, PubMed:22956199). Appears to be essential for the growth of M.smegmatis (PubMed:21346818). {ECO:0000250|UniProtKB:P9WJF1, ECO:0000269|PubMed:21346818, ECO:0000269|PubMed:22188377, ECO:0000269|PubMed:22956199}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R618 | FAA32_MYCS2 | MPFHNPFIKDGQIKFPDGSSIVAHVERWAKVRGDKLAYRFLDFSTERDGVPRDLTWAQFSARNRAVAARLQQVTQPGDRVAILCPQNLDYLVAFFGALYAGRIAVPLFDPSEPGHVGRLHAVLDNCHPSAILTTTEAAEGVRKFFRTRPANQRPRVIAVDAVPDDVASTWVNPDEPDETTIAYLQYTSGSTRIPTGVQITHLNLATNVVQVIEALEGEEGDRGLSWLPFFHDMGLITALLAPMIGHYFTFMTPAAFVRRPERWIRELARKEGDTGGTISVAPNFAFDHAAARGVPKPGSPPLDLSNVKAVLNGSEPISAATVRRFNEAFGPFGFPPKAIKPSYGLAEATLFVSTTPSAEEPKIITVDRDQLNSGRIVEVDADSPKAVAQASAGKVGIAEWAVIVDAESATELPDGQVGEIWISGQNMGTGYWGKPEESVATFQNILKSRTNPSHAEGATDDATWVRTGDYGAFYDGDLYITGRVKDLVIIDGRNHYPQDLEYSAQEASKAIRTGYVAAFSVPANQLPDEVFENAHSGIKRDPDDTSEQLVIVAERAPGAHKLDIGPITDDIRAAIAVRHGVTVRDVLLTAAGAIPRTSSGKIGRRACRAAYLDGSLRAGKVANDFPDATD | 6.2.1.20 | null | fatty acid biosynthetic process [GO:0006633] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | adenylyltransferase activity [GO:0070566]; ATP binding [GO:0005524]; long-chain fatty acid [acyl-carrier-protein] ligase activity [GO:0008922] | PF00501; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:45588, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12682, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57560, ChEBI:CHEBI:64479, ChEBI:CHEBI:133243, ChEBI:CHEBI:456215; EC=6.2.1.20; Evidence={ECO:0000250|UniProtKB:O53580}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45589; Evidence={ECO:0000250|UniProtKB:O53580}; CATALYTIC ACTIVITY: Reaction=ATP + decanoate + H(+) = decanoyl-AMP + diphosphate; Xref=Rhea:RHEA:65008, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:156261; Evidence={ECO:0000269|PubMed:23364516}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65009; Evidence={ECO:0000269|PubMed:23364516}; CATALYTIC ACTIVITY: Reaction=ATP + dodecanoate + H(+) = diphosphate + dodecanoyl-AMP; Xref=Rhea:RHEA:43712, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83623; Evidence={ECO:0000269|PubMed:23364516, ECO:0000269|PubMed:26900152}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43713; Evidence={ECO:0000269|PubMed:23364516, ECO:0000269|PubMed:26900152}; CATALYTIC ACTIVITY: Reaction=ATP + H(+) + tetradecanoate = diphosphate + tetradecanoyl-AMP; Xref=Rhea:RHEA:43704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:30807, ChEBI:CHEBI:33019, ChEBI:CHEBI:83626; Evidence={ECO:0000269|PubMed:23364516, ECO:0000269|PubMed:26900152}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43705; Evidence={ECO:0000269|PubMed:23364516, ECO:0000269|PubMed:26900152}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=259 uM for decanoate {ECO:0000269|PubMed:23364516}; KM=25.9 uM for dodecanoate {ECO:0000269|PubMed:23364516}; KM=5.2 uM for tetradecanoate {ECO:0000269|PubMed:23364516}; KM=76 uM for ATP {ECO:0000269|PubMed:23364516}; KM=112 uM for ATP {ECO:0000269|PubMed:26900152}; Note=kcat is 16.1 min(-1) with decanoate as substrate (PubMed:23364516). kcat is 11.2 min(-1) with dodecanoate as substrate (PubMed:23364516). kcat is 4.2 min(-1) with tetradecanoate as substrate (PubMed:23364516). {ECO:0000269|PubMed:23364516}; | PATHWAY: Lipid metabolism; mycolic acid biosynthesis. {ECO:0000250|UniProtKB:O53580}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:23364516}; | null | FUNCTION: Involved in the biosynthesis of mycolic acids (By similarity). Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the phosphopantetheine arm of the polyketide synthase Pks13 for further chain extension (By similarity). Can use decanoate (C10), dodecanoate (C12) and tetradecanoate (C14) (PubMed:23364516, PubMed:26900152). {ECO:0000250|UniProtKB:O53580, ECO:0000269|PubMed:23364516, ECO:0000269|PubMed:26900152}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R6D0 | NFNB_MYCS2 | MSVPTLPTGPTVDLAQAAERLIKGRRAVRAFRPDEVPEETMRAVFELAGHAPSNSNTQPWHVEVVSGAARDRLAEALVTAHAEERVTVDFPYREGLFQGVLQERRADFGSRLYAALGIARDQTDLLQGYNTESLRFYGAPHVAMLFAPNNTEARIAGDMGIYAQTLMLAMTAHGIASCPQALLSFYADTVRAELGVENRKLLMGISFGYADDTAAVNGVRIPRAGLSETTRFSR | 1.-.-.- | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:20624223}; Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:20624223}; | thyroid hormone metabolic process [GO:0042403]; tyrosine metabolic process [GO:0006570]; xenobiotic catabolic process [GO:0042178] | null | FMN binding [GO:0010181]; identical protein binding [GO:0042802]; NADP binding [GO:0050661]; oxidoreductase activity [GO:0016491]; protein homodimerization activity [GO:0042803] | PF00881; | 3.40.109.10; | Nitroreductase family | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.75 uM for NADH (at pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:20624223}; KM=8.15 uM for NADPH (at pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:20624223}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 to 9.0. {ECO:0000269|PubMed:20624223}; | null | FUNCTION: Confers resistance to antitubercular drugs benzothiazinone (BTZ) and dinitrobenzamide (DNB). Inactivates BTZ and DNB by reducing an essential nitro group of these compounds to amino group or to hydroxyl amine, respectively, using NADH or NADPH as source of reducing equivalents; two electrons are transferred (PubMed:20624223, PubMed:22069462). Able to reduce the nitro group of bicyclic nitroimidazole PA-824, but not of quinone menadione, nitrofurazone, methyl-4-nitrobenzoate, 4-nitrobenzene methyl sulfonate or 4-nitroacetophenone (PubMed:20624223). {ECO:0000269|PubMed:20624223, ECO:0000269|PubMed:22069462}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R6E0 | TRES_MYCS2 | MEEHTQGSHVEAGIVEHPNAEDFGHARTLPTDTNWFKHAVFYEVLVRAFYDSNADGIGDLRGLTEKLDYIKWLGVDCLWLPPFYDSPLRDGGYDIRDFYKVLPEFGTVDDFVTLLDAAHRRGIRIITDLVMNHTSDQHEWFQESRHNPDGPYGDFYVWSDTSDRYPDARIIFVDTEESNWTFDPVRRQFYWHRFFSHQPDLNYDNPAVQEAMLDVLRFWLDLGIDGFRLDAVPYLFEREGTNCENLPETHAFLKRCRKAIDDEYPGRVLLAEANQWPADVVAYFGDPDTGGDECHMAFHFPLMPRIFMAVRRESRFPISEILAQTPPIPDTAQWGIFLRNHDELTLEMVTDEERDYMYAEYAKDPRMKANVGIRRRLAPLLENDRNQIELFTALLLSLPGSPVLYYGDEIGMGDIIWLGDRDSVRTPMQWTPDRNAGFSKATPGRLYLPPNQDAVYGYHSVNVEAQLDSSSSLLNWTRNMLAVRSRHDAFAVGTFRELGGSNPSVLAYIREVTRQQGDGGAKTDAVLCVNNLSRFPQPIELNLQQWAGYIPVEMTGYVEFPSIGQLPYLLTLPGHGFYWFQLREPDPEPGAQQ | 3.2.1.1; 5.4.99.16 | null | glycogen biosynthetic process [GO:0005978]; glycogen metabolic process [GO:0005977]; maltose metabolic process [GO:0000023]; polysaccharide catabolic process [GO:0000272]; trehalose metabolic process [GO:0005991] | null | alpha-amylase activity [GO:0004556]; calcium ion binding [GO:0005509]; maltose alpha-D-glucosyltransferase activity [GO:0047471] | PF00128;PF16657; | 3.20.20.80;2.60.40.1180; | Glycosyl hydrolase 13 family, TreS subfamily | null | null | CATALYTIC ACTIVITY: Reaction=D-maltose = alpha,alpha-trehalose; Xref=Rhea:RHEA:15145, ChEBI:CHEBI:16551, ChEBI:CHEBI:17306; EC=5.4.99.16; Evidence={ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:18505459}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 mM for maltose (at pH 6.8 and 37 degrees Celsius) {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; KM=87 mM for trehalose (at pH 6.8 and at 37 degrees Celsius) {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; KM=2.9 mM for 2,4-dinitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius) {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; KM=2.5 mM for 3,4-dinitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius) {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; KM=2.2 mM for 4-chloro-2-nitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius) {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; KM=5.8 mM for 4-nitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius) {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; KM=0.7 mM for 2-nitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius) {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; KM=0.15 mM for alpha-glucosyl fluoride (at pH 6.8 and 37 degrees Celsius) {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; | PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000269|PubMed:20118231, ECO:0000269|PubMed:27513637}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 6.0-6.2 for the amylase activity and 7.0 for the trehalose synthase activity. {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459}; | null | FUNCTION: Catalyzes the reversible interconversion of maltose and trehalose by transglucosylation (PubMed:15511231, PubMed:18505459, PubMed:20118231, PubMed:21840994). Maltose is the preferred substrate (PubMed:15511231, PubMed:18505459). To a lesser extent, also displays amylase activity, catalyzing the endohydrolysis of (1->4)-alpha-D-glucosidic linkages in glycogen and maltooligosaccharides such as maltoheptaose, to produce maltose which then can be converted to trehalose (PubMed:18505459). TreS plays a key role in the utilization of trehalose for the production of glycogen and alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate (M1P) (PubMed:20118231, PubMed:27513637). Might also function as a sensor and/or regulator of trehalose levels within the cell. Thus, when trehalose levels in the cell become dangerously low, TreS can expedite the conversion of glycogen to maltose via its amylase activity and then convert the maltose to trehalose; but this enzyme also can expedite or promote the conversion of trehalose to glycogen when cytoplasmic trehalose levels become too high. Is also able to catalyze the hydrolytic cleavage of alpha-aryl glucosides, as well as alpha-glucosyl fluoride in vitro. {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:20118231, ECO:0000269|PubMed:21840994, ECO:0000269|PubMed:27513637}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R758 | LERK_MYCS2 | MTYLLNSPDDFADEAVRGLVAANPDLLTEVPGGVVRSTETPKGQPALVIGGGSGHYPAFAGWVGPGMGHGAPCGNIFSSPSASEVYSVVRNAENGGGVILGFGNYAGDVLHFGLAAEKLRHEGIDVRIVTVSDDIASNSPENHRDRRGVAGDLPVFKIAGAAIEAGADLDEAERVAWKANDATRSFGLAFEGCTLPGATEPLFHVEKGWMGVGLGIHGEPGVRDNRLGTAAEVADMLFDEVTAEEPPRGENGYDGRVAVILNGLGTVKYEELFVVYGRIAERLAQQGFTVVRPEVGEFVTSLDMAGVSLTMVFLDDELERLWTAPVETPAYRRGAMPAVDRTPRTTTWDAAETTIPEASEGSRECARNIVAVLETFQQVCADNEAELGRIDAVAGDGDHGQGMSFGSRGAAQAARDAVDRNAGARTTLLLAGQAWADAAGGTSGALWGAALTSAGGVFSDTDGADEQAAVDAICAGIDAILRLGGAQPGDKTMVDAAVPFRDALVKAFDTQAGPAITSAARVAREAAEKTADITARRGRARVLGEKSVGTPDPGALSFAMLMKALGEHLTR | 2.7.1.209 | null | carbohydrate catabolic process [GO:0016052]; carbohydrate utilization [GO:0009758]; cellular response to carbohydrate stimulus [GO:0071322]; glycerol catabolic process [GO:0019563] | cytosol [GO:0005829] | ATP binding [GO:0005524]; carbohydrate binding [GO:0030246]; carbohydrate kinase activity [GO:0019200]; glycerone kinase activity [GO:0004371] | PF02733;PF02734; | 1.25.40.340; | null | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-erythrulose = ADP + H(+) + L-erythrulose 1-phosphate; Xref=Rhea:RHEA:48780, ChEBI:CHEBI:15378, ChEBI:CHEBI:27913, ChEBI:CHEBI:30616, ChEBI:CHEBI:58002, ChEBI:CHEBI:456216; EC=2.7.1.209; Evidence={ECO:0000269|PubMed:26560079, ECO:0000305|PubMed:26978037}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3 uM for L-erythrulose {ECO:0000269|PubMed:26560079}; KM=10.6 uM for D-erythrulose {ECO:0000269|PubMed:26560079}; KM=37.8 uM for dihydroxyacetone {ECO:0000269|PubMed:26560079}; Note=kcat is 1.79 sec(-1) with L-erythrulose as substrate. kcat is 1.60 sec(-1) with D-erythrulose as substrate. kcat is 2.12 sec(-1) with dihydroxyacetone as substrate. {ECO:0000269|PubMed:26560079}; | PATHWAY: Carbohydrate metabolism; L-threitol degradation. {ECO:0000269|PubMed:26560079}. | null | null | FUNCTION: Kinase that has a preference for L-erythrulose, producing L-erythrulose-1P. Involved in the degradation pathway of L-threitol, that allows M.smegmatis to grow on this compound as the sole carbon source. Is also able to phosphorylate D-erythrulose and dihydroxyacetone in vitro. {ECO:0000269|PubMed:26560079, ECO:0000269|PubMed:26978037}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0RV30 | FBPAP_CENSY | MRITVSAIKADVGGIGGHTLPSSGLLDAVRRKVSSSSLLIDHYIGYCGDDVHIVMTHTRGTDNSDIHKLAWDAFMEGTRVAKEEGLYGAGQDLLRDSFSGNVKGMGPGVAELEFEERANEAFTVFAADKTEPGAFNYPFYRMFVDSLSNTGLIVNKSLAEGVVINIMDVSKARTARLVLWEDKPTIEAALMYPGRFVVSSVETRDGEPIASASTDRLHNIAGTYVGKDDPICLVRTQKRFPATEEAGSCFNNPHYVAGNTRGSHHMPLMPVRLNSPASINFCIPIVEALVFSMHEGRLTGPFDGFSTPDWDDVRRTATRRAHAMRRQGFVHPATLVPDELEYAEGYRSRMDVLDSKMVPLKDSGPAGTGRAYEDPD | 3.1.3.11; 4.1.2.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20348906}; | gluconeogenesis [GO:0006094] | null | fructose 1,6-bisphosphate 1-phosphatase activity [GO:0042132]; fructose-bisphosphate aldolase activity [GO:0004332]; magnesium ion binding [GO:0000287]; oxidoreductase activity [GO:0016491] | PF01950; | null | FBP aldolase/phosphatase family | null | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; Evidence={ECO:0000269|PubMed:20348906}; CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence={ECO:0000269|PubMed:20348906}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40 uM for D-fructose 1,6-bisphosphate (when assaying the FBP phosphatase activity, at 48 degrees Celsius) {ECO:0000269|PubMed:20348906}; KM=110 uM for triosephosphates (when assaying the FBP aldolase activity in the anabolic direction, at 48 degrees Celsius) {ECO:0000269|PubMed:20348906}; KM=100 mM for D-fructose 1,6-bisphosphate (when assaying the FBP aldolase activity in the catabolic direction, at 48 degrees Celsius) {ECO:0000269|PubMed:20348906}; Vmax=0.22 umol/min/mg enzyme for the FBP phosphatase activity (at 48 degrees Celsius) {ECO:0000269|PubMed:20348906}; Vmax=0.24 umol/min/mg enzyme for the FBP aldolase activity in the anabolic direction (at 48 degrees Celsius) {ECO:0000269|PubMed:20348906}; Vmax=0.29 umol/min/mg enzyme for the FBP aldolase activity in the catabolic direction (at 48 degrees Celsius) {ECO:0000269|PubMed:20348906}; Note=The aldolase reaction is a classic case for a fully reversible enzymatic reaction but here, the KM values for the substrate for the aldol condensation and the aldol cleavage differ by a factor of 1000, and the intrinsic phosphatase activity renders the process irreversible. {ECO:0000269|PubMed:20348906}; | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000305|PubMed:20348906}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Heat-stabile at 70 degrees Celsius. Displays a half-life of 20 minutes at 82 degrees Celsius. {ECO:0000269|PubMed:20348906}; | FUNCTION: Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P). {ECO:0000269|PubMed:20348906}. | Cenarchaeum symbiosum (strain A) |
A0S864 | 3NBA_BOIIR | MKTLLLAVAVVAFVCLGSADQLGLGRQQIDWGQGQAVGPPYTLCFECNRMTSSDCSTALRCYRGSCYTLYRPDENCELKWAVKGCAETCPTAGPNERVKCCRSPRCNDD | null | null | modulation of receptor activity in another organism [GO:0044504] | extracellular region [GO:0005576] | acetylcholine receptor inhibitor activity [GO:0030550]; ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729] | null | 2.10.60.10; | Snake three-finger toxin family, Ancestral subfamily, Boigatoxin sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18952712}. | null | null | null | null | null | FUNCTION: This bird and reptile-specific postsynaptic neurotoxin inhibits the chick muscle alpha-1-beta-1-gamma-delta (CHRNA1-CHRNB1-CHRNG-CHNRD) nicotinic acetylcholine receptor (nAChR) 100-fold more compared with the mouse receptor. In vivo, produces rapid flaccid paralysis, dyspnea and increased respiratory rate in geckos. At sublethal doses geckos were immobilized for up to three days and then recovered. Chicks injected with lethal doses showed rapid onset of inactivity, dyspnea and neck droop, and no extended paralysis with survival was seen. {ECO:0000269|PubMed:18952712}. | Boiga irregularis (Brown tree snake) |
A0S865 | 3NBB_BOIIR | MKTLLLAVAVVAFVCLGSADQLGLGRQQIDWGKGQAKGPPYTLCFECNRETCSNCFKDNRCPPYHRTCYTLYRPDGNGEMKWAVKGCAKTCPTAQPGESVQCCNTPKCNDY | null | null | modulation of receptor activity in another organism [GO:0044504] | extracellular region [GO:0005576] | acetylcholine receptor inhibitor activity [GO:0030550]; ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729] | PF00087; | 2.10.60.10; | Snake three-finger toxin family, Ancestral subfamily, Boigatoxin sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18952712}. | null | null | null | null | null | FUNCTION: This bird and reptile-specific postsynaptic neurotoxin inhibits the chick muscle alpha-1-beta-1-gamma-delta (CHRNA1-CHRNB1-CHRNG-CHRND) nicotinic acetylcholine receptor (nAChR) 100-fold more compared with the mouse receptor. In vivo, produces rapid flaccid paralysis, dyspnea and increased respiratory rate in geckos. At sublethal doses geckos were immobilized for up to three days and then recovered. Chicks injected with lethal doses showed rapid onset of inactivity, dyspnea and neck droop, and no extended paralysis with survival was seen. {ECO:0000269|PubMed:18952712}. | Boiga irregularis (Brown tree snake) |
A0SVK0 | DOG1_ARATH | MGSSSKNIEQAQDSYLEWMSLQSQRIPELKQLLAQRRSHGDEDNDNKLRKLTGKIIGDFKNYAAKRADLAHRCSSNYYAPTWNSPLENALIWMGGCRPSSFFRLVYALCGSQTEIRVTQFLRNIDGYESSGGGGGASLSDLSAEQLAKINVLHVKIIDEEEKMTKKVSSLQEDAADIPIATVAYEMENVGEPNVVVDQALDKQEEAMARLLVEADNLRVDTLAKILGILSPVQGADFLLAGKKLHLSMHEWGTMRDRRRRDCMVDTEVIFDACTTVNSGPRPTETTNNERN | null | null | abscisic acid-activated signaling pathway [GO:0009738]; DNA-templated transcription [GO:0006351]; regulation of seed dormancy process [GO:2000033]; seed dormancy process [GO:0010162]; sugar mediated signaling pathway [GO:0010182] | nucleus [GO:0005634] | identical protein binding [GO:0042802]; sequence-specific DNA binding [GO:0043565] | PF14144; | null | null | PTM: A shift in isoelectric focusing of the protein occurs during after-ripening, probably leading to its loss of function. {ECO:0000269|PubMed:22829147}. | SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:22829147, ECO:0000269|PubMed:26620523, ECO:0000269|PubMed:26684465}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:26620523}. | null | null | null | null | null | FUNCTION: Required for the induction of seed dormancy (PubMed:17065317, PubMed:22829147, PubMed:26620523). The level of DOG1 protein in freshly harvested seeds determines the level of seed dormancy (PubMed:22829147). Determines the temperature window for germination by regulating the expression of micropylar endosperm-weakening genes through temperature control of the gibberellins metabolism (PubMed:25114251). Regulates seed dormancy and flowering time through an influence on levels of microRNAs miR156 and miR172 (PubMed:27035986). Regulator of seed maturation interfering with abscisic acid signaling components and activating ABI5 (PubMed:26729600). In cv. Cvi-1, enhances glucose induction of ABI4 (PubMed:18410483). {ECO:0000269|PubMed:17065317, ECO:0000269|PubMed:18410483, ECO:0000269|PubMed:22829147, ECO:0000269|PubMed:25114251, ECO:0000269|PubMed:26620523, ECO:0000269|PubMed:26729600, ECO:0000269|PubMed:27035986}. | Arabidopsis thaliana (Mouse-ear cress) |
A0SYQ0 | PTGES_CANLF | MPPPVLALVSGQALPAFLLCSTLLVIKMYVVAVITGQVRLRKKAFANPEDALRHGGLQYCRSDQDVDRCLRAHRNDMETIYPFLFLGFVYSFLGPDPFIAQMHFLVFFLGRMVHTVAYLGKLRAPTRSLAYTVAQLPCASMALQIVWEAACHL | 1.11.1.-; 2.5.1.18; 5.3.99.3 | COFACTOR: Name=glutathione; Xref=ChEBI:CHEBI:57925; Evidence={ECO:0000250|UniProtKB:O14684}; | cell population proliferation [GO:0008283]; negative regulation of cell population proliferation [GO:0008285]; positive regulation of prostaglandin secretion [GO:0032308]; prostaglandin biosynthetic process [GO:0001516]; regulation of fever generation [GO:0031620]; regulation of inflammatory response [GO:0050727]; sensory perception of pain [GO:0019233] | membrane [GO:0016020]; nuclear envelope lumen [GO:0005641]; perinuclear region of cytoplasm [GO:0048471] | glutathione binding [GO:0043295]; glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]; prostaglandin-D synthase activity [GO:0004667]; prostaglandin-E synthase activity [GO:0050220] | PF01124; | 1.20.120.550; | MAPEG family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O14684}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O14684}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O14684}. Note=Colocalizes with PTGS1/COX-1 and PTGS2/COX-2 in the perinuclear compartment. {ECO:0000250|UniProtKB:O14684}. | CATALYTIC ACTIVITY: Reaction=prostaglandin H2 = prostaglandin E2; Xref=Rhea:RHEA:12893, ChEBI:CHEBI:57405, ChEBI:CHEBI:606564; EC=5.3.99.3; Evidence={ECO:0000250|UniProtKB:O14684}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12894; Evidence={ECO:0000250|UniProtKB:O14684}; CATALYTIC ACTIVITY: Reaction=2-glyceryl-prostaglandin H2 = 2-glyceryl-prostaglandin E2; Xref=Rhea:RHEA:53324, ChEBI:CHEBI:85166, ChEBI:CHEBI:137172; Evidence={ECO:0000250|UniProtKB:O14684}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53325; Evidence={ECO:0000250|UniProtKB:O14684}; CATALYTIC ACTIVITY: Reaction=prostaglandin G2 = (15S)-15-hydroperoxy-prostaglandin E2; Xref=Rhea:RHEA:64364, ChEBI:CHEBI:82629, ChEBI:CHEBI:152564; Evidence={ECO:0000250|UniProtKB:O14684}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64365; Evidence={ECO:0000250|UniProtKB:O14684}; CATALYTIC ACTIVITY: Reaction=1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitrophenyl-S-glutathione + chloride + H(+); Xref=Rhea:RHEA:51220, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:34718, ChEBI:CHEBI:57925, ChEBI:CHEBI:133977; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:O14684}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:48620, ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90632; Evidence={ECO:0000250|UniProtKB:O14684}; | null | PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000250|UniProtKB:O14684}. | null | null | FUNCTION: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli (By similarity). Plays a key role in inflammation response, fever and pain (By similarity). Catalyzes also the oxidoreduction of endocannabinoids into prostaglandin glycerol esters and PGG2 into 15-hydroperoxy-PGE2. In addition, displays low glutathione transferase and glutathione-dependent peroxidase activities, toward 1-chloro-2,4-dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE), respectively (By similarity). {ECO:0000250|UniProtKB:O14684, ECO:0000250|UniProtKB:Q9JM51}. | Canis lupus familiaris (Dog) (Canis familiaris) |
A0T2N3 | APJB_DANRE | MNAMDNMTADYSPDYFDDAVNSSMCEYDEWEPSYSLIPVLYMLIFILGLTGNGVVIFTVWRAQSKRRAADVYIGNLALADLTFVVTLPLWAVYTALGYHWPFGVALCKISSYVVLLNMYASVFCLTCLSLDRYMAIVHSLTSTQLRTRGHMRASLTAIWLLSGVLAAPTLLFRTTVYDVETNRTSCAMDFNLVVSQPGQETYWIAGLSISSTALGFLIPLLAMMVCYGFIGCTVTRHFNSLRKEDQRKRRLLKIITTLVVVFAACWMPFHVVKTMDALSYLNLAPDSCTFLNLLLLAHPYATCLAYVNSCLNPLLYAFFDLRFRSQCLCLLNLKKALHASPASSLSSQKTEAQSLATKV | null | null | angioblast cell migration from lateral mesoderm to midline [GO:0035479]; blood vessel development [GO:0001568]; brain development [GO:0007420]; calcium-mediated signaling [GO:0019722]; cardiac muscle tissue development [GO:0048738]; cell chemotaxis [GO:0060326]; cell migration [GO:0016477]; coronary vasculature development [GO:0060976]; determination of heart left/right asymmetry [GO:0061371]; determination of liver left/right asymmetry [GO:0071910]; endodermal cell differentiation [GO:0035987]; establishment of epithelial cell polarity [GO:0090162]; G protein-coupled receptor signaling pathway [GO:0007186]; gastrulation [GO:0007369]; gastrulation with mouth forming second [GO:0001702]; heart development [GO:0007507]; immune response [GO:0006955]; mesodermal cell migration [GO:0008078]; negative regulation of cAMP-mediated signaling [GO:0043951]; neurogenesis [GO:0022008]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:1903589]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of inhibitory G protein-coupled receptor phosphorylation [GO:1904325]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; regulation of nodal signaling pathway [GO:1900107]; sprouting angiogenesis [GO:0002040]; vasculogenesis [GO:0001570] | external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | apelin receptor activity [GO:0060182]; C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P79960}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P79960}. Note=Internalized to the cytoplasm after exposure to apelin (apln). After exposure to apelin receptor early endogenous ligand (apela), internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane. {ECO:0000250|UniProtKB:P35414, ECO:0000250|UniProtKB:P79960}. | null | null | null | null | null | FUNCTION: Receptor for apelin receptor early endogenous ligand (apela) and apelin (apln) hormones coupled to G proteins that inhibit adenylate cyclase activity (PubMed:17336905, PubMed:17336906, PubMed:24316148, PubMed:24407481). Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for apela hormone, promoting endoderm and mesendoderm cell migration and regulating the migration of cells fated to become myocardial progenitors, respectively (PubMed:17336905, PubMed:17336906, PubMed:24316148, PubMed:24407481, PubMed:26017639). Positively regulates angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis (PubMed:26017639). May promote sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development (By similarity). Required for cardiovascular development, particularly for intersomitic vein angiogenesis by acting as a receptor for apln hormone (By similarity). Plays a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility and heart failure (By similarity). Acts redundantly with agtrl1a in heart development (PubMed:17336906). {ECO:0000250|UniProtKB:P35414, ECO:0000250|UniProtKB:P79960, ECO:0000250|UniProtKB:Q4VA82, ECO:0000250|UniProtKB:Q9WV08, ECO:0000269|PubMed:17336905, ECO:0000269|PubMed:17336906, ECO:0000269|PubMed:24316148, ECO:0000269|PubMed:24407481, ECO:0000269|PubMed:26017639}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A1A278 | MANA_BIFAA | MKTTVTKLLATVAAASTIFGMSTLPAFAAEGKSASNGNSVNISDVNATAETRALFDKLKNSGKGDLRFGQQHATDENISSSASQGDVYETTGKYPAVFGWDAGLALRGAEKPGSGADKNANAKALAQNITDADSKGAIVTLSAHWCNPGTGKDFNDTTAVASELLPGGKYSGTFNKELDAIAATAQRAKRSDGTLIPIIFRPLHENNGSWFWWGATHASASEYKELYRYIVDYLRDVKDVHNLLYAYSPGGVFNGDSTDYLATYPGDQWVDVLGYDEYDSDDSADDSSAWINTVVKDMKMVSDQASQRGKIVALTEFGRSGDRKFKESGTGDKDTKFFSELAEALAENVPSTAYMMTWANFGGGGDNFQAYTSWKGSDGEADFKAFADSNKNLMASKDNVDYSNAPAAAMQNGSARIVTPVDGNRVTDTKVVVRVKTEGVKYSDLDLNSAIVTTDRGQNVKLKYSCNGYFTGILDLNAAGINLDQSKLTLTPQVKTKDGKTLAAADGNGSVTVKLGAKPEQTVDNVEDFDSYDNEAELQSVYSPSHSTKSNLTLVDSPEDNGTKAGNIHYDFVSYPEYNGFQRSHTPKQDWSGFSKLNMFLKADGSDHKFVVQVNAGGVTFEAYPKIDGTDGHVVSLNFGDADGNGGDFAPASWDTAHAGMKLSQKLLSKVGSFALYINDNGGNRPKSGDLTLDSIKLDGKRDAYAPNTNPTPGNTAKAQSVDDFSGYSDDAAAQSAWGNRGHTEVLSLDEGPTDGSKALRFKYDFSNGGWYDVAKYLDGANWSGESVLAFQVKGDGSGNAIGLQIGTSDGKYFLASVKLDFTGWKQIEIPLVDNANLTQSWPEDANKDNPMTEDDLASIKELVFASQQWNSESDGLDSSIADIKVEPAENTSNEQTPKDESKTEVKADKEQEQSEDTSADVTAQDPATCPISDEDSKGSTGNTTVTVKPTPDTKEPADNTGKDGLSRTGSNIISAIAAVAVLLLGGCAVLIARKRKGGDIE | 3.2.1.78 | null | cellulose catabolic process [GO:0030245]; galactomannan metabolic process [GO:0051069]; glucomannan metabolic process [GO:0010391]; mannan catabolic process [GO:0046355] | extracellular region [GO:0005576] | cellulase activity [GO:0008810]; mannan binding [GO:2001065]; mannan endo-1,4-beta-mannosidase activity [GO:0016985] | PF03425;PF02156; | 2.60.120.430;3.20.20.80;2.60.40.10; | Glycosyl hydrolase 26 family | null | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}; Peptidoglycan-anchor {ECO:0000305}. Note=Is likely to be cell attached, either by the sortase mechanism (LPXTG motif) or via a C-terminal transmembrane helix. {ECO:0000269|PubMed:23064345}. | CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.; EC=3.2.1.78; Evidence={ECO:0000269|PubMed:23064345}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.3. Retains over 90% of its activity in the pH range of 5 to 6. {ECO:0000269|PubMed:23064345}; | null | FUNCTION: Beta-mannanase likely involved in the utilization of carbohydrates in the human gut. Catalyzes the hydrolysis of different beta-1,4-linked mannans, such as ivory nut mannan, konjac glucomannan, as well as carob and guar gum galactomannans, to a mixture of oligosaccharides. The dominant product from ivory nut mannan is found to be mannotriose; mannobiose and mannotetraose are produced to a lesser extent. Does not hydrolyze mannobiose, and hydrolyzes mannotriose at a significantly lower rate than the longer oligosaccharides. {ECO:0000269|PubMed:23064345}. | Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) |
A1A399 | BGAL_BIFAA | MSARRNFEWPELLTADGRGIAFGGDYNPDQWSEDIWDDDIRLMKQAGVNTVALAIFSWDRIQPTEDRWDFGWLDRIIDKLGNAGIVVDLASATATAPLWLYESHPEVLPRDKYGHPVNAGSRQSWSPTSPVFKEYALTLCRKLAERYGTNPYVTAWHMGNEYGWNNREDYSDNALEAFRAWCRRKYGTIDALNQAWGTTFWGQEMNGFDEVLIPRFMGADSMVNPGQKLDFERFGNDMLLDFYKAERDAIAEICPDKPFTTNFMVSTDQCCMDYAAWAKEVNFVSNDHYFHEGESHLDELACSDALMDSLALGKPWYVMEHSTSAVQWKPLNTRKRKGETVRDSLAHVAMGADAINFFQWRASAFGAEAFHSAMVPHAGEDTKLFRQVCELGASLHTLADAGVQGTELAHSDTAILFSAESEWATRSQTLPSMKLNHWHDVRDWYRAFLDAGSRADIVPLAYDWSSYKTVVLPTVLILSAADTQRLADFAAAGGRVVVGYATGLIDEHFHTWLGGYPGAGDGLLRSMLGVRGEEFNILGAEAEGEPGEIRLSSADDSAALDGTTTRLWQNDVNVTGEHAQVLATYAGEEADEWELDGTAAVTRNPYGSGEAYFVGCDLDVADLTKLVRAYLAASSQENADVLHTVRASADATFDFYLPRGKKTVELQGIEGEPVILFQTDREEKPGSYTVRRNGVLVVRR | 3.2.1.23 | null | carbohydrate metabolic process [GO:0005975] | beta-galactosidase complex [GO:0009341] | beta-galactosidase activity [GO:0004565] | PF02449;PF08532; | 3.40.50.880;3.20.20.80; | Glycosyl hydrolase 42 family | PTM: The N-terminus is blocked. | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.; EC=3.2.1.23; Evidence={ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=60 mM for Gal(beta1-4)Gal (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628}; KM=2.2 mM for p-nitrophenyl-beta-D-galactopyranoside (PNPG) (at 40 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628}; KM=2.2 mM for beta-D-Galp-(1->4)-beta-D-Galp-(1->4)-D-Glcp (at 40 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628}; KM=4 mM for beta-D-Galp-(1->4)-beta-D-Galp-(1->4)-beta-D-Galp-(1->4)-D-Glcp (at 40 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628}; KM=3.7 mM for beta-D-Galp-(1->4)-D-Galp (at 40 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628}; KM=6.4 mM for beta-D-Galp-(1->4)-beta-D-Galp-(1->4)-D-Galp (at 40 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628}; KM=5.2 mM for beta-D-Galp-(1->4)-beta-D-Galp-(1->4)-beta-D-Galp-(1->4)-D-Galp (at 40 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628}; Vmax=1.129 umol/min/mg enzyme with Gal(beta1-4)Gal as substrate (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum is pH 6.0 using PNPG or TOS as substrate. Not active below pH 5. {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius using PNPG as substrate (PubMed:15480628). Optimum temperature is 35 degrees Celsius using TOS as substrate (PubMed:10742215). Stable at 40 degrees Celsius. Half-life time at 50 degrees Celsius is 10 minutes. {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628}; | FUNCTION: Involved in the hydrolysis of transgalactooligosaccharides (TOS). Highly active towards Gal(beta1-4)Gal and Gal(beta1-4)-Gal-containing oligosaccharides. Low activity towards Gal(beta1-3)Gal, lactose and Gal(beta1-3)GalOMe. No activity towards Gal(beta1-6)Gal, Gal(beta1-4)Man, Gal(alpha1-4)Gal, Gal(alpha1-3)Gal(beta1-4)Gal, lactulose, 3'fucosyllactose, lacto-N-fucopentaose I, lacto-N-fucopentaose II, cellobiose, maltose or sucrose. No transglycosylation activity is found at high substrate concentrations (100 mg/ml) and only low transglycosylation activity at lower substrate concentrations (10 mg/ml). {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628}. | Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) |
A1A4I4 | PKN1_BOVIN | MASDAVQSEPRSWSLLEQLGLAGADLAAPGVQQQLELERERLRREIRKELKLKEGAENLRRATTDLGRNLGPVELVLRGSSRRLALLHQQLQELHAHVVLPDPAVGVHDAPQSPGTGDSACSATNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLHRALQACQLESQAAPDEAQGSPDLGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLREALERRLGELPADHPKGRLLREELAAASSAAFSARLAGPFPATHYSTLSKPAPLTGTLEVRVVGCRDLPETIPWNPSPSVGGPGTPDSRTPFLSRPARGLYSRTGSLSGRSSLKAEAENTNEVSTVLKLDNTVVGQTSWKPCGPNAWDQSFTLELERARELELAVFWRDQRGLCALKFLKLEDFLDNERHEVQLDMEPQGCLVAEVTFRNPVIERIPRLRRQKKIFSKQQGKAFQRARQMNIDVATWVRLLRRLIPNATATGTFSPGASPGPEARSTGDISVEKLNLGTETDSSPQKSPLGPPSSPSSLSSPIQATTTTPELPSETQETPGPTLCSPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTNAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAVFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWDALLARRLPPPFVPTLAGRTDVSNFDEEFTGEAPTLSPPRDARPLTATEQAAFRDFDFVAGSC | 2.7.11.13 | null | B cell apoptotic process [GO:0001783]; B cell homeostasis [GO:0001782]; epithelial cell migration [GO:0010631]; hyperosmotic response [GO:0006972]; intracellular signal transduction [GO:0035556]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of protein phosphorylation [GO:0001933]; post-translational protein modification [GO:0043687]; protein phosphorylation [GO:0006468]; regulation of cell motility [GO:2000145]; regulation of germinal center formation [GO:0002634]; regulation of immunoglobulin production [GO:0002637]; regulation of transcription by RNA polymerase II [GO:0006357]; renal system process [GO:0003014]; spleen development [GO:0048536] | cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; endosome [GO:0005768]; midbody [GO:0030496]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; chromatin binding [GO:0003682]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; histone binding [GO:0042393]; histone deacetylase binding [GO:0042826]; histone H3T11 kinase activity [GO:0035402]; nuclear androgen receptor binding [GO:0050681]; nuclear receptor coactivator activity [GO:0030374]; protein kinase C binding [GO:0005080]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; small GTPase binding [GO:0031267] | PF02185;PF00069;PF00433; | 1.10.287.160;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | PTM: Autophosphorylated; preferably on serine. Phosphorylated during mitosis. {ECO:0000250|UniProtKB:Q16512}.; PTM: Activated by limited proteolysis with trypsin. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16512}. Nucleus {ECO:0000250|UniProtKB:Q16512}. Endosome {ECO:0000250|UniProtKB:Q16512}. Cell membrane {ECO:0000250|UniProtKB:Q63433}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q63433}. Cleavage furrow {ECO:0000250|UniProtKB:Q16512}. Midbody {ECO:0000250|UniProtKB:Q16512}. Note=Associates with chromatin in a ligand-dependent manner. Localization to endosomes is mediated via its interaction with RHOB. Association to the cell membrane is dependent on Ser-377 phosphorylation. Accumulates during telophase at the cleavage furrow and finally concentrates around the midbody in cytokinesis. {ECO:0000250|UniProtKB:Q16512, ECO:0000250|UniProtKB:Q63433}. | 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=2.7.11.13; Evidence={ECO:0000250|UniProtKB:Q16512}; 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=2.7.11.13; Evidence={ECO:0000250|UniProtKB:Q16512}; | null | null | null | null | FUNCTION: PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro. {ECO:0000250|UniProtKB:Q16512}. | Bos taurus (Bovine) |
A1A4I9 | UFL1_BOVIN | MADAWEEIRRLAADFQRAQFAEATQRLSERNCIEIVNKLIAQKQLEVVHTLDGKEYITPAQISKEMRDELHVRGGRVNIVDLQQAINVDLTHIENRIGDIVKSEKHVQLVLGQLIDENYLDRLAEEVNDKLQESGQVTIAELCKTYDLPGNFLTQALTQRLGRIINGHIDLDNRGVIFTEAFVSRHKARIRGLFSAITRPTAVNSLISRYGFQEQLLYSVLEELVNDGRLRGTVVGGRQDKAVFIPDIYSRTQSTWVDSFLRQNGYLEFDALSRLGIPDAMSYIKKRYKTTQLLFLKAACVGQGLVDQVEASVEEAISSGTWVDIAPLLPSSLSVEDAAILLQHVMRALSKQASAVVFSDTIVVSEKFINDCTDLFSELMHQKAEKEMKNNPVHLITEEDLKQISILESINTSKKDKKDERRRKATEGSGSVRGGGGSNAREYKIKKTKKKGRKDDDSDDESSHTGKKKPEITFMFQDEIEDFLRKHLQDAPEEFISELAEYLIKPLNKTYLEVVHSVYMSSTSSASGTGRKRTIKDLQEEVSNLYNNIRLFEKGMKFFTDDTQAALTKHLLKTVCTDITNLVFNFLASDLMMAVDDPATITSEVRKKILSKLSEETKVALTKLHNSLNEKSIEDFLACLDSAAEACDIMLKKGDKKRERQVLFQHRQALVEQLKVTEDPALTLHLTSVLLFQFSTHSMLHAPGRCVPQIIAFLSSKIPEDQHALLVKYQGLVVKHLVSQNKKTGQGEDPLSDELDKEQEDIINTTRKELQELSSSIKDLVLKSRKSSVTEE | 2.3.2.- | null | DNA damage checkpoint signaling [GO:0000077]; DNA repair [GO:0006281]; erythrocyte differentiation [GO:0030218]; hematopoietic stem cell differentiation [GO:0060218]; negative regulation of IRE1-mediated unfolded protein response [GO:1903895]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of protein ubiquitination [GO:0031397]; positive regulation of autophagy [GO:0010508]; protein K69-linked ufmylation [GO:1990592]; protein ufmylation [GO:0071569]; regulation of canonical NF-kappaB signal transduction [GO:0043122]; regulation of inflammatory response [GO:0050727]; regulation of intracellular estrogen receptor signaling pathway [GO:0033146]; regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032434]; response to endoplasmic reticulum stress [GO:0034976]; reticulophagy [GO:0061709] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]; site of double-strand break [GO:0035861] | UFM1 ligase activity [GO:0061666]; UFM1 transferase activity [GO:0071568] | PF09743; | null | UFL1 family | PTM: Ubiquitinated, leading to its degradation by the proteasome. Interaction with CDK5RAP3 protects both proteins against ubiquitination and degradation via the proteasome. {ECO:0000250|UniProtKB:O94874}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O94874}. Cytoplasm, cytosol {ECO:0000269|PubMed:30881595, ECO:0000269|PubMed:31721015}. Nucleus {ECO:0000269|PubMed:30881595, ECO:0000269|PubMed:31721015}. Chromosome {ECO:0000250|UniProtKB:O94874}. Note=Recruited to double-strand breaks by the MRE11-RAD50-NBN (MRN) complex following DNA damage. {ECO:0000250|UniProtKB:O94874}. | null | null | null | null | null | FUNCTION: E3 protein ligase that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to lysine residues on target proteins, and which plays a key role in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress (By similarity). In response to endoplasmic reticulum stress, recruited to the endoplasmic reticulum membrane by DDRGK1, and mediates ufmylation of proteins such as RPN1 and RPL26/uL24, thereby promoting reticulophagy of endoplasmic reticulum sheets (By similarity). Ufmylation-dependent reticulophagy inhibits the unfolded protein response (UPR) via ERN1/IRE1-alpha (By similarity). Ufmylation in response to endoplasmic reticulum stress is essential for processes such as hematopoiesis, blood vessel morphogenesis or inflammatory response (PubMed:30881595). Regulates inflammation in response to endoplasmic reticulum stress by promoting reticulophagy, leading to inhibit the activity of the NF-kappa-B transcription factor (PubMed:30881595, PubMed:31078114, PubMed:31721015, PubMed:32050508). Mediates ufmylation of DDRGK1 and CDK5RAP3; the role of these modifications is however unclear: as both DDRGK1 and CDK5RAP3 act as substrate adapters for ufmylation, it is uncertain whether ufmylation of these proteins is a collateral effect or is required for ufmylation (By similarity). Catalyzes ufmylation of various subunits of the ribosomal complex or associated components, such as RPS3/uS3, RPS20/uS10, RPL10/uL16, RPL26/uL24 and EIF6 (By similarity). Anchors CDK5RAP3 in the cytoplasm, preventing its translocation to the nucleus which allows expression of the CCND1 cyclin and progression of cells through the G1/S transition (By similarity). Also involved in the response to DNA damage: recruited to double-strand break sites following DNA damage and mediates monoufmylation of histone H4 and ufmylation of MRE11 (By similarity). Catalyzes ufmylation of TRIP4, thereby playing a role in nuclear receptor-mediated transcription (By similarity). Required for hematopoietic stem cell function and hematopoiesis. Required for cardiac homeostasis (By similarity). {ECO:0000250|UniProtKB:O94874, ECO:0000250|UniProtKB:Q8CCJ3, ECO:0000269|PubMed:30881595, ECO:0000269|PubMed:31078114, ECO:0000269|PubMed:31721015, ECO:0000269|PubMed:32050508}. | Bos taurus (Bovine) |
A1A4J1 | PFKAL_BOVIN | MASVDLEKLRTTGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVEGGENIKQANWLSVSNIIQLGGTVIGSARCKAFTTREGRRAAAYNLVQRGITNLCVIGGDGSLTGANIFRSEWGSLLEELVSEGKISEGTAQTYSHLNIAGLVGSIDNDFCGTDMTIGTDSALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWENFMCERLGETRSRGSRLNIIIIAEGAIDRNGKPISSRYVKDLVVQRLGFDTRVTVLGHVQRGGTPSAFDRILSSKMGMEAVMALLEATPDTPACVVSLSGNQSVRLPLMECVQMTKEVQKAMDEKRFDEAIQLRGGSFENNWNIYKLLSHQKISKEKTNFSLAILNVGAPAAGMNAAVRSAVRSGISQGHTVYVVHDGFEGLAKNQVQEVSWHDVAGWLGRGGSMLGTKRTLPKGFMEKIVENIRLHNIHALLVIGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLGSDTAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNIQDLKANVEHMTEKMKTEIQRGLVLRNEKCHEHYTTEFLYNLYSSEGKGVFDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKAIIWMSEKLRAVYRNGRVFANASDSACVIGLQKKVVAFSPVTELKKDTDFEHRMPREQWWLNLRLMLKMLAHYRISMADYVSGELEHVTRRTLSIETGF | 2.7.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03184}; | canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; glycolytic process [GO:0006096]; negative regulation of insulin secretion [GO:0046676]; response to glucose [GO:0009749] | 6-phosphofructokinase complex [GO:0005945]; membrane [GO:0016020] | 6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; fructose binding [GO:0070061]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029] | PF00365; | 3.40.50.450;3.40.50.460; | Phosphofructokinase type A (PFKA) family, ATP-dependent PFK group I subfamily, Eukaryotic two domain clade 'E' sub-subfamily | PTM: GlcNAcylation at Ser-529 by OGT decreases enzyme activity, leading to redirect glucose flux through the oxidative pentose phosphate pathway. Glycosylation is stimulated by both hypoxia and glucose deprivation (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}. | CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03184}; | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_03184}. | null | null | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (By similarity). Negatively regulates the phagocyte oxidative burst in response to bacterial infection by controlling cellular NADPH biosynthesis and NADPH oxidase-derived reactive oxygen species. Upon macrophage activation, drives the metabolic switch toward glycolysis, thus preventing glucose turnover that produces NADPH via pentose phosphate pathway (By similarity). {ECO:0000250|UniProtKB:P12382, ECO:0000255|HAMAP-Rule:MF_03184}. | Bos taurus (Bovine) |
A1A4K3 | DDB1_BOVIN | MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLEIYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFILTAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGIIGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLEELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREKEFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYHNGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRLFMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNGVVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIVDMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIGIHEHASIDLPGIKGLWPLRSDPNRETDDTLVLSFVGQTRVLMLNGEEVEETELMGFVDDQQTFFCGNVAHQQLIQITSASVRLVSQEPKALVSEWKEPQGKNISVASCNSSQVVVAVGRALYYLQIHPQELRQISHTEMEHEVACLDITPLGDSNGMSPLCAIGLWTDISARIAKLPSFELLHKEMLGGEIIPRSILMTTFESSHYLLCALGDGALFYFGLNIETGLLSDRKKVTLGTQPTVLRTFRSLSTTNVFACSDRPTVIYSSNHKLVFSNVNLKEVNYMCPLNSDGYPDSLALANNSTLTIGTIDEIQKLHIRTVPLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALRPSASTQALSSSVSSSKLFSSSTAPHETSFGEEVEVHNLLIIDQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTAMVYPEEAEPKQGRIVVFQYSDGKLQTVAEKEVKGAVYSMVEFNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYLKTKGDFILVGDLMRSVLLLAYKPMEGNFEEIARDFNPNWMSAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQEVGLFHLGEFVNVFCHGSLVMQNLGETSTPTQGSVLFGTVNGMIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWRSFHTERKTEPATGFIDGDLIESFLDISRPKMQEVVANLQYDDGSGMKREATADDLIKVVEELTRIH | null | null | DNA repair [GO:0006281]; positive regulation of gluconeogenesis [GO:0045722]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]; regulation of circadian rhythm [GO:0042752]; rhythmic process [GO:0048511]; ubiquitin-dependent protein catabolic process [GO:0006511] | Cul4-RING E3 ubiquitin ligase complex [GO:0080008]; Cul4A-RING E3 ubiquitin ligase complex [GO:0031464]; Cul4B-RING E3 ubiquitin ligase complex [GO:0031465]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861] | DNA binding [GO:0003677] | PF03178;PF10433; | 1.10.150.910;2.130.10.10; | DDB1 family | PTM: Phosphorylated by ABL1. {ECO:0000250|UniProtKB:Q3U1J4}.; PTM: Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin-dependent proteolysis. {ECO:0000250|UniProtKB:Q16531}.; PTM: Acetylated, promoting interaction with CUL4 (CUL4A or CUL4B) and subsequent formation of DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes. Deacetylation by SIRT7 impairs the interaction with CUL4 (CUL4A or CUL4B) and formation of DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes. {ECO:0000250|UniProtKB:Q16531}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16531}. Nucleus {ECO:0000250|UniProtKB:Q16531}. Note=Primarily cytoplasmic. Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage. More concentrated in nuclei than in cytoplasm in germinal vesicle (GV) stage oocytes, zygotes and the 2-cell stage, but distributed in the cytoplasm at the MII-stage oocytes (By similarity). {ECO:0000250|UniProtKB:Q16531, ECO:0000250|UniProtKB:Q3U1J4}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q16531}. | null | null | FUNCTION: Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively. Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1. DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage. The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (By similarity). DDB1-mediated CRY1 degradation promotes FOXO1 protein stability and FOXO1-mediated gluconeogenesis in the liver (By similarity). By acting on TET dioxygenses, essential for oocyte maintenance at the primordial follicle stage, hence essential for female fertility (By similarity). Maternal factor required for proper zygotic genome activation and genome reprogramming (By similarity). {ECO:0000250|UniProtKB:Q16531, ECO:0000250|UniProtKB:Q3U1J4}. | Bos taurus (Bovine) |
A1A4K5 | ENPP2_BOVIN | MARRRSCQLHQVISLFTFAVGVNICLGVTANRIKRAEGWGEGPPTVLSDSPSINISGSCKGRCFELQEAGPPDCRCDNLCKSYSSCCLDFDELCLKTAGGWECTKDRCGEVRNEDHACHCSEDCLARGDCCTNYQVVCKGESHWVDDDCEEIKTPECPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDAHFNLRGREKFNHRWWGGQPLWITATKQGVIAGTFFWPVVIPHERRILTILQWLTLPDHERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLRDIDKTVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYLTNVDDIILVPGTLGRIRPKFNNHAKYDPKVIIANLTCKKPDQHFKPYLKQHLPKRLHYANNRRIEDVHLLVERRWHVARKPLEVYKKPSGKCFFQGDHGFDNKVNSMQTVFVGYGPTFKYKTKVPPFENIELYNVMCDLLGLKPAPNNGTHGSLNHLLRTNTFRPTVPEEVTRPNYPGVMYLQSDFDLGCTCDDKAEPKNKLDELNKHLHIKESTEAETRKFRGSKNEIKENVNGNFEPRKERHLLYGRPAVLYRTRYDILYHTDFESGYSEIFLMPLWTSYTVSKQADVSDIPAHLTNCVRPDVRVSPSFSQSCLAYKNDKQMSYGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRIWNYFQRVLVKKYASERNGVNVISGPIFDYDYDGLHDTQDKIKQYVEGSSVPVPTHYYSILTSCLDFTQPADRCDGPLSVSAFVLPHRPDNDESCNSSEDESKWVEELLKMHTARVRDIEHLTSLDFFRKTSRSYPEILTLKTYLQTYESEI | 3.1.4.39 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q13822}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q13822}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q13822}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:Q13822}; | chemotaxis [GO:0006935]; estrous cycle [GO:0044849]; immune response [GO:0006955]; phosphatidylcholine catabolic process [GO:0034638]; phospholipid catabolic process [GO:0009395]; sphingolipid catabolic process [GO:0030149] | extracellular space [GO:0005615] | alkylglycerophosphoethanolamine phosphodiesterase activity [GO:0047391]; calcium ion binding [GO:0005509]; lysophospholipase activity [GO:0004622]; nucleic acid binding [GO:0003676]; phosphodiesterase I activity [GO:0004528]; polysaccharide binding [GO:0030247]; scavenger receptor activity [GO:0005044]; zinc ion binding [GO:0008270] | PF01223;PF01663;PF01033; | 4.10.410.20;3.40.720.10;3.40.570.10; | Nucleotide pyrophosphatase/phosphodiesterase family | PTM: N-glycosylation, but not furin-cleavage, plays a critical role on secretion and on lysoPLD activity. {ECO:0000250|UniProtKB:Q9R1E6}.; PTM: The interdomain disulfide bond between Cys-414 and Cys-831 is essential for catalytic activity. {ECO:0000250|UniProtKB:Q9R1E6}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12119361}. | CATALYTIC ACTIVITY: Reaction=1-O-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-O-alkyl-sn-glycero-3-phosphate + ethanolamine + H(+); Xref=Rhea:RHEA:15965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57603, ChEBI:CHEBI:58014, ChEBI:CHEBI:76168; EC=3.1.4.39; Evidence={ECO:0000269|PubMed:12119361}; CATALYTIC ACTIVITY: Reaction=1-O-(9Z-octadecenyl)-sn-glycero-3-phosphocholine + H2O = 1-O-(9Z-octadecenyl)-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41684, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64396, ChEBI:CHEBI:78402; Evidence={ECO:0000250|UniProtKB:Q13822}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41685; Evidence={ECO:0000250|UniProtKB:Q13822}; CATALYTIC ACTIVITY: Reaction=a 2-acyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycerol 3-phosphate + choline + H(+); Xref=Rhea:RHEA:41712, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57875, ChEBI:CHEBI:64982; Evidence={ECO:0000250|UniProtKB:Q13822}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41713; Evidence={ECO:0000250|UniProtKB:Q13822}; CATALYTIC ACTIVITY: Reaction=a 2-acyl-sn-glycero-3-phospho-L-serine + H2O = a 2-acyl-sn-glycerol 3-phosphate + H(+) + L-serine; Xref=Rhea:RHEA:41716, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:64982, ChEBI:CHEBI:65214; Evidence={ECO:0000250|UniProtKB:Q13822}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41717; Evidence={ECO:0000250|UniProtKB:Q13822}; CATALYTIC ACTIVITY: Reaction=1-dodecanoyl-sn-glycero-3-phosphocholine + H2O = 1-dodecanoyl-sn-glycerol 3-phosphate + choline + H(+); Xref=Rhea:RHEA:38991, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72682, ChEBI:CHEBI:74966; Evidence={ECO:0000250|UniProtKB:Q13822}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38992; Evidence={ECO:0000250|UniProtKB:Q13822}; CATALYTIC ACTIVITY: Reaction=H2O + sphing-4-enine-phosphocholine = choline + H(+) + sphing-4-enine 1-phosphate; Xref=Rhea:RHEA:38919, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58906, ChEBI:CHEBI:60119; Evidence={ECO:0000250|UniProtKB:Q13822}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38920; Evidence={ECO:0000250|UniProtKB:Q13822}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:38915, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28610, ChEBI:CHEBI:74544; Evidence={ECO:0000250|UniProtKB:Q13822}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38916; Evidence={ECO:0000250|UniProtKB:Q13822}; CATALYTIC ACTIVITY: Reaction=1-tetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-tetradecanoyl-sn-glycerol 3-phosphate + choline + H(+); Xref=Rhea:RHEA:38983, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64489, ChEBI:CHEBI:72683; Evidence={ECO:0000250|UniProtKB:Q13822}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38984; Evidence={ECO:0000250|UniProtKB:Q13822}; CATALYTIC ACTIVITY: Reaction=1-decanoyl-sn-glycero-3-phosphocholine + H2O = 1-decanoyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41131, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:77724, ChEBI:CHEBI:77726; Evidence={ECO:0000250|UniProtKB:Q13822}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41132; Evidence={ECO:0000250|UniProtKB:Q13822}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:38975, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:72998; Evidence={ECO:0000250|UniProtKB:Q13822}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38976; Evidence={ECO:0000250|UniProtKB:Q13822}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-octadecanoyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:38979, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73858, ChEBI:CHEBI:74565; Evidence={ECO:0000250|UniProtKB:Q13822}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38980; Evidence={ECO:0000250|UniProtKB:Q13822}; CATALYTIC ACTIVITY: Reaction=1-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine + H2O = 1-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41135, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28733, ChEBI:CHEBI:74547; Evidence={ECO:0000250|UniProtKB:Q13822}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41136; Evidence={ECO:0000250|UniProtKB:Q13822}; CATALYTIC ACTIVITY: Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41139, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74344, ChEBI:CHEBI:74938; Evidence={ECO:0000250|UniProtKB:Q13822}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41140; Evidence={ECO:0000250|UniProtKB:Q13822}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41143, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64496, ChEBI:CHEBI:77580; Evidence={ECO:0000250|UniProtKB:Q13822}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41144; Evidence={ECO:0000250|UniProtKB:Q13822}; CATALYTIC ACTIVITY: Reaction=1-hexanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexanoyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41400, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:78215, ChEBI:CHEBI:78223; Evidence={ECO:0000250|UniProtKB:Q13822}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41401; Evidence={ECO:0000250|UniProtKB:Q13822}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phosphocholine + H2O = 1,2-dioctanoyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41416, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:78228, ChEBI:CHEBI:78229; Evidence={ECO:0000250|UniProtKB:Q13822}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41417; Evidence={ECO:0000250|UniProtKB:Q13822}; CATALYTIC ACTIVITY: Reaction=1,2-didecanoyl-sn-glycero-3-phosphocholine + H2O = 1,2-didecanoyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41412, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:78226, ChEBI:CHEBI:78227; Evidence={ECO:0000250|UniProtKB:Q13822}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41413; Evidence={ECO:0000250|UniProtKB:Q13822}; CATALYTIC ACTIVITY: Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + H2O = 1-O-(1Z-alkenyl)-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41588, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:77283, ChEBI:CHEBI:77287; Evidence={ECO:0000250|UniProtKB:Q13822}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41589; Evidence={ECO:0000250|UniProtKB:Q13822}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ethanolamine + H(+); Xref=Rhea:RHEA:38927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57603, ChEBI:CHEBI:74544, ChEBI:CHEBI:74971; Evidence={ECO:0000250|UniProtKB:Q64610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38928; Evidence={ECO:0000250|UniProtKB:Q64610}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + L-serine; Xref=Rhea:RHEA:38931, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:74544, ChEBI:CHEBI:74617; Evidence={ECO:0000250|UniProtKB:Q64610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38932; Evidence={ECO:0000250|UniProtKB:Q64610}; | null | null | null | null | FUNCTION: Hydrolyzes lysophospholipids to produce the signaling molecule lysophosphatidic acid (LPA) in extracellular fluids. Major substrate is lysophosphatidylcholine (PubMed:12119361). Can also act on sphingosylphosphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP. Involved in several motility-related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation. Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein. May have a role in induction of parturition. Possible involvement in cell proliferation and adipose tissue development. Tumor cell motility-stimulating factor (By similarity). Required for LPA production in activated platelets, cleaves the sn-1 lysophospholipids to generate sn-1 lysophosphatidic acids containing predominantly 18:2 and 20:4 fatty acids (By similarity). Shows a preference for the sn-1 to the sn-2 isomer of 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) (By similarity). {ECO:0000250|UniProtKB:Q13822, ECO:0000269|PubMed:12119361}. | Bos taurus (Bovine) |
A1A4L1 | THEM4_BOVIN | MLRSCTAGLRSIWALRGRREGAPRLSMDLQPARRLFSTEKVIHKDWALPNPSWSKDLKLLFDQFMKKCEDGSWERLPSYKRRSTQESEDFKTYFLDPKLVEEERLSQAQLFTRGFEDGLGFEYVIFKNNDEKRTVCLFQGGPYLQGVPGLLHGGAMATMIDIALGSCTGGAVMTANLNINFKRPVPLCSVVVINSQLDKLEGRKLFLSCNVRSVDEKTLYSEATGLFIKLDPEKSST | 3.1.2.2 | null | fatty acid metabolic process [GO:0006631]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; regulation of mitochondrial membrane permeability involved in apoptotic process [GO:1902108] | cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; ruffle membrane [GO:0032587] | long-chain fatty acyl-CoA hydrolase activity [GO:0052816] | PF03061; | 3.10.129.10; | THEM4/THEM5 thioesterase family | PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q5T1C6}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5T1C6}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q5T1C6}. Cytoplasm {ECO:0000250|UniProtKB:Q5T1C6}. Mitochondrion {ECO:0000250|UniProtKB:Q5T1C6}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q5T1C6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5T1C6}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q5T1C6}. Note=Released from the mitochondria into the cytosol in response to apoptotic stimuli. {ECO:0000250|UniProtKB:Q5T1C6}. | CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence={ECO:0000250|UniProtKB:Q5T1C6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000250|UniProtKB:Q5T1C6}; CATALYTIC ACTIVITY: Reaction=H2O + octanoyl-CoA = CoA + H(+) + octanoate; Xref=Rhea:RHEA:30143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386; Evidence={ECO:0000250|UniProtKB:Q5T1C6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144; Evidence={ECO:0000250|UniProtKB:Q5T1C6}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+); Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430; Evidence={ECO:0000250|UniProtKB:Q5T1C6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; Evidence={ECO:0000250|UniProtKB:Q5T1C6}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+); Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375; Evidence={ECO:0000250|UniProtKB:Q5T1C6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence={ECO:0000250|UniProtKB:Q5T1C6}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate; Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385; Evidence={ECO:0000250|UniProtKB:Q5T1C6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence={ECO:0000250|UniProtKB:Q5T1C6}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000250|UniProtKB:Q5T1C6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; Evidence={ECO:0000250|UniProtKB:Q5T1C6}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA + H(+); Xref=Rhea:RHEA:40151, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368; Evidence={ECO:0000250|UniProtKB:Q5T1C6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40152; Evidence={ECO:0000250|UniProtKB:Q5T1C6}; | null | null | null | null | FUNCTION: Has acyl-CoA thioesterase activity towards medium and long-chain (C14 to C18) fatty acyl-CoA substrates, and probably plays a role in mitochondrial fatty acid metabolism (By similarity). Plays a role in the apoptotic process, possibly via its regulation of AKT1 activity (By similarity). {ECO:0000250|UniProtKB:Q5T1C6}. | Bos taurus (Bovine) |
A1A4L8 | MOCS3_BOVIN | MAAREEVLALQAEVAQREEELSSLKQRLAAALSTGQESARSVPVSPLPPRAALSREEIRRYSRQLVLPELGMQGQLRLAAAAVLVVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEASNLARQVLHGEALAGQAKVFSAAAALRRLNSAVECVPYAQALTPATALDLVRRYDVVADCSDNAPTRYLVSDACVLAGRPLVSASALRFEGQLTVYHYGGGPCYRCVFPRPPPAETVTSCADGGVLGAVTGVLGCLQALEVLKTAAGLGPSYSGRLLLFDALRGDFRCIRLRRRRPDCAACGERPTVTDLQDYESFCGSSATDKCRSLRLLSPEERISIMDYKRLLDSRSPHLLLDVRPQVEVDICRLPHALHIPLKSLERRDAESLKVLGEAIREGKQGAQEGASVPIYVICKLGNDSQKAVKILQSWADLDSLTVKDVVGGLMAWAAKIDGTFPQY | 2.7.7.80; 2.8.1.11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049}; | Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; protein urmylation [GO:0032447]; tRNA thio-modification [GO:0034227]; tRNA wobble position uridine thiolation [GO:0002143]; tRNA wobble uridine modification [GO:0002098] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; molybdopterin-synthase adenylyltransferase activity [GO:0061605]; molybdopterin-synthase sulfurtransferase activity [GO:0061604]; nucleotidyltransferase activity [GO:0016779]; sulfotransferase activity [GO:0008146]; sulfurtransferase activity [GO:0016783]; thiosulfate sulfurtransferase activity [GO:0004792]; URM1 activating enzyme activity [GO:0042292] | PF00581;PF00899; | 3.40.50.720;3.40.250.10; | HesA/MoeB/ThiF family, UBA4 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}. | CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618, ChEBI:CHEBI:90778; EC=2.7.7.80; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + A + AMP + H(+) + L-cysteinyl-[cysteine desulfurase]; Xref=Rhea:RHEA:48612, Rhea:RHEA-COMP:12157, Rhea:RHEA-COMP:12158, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12160, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950, ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, ChEBI:CHEBI:90619, ChEBI:CHEBI:456215; EC=2.8.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; | null | PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.; PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}. | null | null | FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 acting as a sulfur donor for thiocarboxylation reactions. {ECO:0000255|HAMAP-Rule:MF_03049}. | Bos taurus (Bovine) |
A1A4N1 | S29A3_BOVIN | MAIISEDDFRHTSNSTYRTASSSLRADQEALLEKLLDRPPPSLQRPEDRFNGTYIIFFSLGIGGLLPWNFFVTAQEYWIFKLSNCSSPAAGEEPKDSDILNYFESYLAVASTVPSVLCLALNFLLVNRVPIRVRVLASLTVMLAIFIVMTVLVKVDTSSWTHSFFTITITCMAILSGTSTIFNSSVFGMTGSFPMRNSQALISGGAMGGTLSAVASLVDLAVASDVTDSTLAFFLTADIFLALCIGLYLLLPRLDYARYYMKPVWPTVFSGEEQLPQDSPSPTSVAPGSSDPQTPPLGPILKKTTGLGFCIIYLFFITSLIFPAICTNIESLSKGSGSPWSTKFFVPLTTFLLYNFADLCGRQVTAWIQVPGPRSKALPGLALLRTCFVPLFVFCNYQPRGHLHTVLFQSDVYPVLFTSLLGLSNGYLSTLALIYGPKIVPRELAEATGVVMTFYMGLGLVLGSACSALLVHLI | null | null | adenosine transport [GO:0032238]; cytidine transport [GO:0015861]; dopamine transport [GO:0015872]; guanine transmembrane transport [GO:1903716]; inosine transport [GO:0035340]; norepinephrine transport [GO:0015874]; nucleobase transport [GO:0015851]; nucleoside transmembrane transport [GO:1901642]; nucleoside transport [GO:0015858]; purine nucleobase transmembrane transport [GO:1904823]; pyrimidine nucleobase transmembrane transport [GO:1904082]; serotonin transport [GO:0006837]; uracil transmembrane transport [GO:1903791]; uridine transport [GO:0015862] | Golgi apparatus [GO:0005794]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; mitochondrial membrane [GO:0031966]; plasma membrane [GO:0005886] | cytidine transmembrane transporter activity [GO:0015212]; guanine transmembrane transporter activity [GO:0015208]; monoamine transmembrane transporter activity [GO:0008504]; neurotransmitter transmembrane transporter activity [GO:0005326]; nucleobase transmembrane transporter activity [GO:0015205]; nucleoside transmembrane transporter activity [GO:0005337]; organic cation transmembrane transporter activity [GO:0015101]; uracil transmembrane transporter activity [GO:0015210]; uridine transmembrane transporter activity [GO:0015213] | PF01733; | null | SLC29A/ENT transporter (TC 2.A.57) family | null | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9BZD2}; Multi-pass membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:Q9BZD2}; Multi-pass membrane protein {ECO:0000305}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9BZD2}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:Q9BZD2}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=adenosine(in) = adenosine(out); Xref=Rhea:RHEA:75343, ChEBI:CHEBI:16335; Evidence={ECO:0000250|UniProtKB:Q9BZD2}; CATALYTIC ACTIVITY: Reaction=guanosine(in) = guanosine(out); Xref=Rhea:RHEA:75371, ChEBI:CHEBI:16750; Evidence={ECO:0000250|UniProtKB:Q9BZD2}; CATALYTIC ACTIVITY: Reaction=inosine(in) = inosine(out); Xref=Rhea:RHEA:75375, ChEBI:CHEBI:17596; Evidence={ECO:0000250|UniProtKB:Q9BZD2}; CATALYTIC ACTIVITY: Reaction=uridine(out) = uridine(in); Xref=Rhea:RHEA:71519, ChEBI:CHEBI:16704; Evidence={ECO:0000250|UniProtKB:Q9BZD2}; CATALYTIC ACTIVITY: Reaction=cytidine(in) = cytidine(out); Xref=Rhea:RHEA:75367, ChEBI:CHEBI:17562; Evidence={ECO:0000250|UniProtKB:Q9BZD2}; CATALYTIC ACTIVITY: Reaction=thymidine(in) = thymidine(out); Xref=Rhea:RHEA:75363, ChEBI:CHEBI:17748; Evidence={ECO:0000250|UniProtKB:Q9BZD2}; CATALYTIC ACTIVITY: Reaction=2'-deoxyadenosine(in) = 2'-deoxyadenosine(out); Xref=Rhea:RHEA:75691, ChEBI:CHEBI:17256; Evidence={ECO:0000250|UniProtKB:Q9BZD2}; CATALYTIC ACTIVITY: Reaction=2'-deoxycytidine(in) = 2'-deoxycytidine(out); Xref=Rhea:RHEA:75695, ChEBI:CHEBI:15698; Evidence={ECO:0000250|UniProtKB:Q9BZD2}; CATALYTIC ACTIVITY: Reaction=guanine(out) = guanine(in); Xref=Rhea:RHEA:71531, ChEBI:CHEBI:16235; Evidence={ECO:0000250|UniProtKB:Q9BZD2}; CATALYTIC ACTIVITY: Reaction=uracil(in) = uracil(out); Xref=Rhea:RHEA:69404, ChEBI:CHEBI:17568; Evidence={ECO:0000250|UniProtKB:Q9BZD2}; CATALYTIC ACTIVITY: Reaction=(R)-noradrenaline(out) = (R)-noradrenaline(in); Xref=Rhea:RHEA:73871, ChEBI:CHEBI:72587; Evidence={ECO:0000250|UniProtKB:Q9BZD2}; CATALYTIC ACTIVITY: Reaction=dopamine(out) = dopamine(in); Xref=Rhea:RHEA:73863, ChEBI:CHEBI:59905; Evidence={ECO:0000250|UniProtKB:Q9BZD2}; CATALYTIC ACTIVITY: Reaction=serotonin(out) = serotonin(in); Xref=Rhea:RHEA:73867, ChEBI:CHEBI:350546; Evidence={ECO:0000250|UniProtKB:Q9BZD2}; CATALYTIC ACTIVITY: Reaction=tyramine(in) = tyramine(out); Xref=Rhea:RHEA:74783, ChEBI:CHEBI:327995; Evidence={ECO:0000250|UniProtKB:Q9BZD2}; CATALYTIC ACTIVITY: Reaction=ATP(in) = ATP(out); Xref=Rhea:RHEA:75687, ChEBI:CHEBI:30616; Evidence={ECO:0000250|UniProtKB:Q9BZD2}; | null | null | null | null | FUNCTION: Uniporter that mediates the facilitative transport of nucleoside across lysosomal and mitochondrial membranes. Functions as a non-electrogenic Na(+)-independent transporter. Substrate transport is pH-dependent and enhanced under acidic condition, probably reflecting the location of the transporter in acidic intracellular compartments. Proton is not a cotransporting ion but most likely change the ionization state of the transporter which dictates transport-permissible/impermissible conformation for nucleoside translocation. May direct the nucleoside transport from lysosomes to cytosol or cytosol to mitochondria to facilitate the fundamental function of salvage synthesis of nucleic acids. Involved in the transport of nucleosides (adenosine, guanosine, uridine, thymidine, cytidine and inosine) and deoxynucleosides (deoxyadenosine, deoxycytidine). Also mediates transport of purine nucleobases (adenine, guanine) and pyrimidine nucleobases (uracil). Also able to transport monoamine neurotransmitters dopamine, serotonin, noradrenaline and tyramine. Capable of transporting ATP (By similarity). Mediates nucleoside export from lysosomes in macrophages, which regulates macrophage functions and numbers (By similarity). {ECO:0000250|UniProtKB:Q99P65, ECO:0000250|UniProtKB:Q9BZD2}. | Bos taurus (Bovine) |
A1A4Q9 | NUD16_BOVIN | MAGMRRLELSEALHLGPGWRHACHALLYAPDPGLLFGRIPLRYAVLMQMRFDGRLGFPGGFVDLRDGSLEDGLNRELGEELGEAAGAFRVERADYRSSHAGSRPRVVAHFYTKLLTLEQLTAVEMGAPRARDHGLEVLGLVRVPLYTLRDGVGGLPAFLENTFIGNAREQLLEAVQNLGLLEPGSFARLKISTPP | 3.6.1.62; 3.6.1.64 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q96DE0}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q96DE0}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250|UniProtKB:Q96DE0}; Note=Binds 3 or 4 divalent metal cations. Acts specifically on U8 snoRNA with magnesium as cofactor. Has broad substrate specificity with bound manganese or cobalt (in vitro). {ECO:0000250|UniProtKB:Q96DE0}; | dITP catabolic process [GO:0035863]; mRNA catabolic process [GO:0006402]; NAD-cap decapping [GO:0110155]; negative regulation of rRNA processing [GO:2000233]; positive regulation of cell cycle process [GO:0090068]; sno(s)RNA catabolic process [GO:0016077] | cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity [GO:0140933]; chloride ion binding [GO:0031404]; cobalt ion binding [GO:0050897]; dIDP phosphatase activity [GO:0097383]; dITP diphosphatase activity [GO:0035870]; IDP phosphatase activity [GO:1990003]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; metalloexopeptidase activity [GO:0008235]; mRNA binding [GO:0003729]; nucleotide binding [GO:0000166]; phosphodiesterase decapping endonuclease activity [GO:1990174]; protein homodimerization activity [GO:0042803]; RNA NAD-cap (NAD-forming) hydrolase activity [GO:0110152]; snoRNA binding [GO:0030515] | PF00293; | 3.90.79.10; | Nudix hydrolase family, NUDT16 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96DE0}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q6TEC1}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6TEC1}. Cytoplasm {ECO:0000250|UniProtKB:Q96DE0}. Note=Localized predominantly in the cytoplasm. Localized in nucleolus, and in a minor proportion in distinct foci in the nucleoplasm. {ECO:0000250|UniProtKB:Q6TEC1, ECO:0000250|UniProtKB:Q96DE0}. | CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GDP; Xref=Rhea:RHEA:67484, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:63714, ChEBI:CHEBI:138282, ChEBI:CHEBI:156461; EC=3.6.1.62; Evidence={ECO:0000250|UniProtKB:Q96DE0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67485; Evidence={ECO:0000250|UniProtKB:Q96DE0}; CATALYTIC ACTIVITY: Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053, ChEBI:CHEBI:58280; EC=3.6.1.64; Evidence={ECO:0000250|UniProtKB:Q96DE0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208; Evidence={ECO:0000250|UniProtKB:Q96DE0}; CATALYTIC ACTIVITY: Reaction=dIDP + H2O = dIMP + H(+) + phosphate; Xref=Rhea:RHEA:35211, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:61194, ChEBI:CHEBI:62286; EC=3.6.1.64; Evidence={ECO:0000250|UniProtKB:Q96DE0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35212; Evidence={ECO:0000250|UniProtKB:Q96DE0}; CATALYTIC ACTIVITY: Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + H(+) + NAD(+); Xref=Rhea:RHEA:60880, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:15698, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:138282, ChEBI:CHEBI:144029; Evidence={ECO:0000250|UniProtKB:Q96DE0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60881; Evidence={ECO:0000250|UniProtKB:Q96DE0}; CATALYTIC ACTIVITY: Reaction=a 5'-end FAD-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-adenosine-phospho-ribonucleoside in mRNA + FMN + 2 H(+); Xref=Rhea:RHEA:67588, Rhea:RHEA-COMP:15719, Rhea:RHEA-COMP:17275, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58210, ChEBI:CHEBI:144051, ChEBI:CHEBI:172372; Evidence={ECO:0000250|UniProtKB:Q96DE0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67589; Evidence={ECO:0000250|UniProtKB:Q96DE0}; CATALYTIC ACTIVITY: Reaction=a 5'-end CoA-ribonucleoside in mRNA + H2O = (R)-4'-phosphopantetheine + a 5'-end phospho-adenosine-phospho-ribonucleoside in mRNA + 2 H(+); Xref=Rhea:RHEA:67592, Rhea:RHEA-COMP:15719, Rhea:RHEA-COMP:17276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:61723, ChEBI:CHEBI:144051, ChEBI:CHEBI:172371; Evidence={ECO:0000250|UniProtKB:Q6P3D0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67593; Evidence={ECO:0000250|UniProtKB:Q6P3D0}; | null | null | null | null | FUNCTION: RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation. Acts also as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms. The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP. Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions (By similarity). Exhibits decapping activity towards NAD-capped RNAs and FAD-capped RNAs (By similarity). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity). {ECO:0000250|UniProtKB:Q6P3D0, ECO:0000250|UniProtKB:Q96DE0}. | Bos taurus (Bovine) |
A1A4R9 | AP2A_BOVIN | MLWKLTDNIKYEDCEDRHDGASNGTARLPQLGTVGQSPYTSAPPLSHTPNADFQPPYFPPPYQPIYPQSQDPYSHVNDPYSLNPLHAQPQPQHPGWPGQRQSQESGLLHTHRGLPHQLSGLDPRRDYRRHEDLLHGPHGLGSGLGDLPIHSLPHAIEDVPHVEDPGINIPDQTVIKKGPVSLSKSNSNAVSAIPINKDNLFGGVVNPNEVFCSVPGRLSLLSSTSKYKVTVAEVQRRLSPPECLNASLLGGVLRRAKSKNGGRSLREKLDKIGLNLPAGRRKAANVTLLTSLVEGEAVHLARDFGYVCETEFPAKAVAEFLNRQHSDPNEQVTRKNMLLATKQICKEFTDLLAQDRSPLGNSRPNPILEPGIQSCLTHFNLISHGFGSPAVCAAVTALQNYLTEALKAMDKMYLSNNPNSHTDNNAKSSDKEEKHRK | null | null | bone morphogenesis [GO:0060349]; cellular response to iron ion [GO:0071281]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic forelimb morphogenesis [GO:0035115]; eyelid development in camera-type eye [GO:0061029]; inner ear morphogenesis [GO:0042472]; kidney development [GO:0001822]; negative regulation of apoptotic process [GO:0043066]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; negative regulation of transcription by competitive promoter binding [GO:0010944]; negative regulation of transcription by RNA polymerase II [GO:0000122]; oculomotor nerve formation [GO:0021623]; optic cup structural organization [GO:0003409]; optic vesicle morphogenesis [GO:0003404]; positive regulation of bone mineralization [GO:0030501]; positive regulation of tooth mineralization [GO:0070172]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell population proliferation [GO:0042127]; regulation of transcription by RNA polymerase II [GO:0006357]; roof of mouth development [GO:0060021]; sensory perception of sound [GO:0007605]; trigeminal nerve development [GO:0021559] | nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF03299; | null | AP-2 family | PTM: Sumoylated on Lys-10; which inhibits transcriptional activity. {ECO:0000305}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-alpha is the only AP-2 protein required for early morphogenesis of the lens vesicle. Together with the CITED2 coactivator, stimulates the PITX2 P1 promoter transcription activation. Associates with chromatin to the PITX2 P1 promoter region (By similarity). {ECO:0000250}. | Bos taurus (Bovine) |
A1A4S6 | RHG10_HUMAN | MGLQPLEFSDCYLDSPWFRERIRAHEAELERTNKFIKELIKDGKNLIAATKSLSVAQRKFAHSLRDFKFEFIGDAVTDDERCIDASLREFSNFLKNLEEQREIMALSVTETLIKPLEKFRKEQLGAVKEEKKKFDKETEKNYSLIDKHLNLSAKKKDSHLQEADIQVEQNRQHFYELSLEYVCKLQEIQERKKFEFVEPMLSFFQGMFTFYHQGHELAKDFNHYKMELQINIQNTRNRFEGTRSEVEELMNKIRQNPKDHKRASQFTAEGYLYVQEKRPAPFGSSWVKHYCMYRKAAKKFNMIPFEHRSGGKLGDGEVFFLKECTKRHTDSIDRRFCFDIEAADRPGVSLTMQAFSEEERKQWLEALGGKEALSHSFNTAIIPRPEGNAQLDKMGFTIIRKCISAVETRGINDQGLYRVVGVSSKVQRLLSMLMDVKTCNEVDLENSADWEVKTITSALKQYLRSLPEPLMTYELHGDFIVPAKSGSPESRVNAIHFLVHKLPEKNKEMLDILVKHLTNVSNHSKQNLMTVANLGVVFGPTLMRPQEETVAALMDLKFQNIVVEILIENHEKIFRTPPDTTFPEPTCLSASPPNAPPRQSKRQGQRTKRPVAVYNLCLELEDGDNPYPSKEDTPTSSLDSLSSPSPVTTAVPGPPGPDKNHLLADGGSFGDWASTIPGQTRSSMVQWLNPQSPTTTSSNSAVTPLSPGSSPFPFSPPATVADKPPESIRSRKARAVYPCEAEHSSELSFEIGAIFEDVQTSREPGWLEGTLNGKRGLIPQNYVKLL | null | null | cytoskeleton organization [GO:0007010]; negative regulation of apoptotic process [GO:0043066]; regulation of small GTPase mediated signal transduction [GO:0051056]; signal transduction [GO:0007165] | cytosol [GO:0005829]; endosome membrane [GO:0010008]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | GTPase activator activity [GO:0005096] | PF16746;PF00169;PF00620;PF14604; | 1.20.1270.60;2.30.29.30;1.10.555.10;2.30.30.40; | null | PTM: Phosphorylated. Phosphorylated in vitro by constitutive active PKN3. {ECO:0000269|PubMed:11432776}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Endosome membrane {ECO:0000269|PubMed:32344433}. Note=Association to cell membrane is dependent on PH domain. Colocalized with MICAL1, RAB8A, RAB8B and RAB10 on endosomal tubules (PubMed:32344433). {ECO:0000250, ECO:0000269|PubMed:32344433}. | null | null | null | null | null | FUNCTION: GTPase-activating protein that catalyzes the conversion of active GTP-bound Rho GTPases to their inactive GDP-bound form, thus suppressing various Rho GTPase-mediated cellular processes (PubMed:11432776). Also converts Cdc42 to an inactive GDP-bound state (PubMed:11432776). Essential for PTKB2 regulation of cytoskeletal organization via Rho family GTPases. Inhibits PAK2 proteolytic fragment PAK-2p34 kinase activity and changes its localization from the nucleus to the perinuclear region. Stabilizes PAK-2p34 thereby increasing stimulation of cell death (By similarity). Associates with MICAL1 on the endosomal membrane to promote Rab8-Rab10-dependent tubule extension. After dissociation with MICAL1, recruits WDR44 which connects the endoplasmic reticulum (ER) with the endosomal tubule, thereby participating in the export of a subset of neosynthesized proteins (PubMed:32344433). {ECO:0000250|UniProtKB:Q6Y5D8, ECO:0000269|PubMed:11432776, ECO:0000269|PubMed:32344433}. | Homo sapiens (Human) |
A1A4Y4 | IRGM_HUMAN | MEAMNVEKASADGNLPEVISNIKETLKIVSRTPVNITMAGDSGNGMSTFISALRNTGHEGKASPPTELVKATQRCASYFSSHFSNVVLWDLPGTGSATTTLENYLMEMQFNRYDFIMVASAQFSMNHVMLAKTAEDMGKKFYIVWTKLDMDLSTGALPEVQLLQIRENVLENLQKERVCEY | 3.6.5.- | null | autophagosome assembly [GO:0000045]; autophagosome maturation [GO:0097352]; CAMKK-AMPK signaling cascade [GO:0061762]; cellular response to interferon-beta [GO:0035458]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to virus [GO:0098586]; defense response [GO:0006952]; defense response to bacterium [GO:0042742]; defense response to Gram-negative bacterium [GO:0050829]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of cGAS/STING signaling pathway [GO:0160049]; negative regulation of defense response to virus [GO:0050687]; negative regulation of inflammatory response [GO:0050728]; negative regulation of NLRP3 inflammasome complex assembly [GO:1900226]; negative regulation of type I interferon production [GO:0032480]; negative regulation of type II interferon production [GO:0032689]; nucleotide-binding oligomerization domain containing 2 signaling pathway [GO:0070431]; positive regulation of autophagosome maturation [GO:1901098]; positive regulation of autophagy [GO:0010508]; positive regulation of lysosome organization [GO:1905673]; positive regulation of macrophage activation [GO:0043032]; positive regulation of mitochondrial fission [GO:0090141]; positive regulation of mitophagy [GO:1901526]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; positive regulation of type II interferon-mediated signaling pathway [GO:0060335]; positive regulation of xenophagy [GO:1904417]; protein destabilization [GO:0031648]; protein lipidation involved in autophagosome assembly [GO:0061739]; protein stabilization [GO:0050821]; protein targeting to vacuole involved in autophagy [GO:0071211]; protein-containing complex assembly [GO:0065003]; regulation of protein complex stability [GO:0061635]; regulation of protein-containing complex assembly [GO:0043254] | autophagosome membrane [GO:0000421]; cell projection [GO:0042995]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; phagocytic cup [GO:0001891]; phagocytic vesicle membrane [GO:0030670] | BH3 domain binding [GO:0051434]; CARD domain binding [GO:0050700]; cardiolipin binding [GO:1901612]; G protein activity [GO:0003925]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase binding [GO:0019901]; protein serine/threonine kinase activator activity [GO:0043539]; protein-macromolecule adaptor activity [GO:0030674] | PF05049; | 3.40.50.300; | TRAFAC class dynamin-like GTPase superfamily, IRG family | PTM: Ubiquitinated via 'Lys-63'-linked polyubiquitination in a NOD2-dependent process. 'Lys-63'-linked polyubiquitination is required for interactions with the core autophagy factors. {ECO:0000269|PubMed:25891078}. | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:28389568}. Cell membrane {ECO:0000250|UniProtKB:Q60766}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q60766}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:29420192}. Lysosome membrane {ECO:0000250|UniProtKB:Q60766}. Late endosome membrane {ECO:0000250|UniProtKB:Q60766}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q60766}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q60766}. Note=Behaves like an integral membrane protein. Recruited to the plasma membrane around forming phagocytic cups, it remains associated with maturing phagosomes. Association with phagosomes is dependent on nucleotide-binding but is IFNG-independent. Also detected in late endosomes and lysosomes. {ECO:0000250|UniProtKB:Q60766}.; SUBCELLULAR LOCATION: [Isoform IRGMd]: Mitochondrion {ECO:0000269|PubMed:21102437}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000269|PubMed:29420192, ECO:0000269|PubMed:30612879}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000269|PubMed:29420192, ECO:0000269|PubMed:30612879}; | null | null | null | null | FUNCTION: Immunity-related GTPase that plays important roles in innate immunity and inflammatory response (PubMed:16888103, PubMed:19165925, PubMed:25891078). Acts as a dynamin-like protein that binds to intracellular membranes and promotes remodeling and trafficking of those membranes (By similarity). Required for clearance of acute protozoan and bacterial infections by interacting with autophagy and lysosome regulatory proteins, thereby promoting the fusion of phagosomes with lysosomes for efficient degradation of cargo including microbes (PubMed:16888103, PubMed:25891078, PubMed:29420192, PubMed:32939830). Regulates selective autophagy, including xenophagy and mitophagy, both directly and indirectly (PubMed:16888103, PubMed:25891078, PubMed:29420192, PubMed:32939830). Directly regulates autophagy by acting as a molecular adapter that promotes the coassembly of the core autophagy machinery to mediate antimicrobial defense: IRGM (1) activates AMPK, which in turn phosphorylates ULK1 and BECN1 to induce autophagy, (2) promotes the coassembly of ULK1 and BECN1, enhancing BECN1-interacting partners and (3) influences the composition of the BECN1 complex, by competing with the negative regulators BCL2 and RUBCN, to trigger autophagy (PubMed:25891078). Also activates autophagy by promoting recruitment of STX17 to autophagosomes (PubMed:29420192). In collaboration with ATG8 proteins, regulate lysosomal biogenesis, a fundamental process for any autophagic pathway, by promoting TFEB dephosphorylation (PubMed:32753672). Also modulates autophagy by assisting with autophagosome formation and preventing lysosomal deacidification (By similarity). While activating autophagy, acts as a key negative regulator of the inflammatory and interferon responses both by (1) promoting mitophagy and (2) mediating autophagy-dependent degradation of effectors of the inflammatory response (PubMed:30612879, PubMed:32715615, PubMed:36221902). Promotes degradation of damaged and IFNG/IFN-gamma-stressed mitochondria via mitophagy, preventing cytosolic release of ligands that activate inflammation (PubMed:32715615). Acts as a suppressor of inflammation by promoting recruitment of inflammation effectors, such as CGAS, RIGI/RIG-I and NLRP3, to autophagosome membranes, leading to their SQSTM1/p62-dependent autophagic degradation (PubMed:30612879, PubMed:32715615). Also directly inhibits assembly of the NLRP3 inflammasome by preventing the association between NLRP3 and PYCARD (PubMed:30612879). Acts as a negative regulator of antiviral innate immune response by suppressing the RIPK2-dependent pro-inflammatory response: mediates recruitment of RIPosomes, composed of RIPK2 and NOD1 or NOD2, to autophagosome membranes, promoting their SQSTM1/p62-dependent autophagic degradation (PubMed:34467632, PubMed:36221902). {ECO:0000250|UniProtKB:Q60766, ECO:0000269|PubMed:16888103, ECO:0000269|PubMed:19165925, ECO:0000269|PubMed:25891078, ECO:0000269|PubMed:29420192, ECO:0000269|PubMed:30612879, ECO:0000269|PubMed:32715615, ECO:0000269|PubMed:32753672, ECO:0000269|PubMed:32939830, ECO:0000269|PubMed:34467632, ECO:0000269|PubMed:36221902}.; FUNCTION: [Isoform IRGMd]: Acts as a positive regulator of mitophagy in response to intracellular mycobacteria infection: specifically binds cardiolipin, leading to its translocation to mitochondria, where it promotes affected mitochondrial fission and mitophagy. {ECO:0000269|PubMed:21102437}.; FUNCTION: (Microbial infection) Following infection by hepatitis C virus (HCV), promotes HCV-triggered membrane remodeling, leading to autophagy and Golgi fragmentation, a step required for HCV replication. {ECO:0000269|PubMed:28389568}. | Homo sapiens (Human) |
A1A519 | F170A_HUMAN | MKRRQKRKHLENEESQETAEKGGGMSKSQEDALQPGSTRVAKGWSQGVGEVTSTSEYCSCVSSSRKLIHSGIQRIHRDSPQPQSPLAQVQERGETPPRSQHVSLSSYSSYKTCVSSLCVNKEERGMKIYYMQVQMNKGVAVSWETEETLESLEKQPRMEEVTLSEVVRVGTPPSDVSTRNLLSDSEPSGEEKEHEERTESDSLPGSPTVEDTPRAKTPDWLVTMENGFRCMACCRVFTTMEALQEHVQFGIREGFSCHVFHLTMAQLTGNMESESTQDEQEEENGNEKEEEEKPEAKEEEGQPTEEDLGLRRSWSQCPGCVFHSPKDRNS | null | null | fertilization [GO:0009566]; positive regulation of DNA-templated transcription [GO:0045893]; transcription by RNA polymerase II [GO:0006366] | nucleus [GO:0005634] | DNA binding [GO:0003677]; metal ion binding [GO:0046872] | PF17734; | null | FAM170 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20162441}. | null | null | null | null | null | FUNCTION: Acts as a nuclear transcription factor that positively regulates the expression of heat shock genes. Binds to heat shock promoter elements (HSE). {ECO:0000269|PubMed:20162441}. | Homo sapiens (Human) |
A1A546 | ISX_MOUSE | MAGPTIHRDMEKSSGYCEAPENLGLSFSIEAILKKPTERRSLPRPQSICKEDSRQTTIPGSKLERPPQDQPQEEKKNKRRVRTTFTTEQLQELEKLFHFTHYPDIHVRSQLASRINLPEARVQIWFQNQRAKWRKQEKSGNLSAPQQPGEAGLALPSNMDVSGPVLTPTAMTTLVPPTECCLLSQTQLPSSWFPTQIPLVPWHPWDLQPLPGPLTQHPCVPTFMFPPLHPKWGSICATST | null | null | negative regulation of intestinal absorption [GO:1904479]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of vitamin A metabolic process [GO:1901738] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565] | PF00046; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. | null | null | null | null | null | FUNCTION: Transcription factor that regulates gene expression in intestine. May participate in vitamin A metabolism most likely by regulating BCO1 expression in the intestine. {ECO:0000269|PubMed:16971476, ECO:0000269|PubMed:18093975}. | Mus musculus (Mouse) |
A1A547 | PGRP3_MOUSE | MLVSWDHPKMLPRLLGFLALSLLACGNPTIVSRKEWGASSLTCRVPLSLPVPYLIIEQVTRMQCQDQITCSQVVRVLQSQYVHNKGWCDIAFNFLVGDDGKVYEGVGWYVQGLHTQGYNNVSLGIAFFGSKIGSPSPAALSATEDLIFFAIQNGYLSPKYIQPFLLKEETCLVPQHSEIPKKACPNITPRSAWEARETHCPQMNLPAKFVIIIHTAGKSCNESADCLVRVRDTQSFHIDNQDFCDIAYHFLVGQDGEVYEGVGWNIEGSHTYGYNDIALGIAFMGNFVEKPPNEASLKAAQSLIQCAVAKGYLTSNYLLMGHSDVSNILSPGQALYNIIKTWPHFKH | null | null | antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; biological process involved in interaction with host [GO:0051701]; defense response to Gram-positive bacterium [GO:0050830]; detection of bacterium [GO:0016045]; innate immune response [GO:0045087]; killing of cells of another organism [GO:0031640]; negative regulation of natural killer cell differentiation involved in immune response [GO:0032827]; negative regulation of type II interferon production [GO:0032689]; peptidoglycan catabolic process [GO:0009253] | extracellular region [GO:0005576]; protein-containing complex [GO:0032991] | N-acetylmuramoyl-L-alanine amidase activity [GO:0008745]; peptidoglycan binding [GO:0042834]; peptidoglycan immune receptor activity [GO:0016019]; protein heterodimerization activity [GO:0046982]; zinc ion binding [GO:0008270] | PF01510; | 3.40.80.10; | N-acetylmuramoyl-L-alanine amidase 2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram-negative bacteria, and has bacteriostatic activity towards Gram-negative bacteria. Plays a role in innate immunity (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
A1A5B4 | ANO9_HUMAN | MQGEESLRILVEPEGDSFPLMEISTCETEASEQWDYVLVAQRHTQRDPRQARQQQFLEELRRKGFHIKVIRDQKQVFFGIRADNSVFGLYRTLLLEPEGPAPHAELAAPTTIPVTTSLRIRIVNFVVMNNKTSAGETFEDLMKDGVFEARFPLHKGEGRLKKTWARWRHMFREQPVDEIRNYFGEKVALYFVWLGWYTYMLVPAALTGLLVFLSGFSLFEASQISKEICEAHDILMCPLGDHSRRYQRLSETCTFAKLTHLFDNDGTVVFAIFMALWATVFLEIWKRQRARVVLHWDLYVWDEEQEEMALQLINCPDYKLRPYQHSYLRSTVILVLTLLMICLMIGMAHVLVVYRVLASALFSSSAVPFLEEQVTTAVVVTGALVHYVTIIIMTKINRCVALKLCDFEMPRTFSERESRFTIRFFTLQFFTHFSSLIYIAFILGRINGHPGKSTRLAGLWKLEECHASGCMMDLFVQMAIIMGLKQTLSNCVEYLVPWVTHKCRSLRASESGHLPRDPELRDWRRNYLLNPVNTFSLFDEFMEMMIQYGFTTIFVAAFPLAPLLALFSNLVEIRLDAIKMVWLQRRLVPRKAKDIGTWLQVLETIGVLAVIANGMVIAFTSEFIPRVVYKYRYSPCLKEGNSTVDCLKGYVNHSLSVFHTKDFQDPDGIEGSENVTLCRYRDYRNPPDYNFSEQFWFLLAIRLAFVILFEHVALCIKLIAAWFVPDIPQSVKNKVLEVKYQRLREKMWHGRQRLGGVGAGSRPPMPAHPTPASIFSARSTDV | null | null | calcium activated galactosylceramide scrambling [GO:0061591]; calcium activated phosphatidylcholine scrambling [GO:0061590]; calcium activated phosphatidylserine scrambling [GO:0061589]; chloride transmembrane transport [GO:1902476]; establishment of localization in cell [GO:0051649]; lipid metabolic process [GO:0006629]; monoatomic ion transmembrane transport [GO:0034220] | plasma membrane [GO:0005886] | chloride channel activity [GO:0005254]; chloride channel inhibitor activity [GO:0019869]; intracellular calcium activated chloride channel activity [GO:0005229]; phospholipid scramblase activity [GO:0017128] | PF04547; | null | Anoctamin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}; Multi-pass membrane protein {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}. Note=Shows predominantly an intracellular localization with a weak expression in the cell membrane. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663, ChEBI:CHEBI:57262; Evidence={ECO:0000250|UniProtKB:P86044}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38664; Evidence={ECO:0000250|UniProtKB:P86044}; CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine(out) = a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine(in); Xref=Rhea:RHEA:38899, ChEBI:CHEBI:18390; Evidence={ECO:0000250|UniProtKB:P86044}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38900; Evidence={ECO:0000250|UniProtKB:P86044}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:P86044}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38573; Evidence={ECO:0000250|UniProtKB:P86044}; | null | null | null | null | FUNCTION: Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide (By similarity). Does not exhibit calcium-activated chloride channel (CaCC) activity (PubMed:22178883). Can inhibit the activity of ANO1 (PubMed:20056604, PubMed:22946059). {ECO:0000250|UniProtKB:P86044, ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22178883, ECO:0000269|PubMed:22946059}. | Homo sapiens (Human) |
A1A5C7 | S22AN_HUMAN | MAIDRRREAAGGGPGRQPAPAEENGSLPPGDAAASAPLGGRAGPGGGAEIQPLPPLHPGGGPHPSCCSAAAAPSLLLLDYDGSVLPFLGGLGGGYQKTLVLLTWIPALFIGFSQFSDSFLLDQPNFWCRGAGKGTELAGVTTTGRGGDMGNWTSLPTTPFATAPWEAAGNRSNSSGADGGDTPPLPSPPDKGDNASNCDCRAWDYGIRAGLVQNVVSKWDLVCDNAWKVHIAKFSLLVGLIFGYLITGCIADWVGRRPVLLFSIIFILIFGLTVALSVNVTMFSTLRFFEGFCLAGIILTLYALRIELCPPGKRFMITMVASFVAMAGQFLMPGLAALCRDWQVLQALIICPFLLMLLYWSIFPESLRWLMATQQFESAKRLILHFTQKNRMNPEGDIKGVIPELEKELSRRPKKVCIVKVVGTRNLWKNIVVLCVNSLTGYGIHHCFARSMMGHEVKVPLLENFYADYYTTASIALVSCLAMCVVVRFLGRRGGLLLFMILTALASLLQLGLLNLIGKYSQHPDSGMSDSVKDKFSIAFSIVGMFASHAVGSLSVFFCAEITPTVIRCGGLGLVLASAGFGMLTAPIIELHNQKGYFLHHIIFACCTLICIICILLLPESRDQNLPENISNGEHYTRQPLLPHKKGEQPLLLTNAELKDYSGLHDAAAAGDTLPEGATANGMKAM | null | null | monoatomic ion transport [GO:0006811] | plasma membrane [GO:0005886] | transmembrane transporter activity [GO:0022857] | PF00083; | 1.20.1250.20; | Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | null | Homo sapiens (Human) |
A1A5H8 | YES_DANRE | MGCVKSKEDKGPTQKYRPDPTNPTPGSHMGLYGPDPTQMGQSPALKGPTNNYNSRSSGLTPFGGSSSVITPFGGASSSFSTVAVNNPFPGVVTGGVTFFVALYDYEARTSDDLSFSKGDRFQIINNTEGDWWEARSINTGQKGYIPSNYVAPADSIQAEEWYFGKMGRKDAERLLLLPGNQRGTFLVRESETTKGAYSLSIRDWDEMKGDNVKHYKIRKLDSGGYYITTRAQFDTLQKLVKHYTEHADGLCYRLTTVCPTVKPQTQGLAKDAWEIPRESLRLELKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMSPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYIVTEYMGKGSLLDFLKEGEGKYLKLPQLVDMAAQIADGMAFIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESLHEMMRLCWKKEPDERPTFEYIQSFLEDYFTATEPQYQPGDNL | 2.7.10.2 | null | adherens junction maintenance [GO:0034334]; cell differentiation [GO:0030154]; convergent extension involved in gastrulation [GO:0060027]; innate immune response [GO:0045087]; phosphorylation [GO:0016310]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | centrosome [GO:0005813]; cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234] | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713]; signaling receptor binding [GO:0005102] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: Autophosphorylation at Tyr-429 maintains enzyme activity. {ECO:0000250}.; PTM: Palmitoylation at Cys-3 promotes membrane localization. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15572145}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028}; | null | null | null | null | FUNCTION: Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, differentiation, G2/M progression and cytokinesis (By similarity). Required for convergent extension cell movements during gastrulation, acting with fyna via rhoa. May be required for epiboly to occur, possibly through its effects in calcium signaling. During embryonic development, phosphorylates ptk2.1/fak. {ECO:0000250, ECO:0000269|PubMed:15572145, ECO:0000269|PubMed:15815683}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A1A5K2 | CLA1B_XENLA | MEQGMDYWLGQIQQKDVGKRLQVGPDLIEYLLDRQKSIDLEQDQTLLDRMVDGLATSWVNSSNYKVALLGMDILSALVTRLQDRFRTQIGTVLPSLMDRLGDAKDSVRDQDQNLLIKIMEQASNPQYMWERMFSGFKHKNFRTREGVCLCLIATLNVYGANSLTLSKIVPHICNLLGDPNSQVRDAAINCLVEIYRHVGERVRADLSKKGLPQSRLNVIFTKFDEVQKSGTMILSTTDKNFDDEDSVDGNRPSSASSSASSKAPQTARRGVSLGTGRRPGTSSAAPKTGGTAKEGAGALDEEDFIRAFEDAPTVQIYSSRDLEESLNKIREILSDDKHDWEQRISALKKIRSLLLAGAAEYDNFFQQLRLLDGAFKLSAKDLRSQVVREACITLGHLSSVLGNKFDHGAEAVMPTVFNLVPNSTKIMATSGVVTIRLIIRHTHVPRLIPIITSNCTSKSVAVRRRCYEFLDLLLQEWQTHSLERHVSVLAETIKKGIHDADSEARIVARKCYWGFHGHFSKEAEQLFHALESSYQKALQSHLKNSDSIVSLPQSDRSSSSSQESLNRPLSAKRSPTGSTVSRATSKSTTGSLQRSRSDIDVNAAATSKTKAASGASTAPFSSVAALPPGSYASLGRIRTRRQSSGSTTSTASTPADTRGRSRAKVVSQSQPGSRSSSPGKLLGSSYGGIATGPQRVPQMPSEKRSKIPRSQGCSRETSPSRTVLDRFGISQPGRIPSAMRVLSSSTDLEAAVADALLLGDSRNKMKPVRRRYEPYGMYSDDDANSDASSACSERSYSSKNGGIPHYLRQTEDVAEVLNHCASSNWSERKEGLVGLQNLLKSQRLLSRVELKRLCEIFTRMFADPHSKRVFSMFLETLVDFVIIHKDDLQDWLFILLTQLLKKMGADLLGSVQAKVQKALDVTRDSFPFDQQFNILMRFIVDQTQTPNLKVKVAILKYIESLARQMDPTDFVNSSETRLAVSRIITWTTEPKSSDVRKAAQVVLISLFELNTPEFTMLLGALPKTFQDGATKLLHNHLKNSSNSSMGSPSNTIGRTPSRHSSSRASPLTSPTNCSHGGLSPSMLDYDTENLNSDEIYSSLRGVTEAIEKFSFRSQVDLNEPVRRDGKKESEMGSCDAGMASPASDLRGGTDMVEGGRMALDNKTSLLNTQPPRAFTGPRGREYNPYAYSDSINSYDKTALKEAVFDDDMDQLRDVPIDHSDLVADLLKELSNHNERVEERKGALCELLKITREDNLAVWEEHFKTILLLLLETLGDKDHAIRALALRVLREILRNQPARFKNYAELTIMKTLEAHKDSHKEVVRAAEEAASTLAGSIHPEQCIKVLCPIIQTADYPINLAAIKMQTKVIERISKESLHQILPDIIPGLLQGYDNTESSVRKASVFCLVAVYSVIGEELKPYLAQLTGSKMKLLNLYIKRAQTTNSNSSSSSDVSTHS | null | null | cell division [GO:0051301]; establishment of mitotic spindle localization [GO:0040001]; microtubule anchoring [GO:0034453]; microtubule nucleation [GO:0007020]; microtubule organizing center organization [GO:0031023]; mitotic spindle assembly [GO:0090307]; regulation of microtubule polymerization or depolymerization [GO:0031110]; regulation of supramolecular fiber organization [GO:1902903] | basal cortex [GO:0045180]; centrosome [GO:0005813]; cytoplasmic microtubule [GO:0005881]; Golgi apparatus [GO:0005794]; kinetochore [GO:0000776]; mitotic spindle [GO:0072686]; spindle microtubule [GO:0005876] | kinetochore binding [GO:0043515]; microtubule binding [GO:0008017] | PF12348;PF21041; | 1.25.10.10; | CLASP family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16390996}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:16390996}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16390996}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16390996}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Note=Localizes to microtubule plus ends. Associates with spindle microtubules, spindle poles, and kinetochores during metaphase, and shifts to the central spindle in late anaphase. | null | null | null | null | null | FUNCTION: Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules during anaphase. Plays a crucial role in chromatin-induced microtubule formation. May also act at microtubule minus ends. May be involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). {ECO:0000269|PubMed:16390996}. | Xenopus laevis (African clawed frog) |
A1A5Q0 | LMOD2_RAT | MSTFGYRRGLSKYESIDEDELLASLTAEELKELERELEDIEPDRNLPVGLRQKSLTEKTPTGNFSREALMAYWEKESQKLLEKERLGECGKLAEEDKEESEEELIFTESNSEVSEEVCTEEEEESTEEEEEEEEEDSEEEEVTTEVTKHINGTVSHNGVNPDNSKPKTFKSQIENINLTNGNSGGTQRNTESPAAIHPCGNPTVIEDALEKIKNNDPDTTEVNLNNIENITTQTLSRFAEALKENTVVKTFSLANTHADDAAAIAIAEMLKVNEHITSVNVESNFITGKGILAIMRALQHNTVLTELRFHNQRHIMGSQVEMEIVKLLKENTTLLRLGYHFELPGPRMSMTSILTRNMDKQRQKRMQEQKQQEGHDGGATLRTKVWQRGTPGSSPYASPRQSPWSSPKVSKKVHTGRSRPPSPVAPPPPPPPPPLPPHMLPPPPPPPAPPLPGKKLITRNIAEVIKQQESAQRALQNGQRKKKGKKVKKQPNNILKEIKNSLRSVQEKKMEESSRPSTPQRSAHENLMEAIRGSSIRQLRRVEVPEALR | null | null | actin filament organization [GO:0007015]; actin filament polymerization [GO:0030041]; actin nucleation [GO:0045010]; muscle contraction [GO:0006936]; myofibril assembly [GO:0030239]; pointed-end actin filament capping [GO:0051694]; positive regulation of actin filament polymerization [GO:0030838]; sarcomere organization [GO:0045214] | actin filament [GO:0005884]; cardiac myofibril [GO:0097512]; cytoskeleton [GO:0005856]; M band [GO:0031430]; myofibril [GO:0030016]; sarcomere [GO:0030017]; striated muscle thin filament [GO:0005865] | actin binding [GO:0003779]; actin monomer binding [GO:0003785]; tropomyosin binding [GO:0005523] | PF03250; | 3.80.10.10; | Tropomodulin family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:18403713, ECO:0000269|PubMed:20685966}. Cytoplasm, myofibril {ECO:0000269|PubMed:20685966}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:18403713}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18403713}. Note=Colocalizes with actin filaments in sarcomeres. Detected close to the M line. {ECO:0000269|PubMed:18403713}. | null | null | null | null | null | FUNCTION: Mediates nucleation of actin filaments and thereby promotes actin polymerization (PubMed:18403713). Plays a role in the regulation of actin filament length (By similarity). Required for normal sarcomere organization in the heart, and for normal heart function (PubMed:18403713). {ECO:0000250|UniProtKB:Q6P5Q4, ECO:0000269|PubMed:18403713}. | Rattus norvegicus (Rat) |
A1A5Q5 | KDM4D_RAT | MKTKSTCAQNPNCSIMIFRPTKEEFNDFDKYIAYMESQGAHRAGLAKVIPPKEWRARQSYDNISNILIATPLQQVVSGQAGVFTQYHKKKKAMTVGQYRHLANSKKYQTPPHLDFEDLERKYWKNRLYESPIYGADVSGSLFDGKTQQWNVGHLGTIQDLLEQECGIVIEGVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGQPKTWYAVPPEHGRRLELLAKELFPGSSQGCQAFLRHKVALISPTVLKENGIPFGRITQEAGEFMVTFPYGYHAGFNHGFNCAEAINFATPRWIDYGKVASQCSCGEARVSFSMDAFVRILQPERYEMWKRGQDQAVVDHTEAMGPTSQELTTWRVIQAPRKTWGLKHLRLRQVSRCLLPVATDSNIANNTQMCHTSRQAADSKGDEVQESDPAIAPPYPLGLSSPGHMSTGKRGLGRRPCELGVQESTNGAPVKRRLPEGRDDRSPSPELQSQSVTGDLIVNSDLVNPGPQHPVTASEGGLTSDP | 1.14.11.66 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250}; | cellular response to ionizing radiation [GO:0071479]; chromatin remodeling [GO:0006338]; DNA damage response [GO:0006974]; double-strand break repair via homologous recombination [GO:0000724]; inflammatory response [GO:0006954]; positive regulation of double-strand break repair via nonhomologous end joining [GO:2001034]; regulation of gene expression [GO:0010468]; regulation of protein phosphorylation [GO:0001932] | chromatin [GO:0000785]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; site of double-strand break [GO:0035861] | chromatin DNA binding [GO:0031490]; damaged DNA binding [GO:0003684]; histone demethylase activity [GO:0032452]; histone H3K9 demethylase activity [GO:0032454]; histone H3K9me2/H3K9me3 demethylase activity [GO:0140684]; metal ion binding [GO:0046872] | PF02373;PF02375; | 2.60.120.650; | JHDM3 histone demethylase family | PTM: Ubiquitinated via 'Lys-63'-linked ubiquitin chains. Deubiquitinated by USP14 with the help of TRIM14 leading to stabilization. {ECO:0000250|UniProtKB:Q6B0I6}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537}. | CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961; EC=1.14.11.66; Evidence={ECO:0000250|UniProtKB:Q6B0I6}; | null | null | null | null | FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. {ECO:0000250|UniProtKB:Q6B0I6}. | Rattus norvegicus (Rat) |
A1A5R1 | RFOX2_RAT | MAEGGQAQQQPPQLGPGAAARGMKRESEVELPVPGAGADGPEPGLSKRPRTEEAADEGMQGNQEPTTTPDAMVQPFTTIPFPPPPQNGIPTEYGVPHTQDYAGQTSEHNLTLYGSSQPHGEQSSNSPSNQNGSLTQTEGGAQTDGQQSQTQSSENSESKSTPKRLHVSNIPFRFRDPDLRQMFGQFGKILDVEIIFNERGSKGFGFVTFENSADADRAREKLHGTVVEGRKIEVNNATARVMTNKKMVTPYANGWKLSPVVGAVYGPELYAASSFQADVSLGNEAAVPLSGRGGINTYIPLISLPLVPGFPYPTAATTAAAFRGAHLRGRGRTVYGAVRAVPPTAIPAYPGVVYQDGFYGADLYGGYAAYRYAQPATATAATAAAAAAAAYSDGYGRVYTADPYHALAPAASYGVGAVASLYRGGYSRFAPY | null | null | cellular response to angiotensin [GO:1904385]; cellular response to endothelin [GO:1990859]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to retinoic acid [GO:0071300]; dendrite morphogenesis [GO:0048813]; heart development [GO:0007507]; intracellular estrogen receptor signaling pathway [GO:0030520]; mRNA alternative polyadenylation [GO:0110104]; negative regulation of apoptotic process [GO:0043066]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of membrane hyperpolarization [GO:1902631]; negative regulation of mitochondrial depolarization [GO:0051902]; nervous system development [GO:0007399]; neuromuscular process controlling balance [GO:0050885]; positive regulation of gene expression [GO:0010628]; positive regulation of vasoconstriction [GO:0045907]; radial glia guided migration of Purkinje cell [GO:0021942]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of definitive erythrocyte differentiation [GO:0010724]; regulation of mitochondrial gene expression [GO:0062125]; RNA splicing [GO:0008380] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA-binding transcription factor binding [GO:0140297]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; single-stranded RNA binding [GO:0003727]; transcription corepressor activity [GO:0003714] | PF12414;PF00076; | 3.30.70.330; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: RNA-binding protein that regulates alternative splicing events by binding to 5'-UGCAUGU-3' elements. Prevents binding of U2AF2 to the 3'-splice site. Regulates alternative splicing of tissue-specific exons and of differentially spliced exons during erythropoiesis. Seems to act as a coregulatory factor of ER-alpha (By similarity). Together with RNA binding proteins RBPMS and MBNL1/2, activates vascular smooth muscle cells alternative splicing events (PubMed:37548402). {ECO:0000250, ECO:0000269|PubMed:37548402}. | Rattus norvegicus (Rat) |
A1A696 | OHK3_ORYSJ | MDEMSCGGGGGGARWKRARVAGMGEGKAGGGGGAAFLGLERVGMVVRMLPVPEKVSARARVVRGSLVAHFRGWRVVRETWWWVLLLWILAGSLGSFYLFLFMNAQSLDKRRDSLASMCDERARMLQDQFNVSMNHLQALAILVSTFHHSKTPSAIDQMTFARYAERTAFERPLTSGVAYAVRVTHGEREQFERQQGWAIKKMYSSSNKKQSSPGPGPGDAAVAEIREPAEEYAPVIFAQDAYKHVISFDMLSGNEDRDNILRARKSGKGVLTAPFKLLNNRLGVILTYTVYKYELPAYARPHERIQAAIGYLGGIFDIQALVEKLLKQLASQESIMVNVYDTTNESPISMYGDDTGSGMCHVSVLNFGDPSRKHEMHCRFEKKPPWPWLAITSSFGTLVIALLTGHIFQATVHRIAKVEDDFHKMSELKKRAEDADVAKSQFLATVSHEIRTPMNGVLGMLQMLMDTDLDTTQQDYVRTAQASGKALVSLINEVLDQAKIESGKLELETVPFDLRTVCDDILSLFCGKAQEKGLELAVYVSDQVPQILIGDPGRIRQIITNLVGNSIKFTERGHIYLTVHVVEEVMSCLEVETGIQNTNTLSGYPVANRRCSWESIRLFNRELHSSEKSFAPIASDSISLVISVEDTGVGIPFEAQSRVFTPFMQVGPSIARIHGGTGIGLSISKCLVGLMKGEIGFASKPHVGSTFTFTAVLMRAHCKGNDIKSSEFKGINALVVDHRPVRAKVTKYHLQRLGVKTELTAELNQFISKLNSGSLTAKLVLIDKETWLKESHCTPLLVNKLRNNDKPDSPKLFLLGSSASSPKGGSDTSREHNLNVIMKPLRASMLQVSLRRALGGVDKVHCRNGVVGNSTLGSLLHKKQIIVVDDNIVNLKVAAGALKKYGAEVTCADSGKKAITLLKPPHNFDACFMDIQMPEMDGFEATRRIRVMERDLNERIERGEAPPECASIQRWRTPILAMTADVIQATHEECLKSEMDGYVSKPFEGEQLYSEVARFFQNHDQVE | 2.7.13.3 | null | cellular response to abscisic acid stimulus [GO:0071215]; cellular response to cold [GO:0070417]; cellular response to phosphate starvation [GO:0016036]; cellular response to sucrose stimulus [GO:0071329]; cytokinin-activated signaling pathway [GO:0009736]; defense response to bacterium [GO:0042742]; leaf senescence [GO:0010150]; negative regulation of iron ion transport [GO:0034757]; phloem or xylem histogenesis [GO:0010087]; regulation of chlorophyll catabolic process [GO:0010271]; regulation of flower development [GO:0009909]; regulation of meristem development [GO:0048509]; regulation of seed germination [GO:0010029]; response to salt stress [GO:0009651]; response to water deprivation [GO:0009414]; secondary growth [GO:0080117] | plasma membrane [GO:0005886] | phosphorelay sensor kinase activity [GO:0000155]; protein histidine kinase binding [GO:0043424] | PF03924;PF02518;PF00512;PF00072; | 1.10.287.130;3.40.50.2300;6.10.250.1190;3.30.450.350;3.30.565.10; | null | PTM: Activation probably requires a transfer of a phosphate group between a His in the transmitter domain and an Asp of the receiver domain. {ECO:0000305}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Cytokinin receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade. {ECO:0000250|UniProtKB:A1A698}. | Oryza sativa subsp. japonica (Rice) |
A1A698 | OHK4_ORYSJ | MGVGGGGGGGGGEAAAAVAVEGDEAGKGRRWWRVKVKLSTVAVVAWVLASAALWAGLHWRFRRAALHKAEEALVCMCEERARMLQDQFAVSVNHVHALAILVATFHYDKHPPALDQDTFAVYAARTSFERPLLSGVAYAQRVVHADRESFERQQGWIIKTMKHEPSPAQDEYAPVIYSQETISYIEGLDVMSGEEDRENILRARATGKAVLTRPFRLMSNHLGVVLTFPVYLVDLPNDTAVEDRVAATAGYLGGAFDVESLVENLLRQLAGNQELVVNVYDVTNHSNPLVMYGSEVPLGIPSPSHTYTLDFGDPLRKHQMVCRYRNKLHVSWSAITTPSGVFVICMLVGYIIYAAWSRYDNVKEDCRKMEALKKRAEAADIAKSQFLATVSHEIRTPMNGVLGMLDMLLDTELKSTQRDYAQTAQVCGKALISLINEVLDRAKIEAGKIDLESVPFDLRSILDDVISLFSSKSREKGIELAVYVSERVPEILLGDPGRFRQIITNLVGNSIKFTERGHIFVQVHLADHSNLATEAKIEPVVNGMNGHKDEAIAIPTSGSHNTLSGFEAADSRNNWENFKLLLSYEKNEMPYESDSDKVTLVVSVEDTGIGIPLHAQGRVFTPFMQADSSTSRNYGGTGIGLSISKCLVEIMGGQINFVSRPLVGSTFTFTAVLRRCDKNAISDSKTVALHPLPSSFKGLSALLVDKRPVRATVTKYHLQRLGITSEVVGTIDPTFGVLSGRNGSSLTSIGKKQPCMLLIESDSWGPQMDVSLHARLQEMKQSDRIHVLPKVFLLSAAESDKVKKIHAVDSVIPKPLKASALAACLFQALGITQPSHEKRDDSGSLHGRDGSGSLHGLLLGKNILVVDDNKVNLRVAAGTLKKYGAKVECVESGKDALSLLQVPHKFDLCLMDIQMPEMDGFEATRQIRAMEGKANEQADDSESGSEIAAKTAKWHLPILAMTADVIQATHEECTKCGMDGYVSKPFEEKQLFQAVQKFLGPCVSS | 2.7.13.3 | null | cytokinin-activated signaling pathway [GO:0009736]; protein phosphorylation [GO:0006468] | plasma membrane [GO:0005886] | cytokine binding [GO:0019955]; phosphorelay sensor kinase activity [GO:0000155]; protein histidine kinase activity [GO:0004673] | PF03924;PF02518;PF00512;PF00072; | 1.10.287.130;3.40.50.2300;6.10.250.1190;3.30.450.350;3.30.565.10; | null | PTM: Activation probably requires a transfer of a phosphate group between a His in the transmitter domain and an Asp of the receiver domain. {ECO:0000305}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Cytokinin receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade. {ECO:0000269|PubMed:22642989}. | Oryza sativa subsp. japonica (Rice) |
A1A699 | OHK6_ORYSJ | MGKPEARSGWRNAAAAAWVLVAVACAAYMHWHLRRETMDRAEERLVSMCEERARMLQEQFGVTVNHVHALAILISTFHFEKFPSAIDQDTFAKYTARTSFERPLLNGVAYAQRIFHHEREMFENQQGWIMKTMKRQAAPPQDEYAPVIFSQDTVSYLARIDMMSGEEDRENILRARATGKAVLTNPFRLLGSNHLGVVLTFAVYRPGLAADASVEERVEATAGYLGGAFDVESLVENLLSKLAGNQDIVVNVYDVTNASEPMAMYGPQSPDGKVSLFHVSTLDFGDPFRAHEMRCRYRQKPPLPWSAITNPLGTFVIWMLVGYIICAAWSRYDKVSEDCRKMEELKTQAEAADVAKSQFLATVSHEIRTPMNGVLGMLDMLLGTDLSMTQKDYAQTAQMCGRALITLINDVLDRAKIEAGKLELEAVPFDLRSLMDDVISLFSSKSREKCIELAVFVCDDVPKVVIGDPWRYRQILTNLVGNAVKFTERGHVFVRVCLAENSKVEANQVLNGTMNGKDGKVETTANGAFNTLSGFQAADERNNWDYFKLLLSDKEPHMDELECDRSYQNDCDCVTLMISIEDTGVGIPLHAQDRVFTPFMQADSSTSRNYGGTGIGLSISKCLAELMGGQISFTSRPFVGSTFTFSAVLKRSCKDTSSDSKRSLSEALPTAFKGMKAILVDGRPVRGAVTRYHLNRLGIVVKVVNNLSMGLQTLAGQNGVKESREKLSMLFIESDIWRPETDILLLNRLHELKNNGQVHELPKLVLLVTSEADKDRYGSAFDIVMYKPIRASTIASCLQQLLKVVMPERKDNQNRPSFLRSLLIGKNILIVDDNKVNLRVAAAALKKYGAKVHCVESGKDAVSLLQQPHCFDACFMDVQMPEMDGFEATRQIRQMEVKANEERKALDLMEGSTFVESHLPVLAMTADVIQATYEECIKSGMDGYVSKPFDEEQLYQAVSRLVVGTKESAV | 2.7.13.3 | null | cytokinin-activated signaling pathway [GO:0009736]; protein phosphorylation [GO:0006468] | plasma membrane [GO:0005886] | cytokine binding [GO:0019955]; phosphorelay sensor kinase activity [GO:0000155]; protein histidine kinase activity [GO:0004673] | PF03924;PF02518;PF00512;PF00072; | 1.10.287.130;3.40.50.2300;6.10.250.1190;3.30.450.350;3.30.565.10; | null | PTM: Activation probably requires a transfer of a phosphate group between a His in the transmitter domain and an Asp of the receiver domain. {ECO:0000305}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Cytokinin receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade. {ECO:0000269|PubMed:22642989}. | Oryza sativa subsp. japonica (Rice) |
A1A6H3 | RBSK_ARATH | MMKGISSVSQSINYNPYIEFNRPQLQISTVNPNPAQSRFSRPRSLRVLSLSADPSANRNPKSAVDAHAPPLVVVGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGCGVHLDYVRSVNNEPTGHAVVMLQSDGQNSIIIVGGANMKAWPEIMSDDDLEIVRNAGIVLLQREIPDSINIQVAKAVKKAGVPVILDVGGMDTPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGSALFIQGEKPIQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGAIPSMPDRKSVLKLLKFSI | 2.7.1.15 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03215}; Note=Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate. {ECO:0000255|HAMAP-Rule:MF_03215}; | D-ribose catabolic process [GO:0019303]; nucleoside metabolic process [GO:0009116] | chloroplast [GO:0009507]; chloroplast nucleoid [GO:0042644]; chloroplast stroma [GO:0009570]; cytosol [GO:0005829]; nucleus [GO:0005634]; plastid nucleoid [GO:0042646] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; ribokinase activity [GO:0004747] | PF00294; | 3.40.1190.20; | Carbohydrate kinase PfkB family, Ribokinase subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast nucleoid {ECO:0000269|PubMed:27601466}. | 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:0000255|HAMAP-Rule:MF_03215, ECO:0000269|PubMed:27601466}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=150 uM for D-ribose {ECO:0000269|PubMed:27601466}; KM=45 uM for ATP {ECO:0000269|PubMed:27601466}; Note=kcat is 2 sec(-1). {ECO:0000269|PubMed:27601466}; | PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2. {ECO:0000255|HAMAP-Rule:MF_03215}. | null | null | FUNCTION: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway (By similarity) (PubMed:27601466). Can also use xylose and fructose as carbohydrate substrates with a low efficiency (PubMed:27601466). Can use GTP, and, to a lower extent, CTP and UTP as alternative phosphoryl donors (PubMed:27601466). {ECO:0000255|HAMAP-Rule:MF_03215, ECO:0000269|PubMed:27601466}. | Arabidopsis thaliana (Mouse-ear cress) |
A1A6M1 | PTAC5_ARATH | MASSSLPLSLPFPLRSLTSTTRSLPFQCSPLFFSIPSSIVCFSTQNPDREEVRWLREEQRWIREEQRWIREEQRWIRERESLLQEISDLQLRIQSLESRNSQLGNSIPDTISNIAALLQVLKEKNRISESGLSATPMVLESTREQIVEEVEEEEKRVIIAEEKVRVSEPVKKIKRRILKVGSEGDDVQALQEALLKLGFYSGEEDMEFSSFSSGTASAVKTWQASLGVREDGVMTAELLQRLFMDEDVETDKDEASTMKKEEAGNGAVFTSVTQVPEKKQSIVKDQSDREVDVTQNRVFLLGENRWEDPSRLIGRNKPVDRSESTNTKTRCITCRGEGRLMCLECDGTGEPNIEPQFMEWVGEDTKCPYCEGLGYTVCDVCDGKKNL | 5.3.4.1 | null | chloroplast organization [GO:0009658]; plastid transcription [GO:0042793]; regulation of DNA-templated transcription [GO:0006355]; response to heat [GO:0009408]; response to light stimulus [GO:0009416] | chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast nucleoid [GO:0042644]; chloroplast thylakoid [GO:0009534]; chloroplast thylakoid membrane [GO:0009535]; cytosol [GO:0005829] | metal ion binding [GO:0046872]; protein disulfide isomerase activity [GO:0003756] | PF01471; | 1.10.101.10; | null | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast nucleoid {ECO:0000269|PubMed:23922206}. | CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; Evidence={ECO:0000269|PubMed:23922206}; | null | null | null | null | FUNCTION: Exhibits zinc-dependent disulfide isomerase activity. Required for seedling and chloroplast development under heat stress, probably by maintaining plastid-encoded RNA polymerase (PEP)-dependent transcription. {ECO:0000269|PubMed:23922206}. | Arabidopsis thaliana (Mouse-ear cress) |
A1ACB2 | HCHA_ECOK1 | MTVQKSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESEDVAAALQWAIENDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | 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 O1:K1 / APEC |
A1B198 | HPBD_PARDP | MKIAEIHVYAHDLPVKDGPYTIASSTVWSLQTTLVKIVADSGLAGWGETCPVGPTYAPSHALGARAALAEMAPGLIGANPLQPLVLRRRMDGLLCGHNYAKAAIDIAAYDLMGKHYGVRVADLLGGVAAERVPSYYATGIGQPDEIARIAAEKVAEGFPRLQIKIGGRPVEIDIETVRKVWERIRGTGTRLAVDGNRSLPSRDALRLSRECPEIPFVLEQPCNTLEEIAAIRGRVQHGIYLDESGEDLSTVIRAAGQGLCDGFGMKLTRIGGLQQMAAFRDICEARALPHSCDDAWGGDIIAAACTHIGATVQPRLNEGVWVAQPYIAQPYDEENGIRIAGGHIDLPKGPGLGITPDESLFGPPVASFS | 5.1.1.22 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:24520058}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:24520058}; | amino-acid betaine catabolic process [GO:0006579] | null | metal ion binding [GO:0046872]; racemase activity, acting on amino acids and derivatives [GO:0036361]; racemase and epimerase activity, acting on amino acids and derivatives [GO:0016855] | PF13378;PF02746; | 3.20.20.120;3.30.390.10; | Mandelate racemase/muconate lactonizing enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=trans-4-hydroxy-L-proline betaine = cis-4-hydroxy-D-proline betaine; Xref=Rhea:RHEA:47544, ChEBI:CHEBI:85533, ChEBI:CHEBI:85534; EC=5.1.1.22; Evidence={ECO:0000269|PubMed:24056934, ECO:0000269|PubMed:24520058}; CATALYTIC ACTIVITY: Reaction=L-proline betaine = D-proline betaine; Xref=Rhea:RHEA:51884, ChEBI:CHEBI:35280, ChEBI:CHEBI:134398; EC=5.1.1.22; Evidence={ECO:0000269|PubMed:24056934, ECO:0000269|PubMed:24520058}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=64 mM for trans-4-hydroxy-L-proline betaine {ECO:0000269|PubMed:24056934}; KM=34 mM for L-proline betaine {ECO:0000269|PubMed:24056934}; KM=7.3 mM for D-proline betaine {ECO:0000269|PubMed:24520058}; Note=kcat is 110 sec(-1) with trans-4-hydroxy-L-proline betaine as substrate (PubMed:24056934). kcat is 68 sec(-1) with L-proline betaine as substrate (PubMed:24056934). kcat is 28 sec(-1) with D-proline betaine as substrate (PubMed:24520058). {ECO:0000269|PubMed:24056934, ECO:0000269|PubMed:24520058}; | null | null | null | FUNCTION: Catalyzes the 2-epimerization of trans-4-hydroxy-L-proline betaine (tHyp-B) to cis-4-hydroxy-D-proline betaine (cHyp-B). Is involved in a catabolic pathway that degrades tHyp-B to alpha-ketoglutarate. This pathway would permit the utilization of tHyp-B as a carbon and nitrogen source in the absence of osmotic stress, since tHyp-B functions as an osmolyte and is not catabolized when it is needed as osmoprotectant. Can also catalyze the racemization of L-proline betaine. {ECO:0000269|PubMed:24056934}. | Paracoccus denitrificans (strain Pd 1222) |
A1B2F3 | AZTC_PARDP | MKDWLFRIATCSIMTFSSLAAAQAEPLDVVATFSIIGDFAAKVGGDRIRLNVLVGPDSDTHVYEPRPADAIALAGADVVLTNGLEFEGFLTRLIAASGTDAAVATLTDGVETMEEPGGGHYHYIDGKAVFHAGAHDPHAWQAVPNAKVYVQNIAAAFCAADAEGCAAYQANAARYIGELDALDTEIRAAIAALPQDRRTVVVAHNAFRYFEAAYGVHFLSPQGVSTESEAAAADVAGLIREIRARNASAIFAENISDTRLLEQIAREAGLPLAGTLYSDALSGPDGPASNYIAMMRHNAGAIAAALAAR | null | null | cell adhesion [GO:0007155]; zinc ion transport [GO:0006829] | periplasmic space [GO:0042597] | zinc ion binding [GO:0008270] | PF01297; | 3.40.50.1980; | Bacterial solute-binding protein 9 family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:25787075}. | null | null | null | null | null | FUNCTION: Part of the ATP-binding cassette (ABC) transport system AztABCD involved in zinc import (PubMed:25787075, PubMed:26468286, PubMed:30353723, PubMed:32781785, PubMed:35128285). Binds zinc with high affinity and specificity and delivers it to the membrane permease for translocation into the cytoplasm (PubMed:25787075, PubMed:26468286, PubMed:30353723, PubMed:32781785, PubMed:35128285). {ECO:0000269|PubMed:25787075, ECO:0000269|PubMed:26468286, ECO:0000269|PubMed:30353723, ECO:0000269|PubMed:32781785, ECO:0000269|PubMed:35128285}. | Paracoccus denitrificans (strain Pd 1222) |
A1B2F4 | AZTD_PARDP | MLRHLAGASALALTLAGAGFAQDHDHDHEDVTLYRVFVGDHEKGQVTAFDLAEPDHRWTFPTTGQVKLYSVAGGAVVAAVQSDADTVQFIRSGISFHDHGDHRDIEVGDPAAIDASLTGPRPFHLVEHDGKVVLNYDQGGYAEILDGHALAEGKAEPGRFPQARAHHGFVAPLGGNWLSTVASDEKVEGDASVPRLGLQAFDAEGNPAGNLATCTGIHGEAFSGAYLAAGCKEGVLTVKAGANGSEYKLLPYPADLPQGVTTGTLLGSTGIQVFLGNYGPDGLVVIDPVDEPHYRYIKLPFRRVDFALDPAKPSTGYVLTEDGSLHRIDLLKAEIVASAKVTEPYSMDGHWNDPRPRIAMAGDEIVVTDPNAGLVRRIATEDLSERGTVPVEGKPYNIAVTGGSGVTH | null | null | null | periplasmic space [GO:0042597] | zinc chaperone activity [GO:0140827]; zinc ion binding [GO:0008270] | null | null | null | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:26468286, ECO:0000269|PubMed:31428696}. | null | null | null | null | null | FUNCTION: Acts as a zinc chaperone in the AztABCD zinc transport system (PubMed:26468286, PubMed:30353723, PubMed:31428696, PubMed:32781785). Directly transfers one zinc cation to the solute binding protein AztC; the transfer occurs without the formation of a stable interaction (PubMed:26468286, PubMed:31428696, PubMed:32781785). Binds 3 Zn(2+), two with high affinity and one with low affinity, and transfers only Zn(2+) bound to site 2 to AztC (PubMed:26468286, PubMed:31428696). Likely functions to store zinc in the periplasm and may be important for zinc accumulation in zinc-limited environments (PubMed:32781785). {ECO:0000269|PubMed:26468286, ECO:0000269|PubMed:30353723, ECO:0000269|PubMed:31428696, ECO:0000269|PubMed:32781785}. | Paracoccus denitrificans (strain Pd 1222) |
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