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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
A0A0D1DWZ5 | RRM4_USTMA | MSDSIYAPHNKHKLEAARAADAAADDAATVSALVEPTDSTAQASHAAEQTIDAHQQAGDVEPERCHPHLTRPLLYLSGVDATMTDKELAGLVFDQVLPVRLKIDRTVGEGQTASGTVEFQTLDKAEKAYATVRPPIQLRINQDASIREPHPSAKPRLVKQLPPTSDDAFVYDLFRPFGPLRRAQCLLTNPAGIHTGFKGMAVLEFYSEQDAQRAESEMHCSEVGGKSISVAIDTATRKVSAAAAEFRPSAAAFVPAGSMSPSAPSFDPYPAGSRSVSTGSAASIYATSGAAPTHDTRNGAQKGARVPLQYSSQASTYVDP... | null | null | mRNA transport [GO:0051028] | cytoplasmic stress granule [GO:0010494]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endosome [GO:0005768]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904] | mRNA 3'-UTR binding [GO:0003730]; poly(A) binding [GO:0008143]; poly(U) RNA binding [GO:0008266] | PF00658;PF00076; | 3.30.70.330;1.10.1900.10; | Polyadenylate-binding protein type-1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17105762, ECO:0000269|PubMed:19494833, ECO:0000269|PubMed:25985087}. Endosome {ECO:0000269|PubMed:22357951, ECO:0000269|PubMed:24355572, ECO:0000269|PubMed:25985087}. Note=Assembles into particles that shuttle along microtubules to both poles (PubMed:171... | null | null | null | null | null | FUNCTION: Key RNA-binding protein involved in the formation of polar-growing hyphae which is essential for infection by the plant pathogen (PubMed:15643068, PubMed:17105762, PubMed:19494833). During filamentation, assembles into particles that shuttle bidirectionally along microtubules to both poles (PubMed:17105762, P... | Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) |
A0A0D1E015 | UPA1_USTMA | MTIPDPANIIHNDAGTASPHHIWADVGDSTSSSQHEATRSRSDDANGGASASMHAPQHVKANRAAQPTYDSSDLPSFGLSARLTRDSSSFGSKPSSSASDSRRPKFAPYEAENLWATSSTTSHPSKASQSTLSPNASVFKPSRSLQPNHFEPHAVANVHDFDDPLNSAYSSDTVSPRPDHAPLDHEQPQQPSALDPVAVSKVEEQRGDHSIPHQNGLVSAQAQTASDAVSTSKYTTEAADQEEDQDDFVYPGADSPSSGQAAVQDEQQAVTDSQTTKSLTKQESDPEASSTSLSAPAEAEHIVVGSAAEQSLTSSAPAET... | null | null | mRNA transport [GO:0051028] | cytoskeleton [GO:0005856]; endosome [GO:0005768] | metal ion binding [GO:0046872]; NF-kappaB binding [GO:0051059]; transferase activity [GO:0016740] | PF00023;PF13637;PF01363;PF13639; | 1.25.40.20;3.30.40.10; | UPA1 PAM2 domain-binding protein family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:25985087}. Endosome {ECO:0000269|PubMed:25985087}. Note=Shuttles with endosomes along microtubules (PubMed:25985087). the FYVE domain mediates endosomal localization and endosomal targeting is crucial for its function during polar growth and CTS1 secreti... | null | null | null | null | null | FUNCTION: FYVE zinc finger domain protein that functions in endosomal targeting and transport of mRNAs, as well as associated ribosomes (PubMed:25985087, PubMed:28422978). The endosomal mRNA transport regulates polarity of the infectious hyphae by transporting a broad spectrum of cargo mRNAs from the nucleus to cell po... | Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) |
A0A0D2UG83 | H2AY_CAPO3 | MAKSKKIVAATSGSRSRSSRAGLAFPVGRVHRLLRKGHFADRIGSGSAVYLAAVLEYLTAEILELAGNAARDNRKTRINPRHIQLAVRNDEELSKLFTGVVIPSGGTLPHIWPALIPNEAKDSSTASASFNAPAKSATVKALAAAKSAGKKPAAVSSSSAAASSSSSASSSSSVAPKKPVRGFTILSKKTLHLGQTLYVVNGDLTEVRCDAVVHPTNGTMSFAGQVGGAIRAAAGAGVDAEVNSYMSEHSQLQVTKAAITSGHNLPSKWIVHVHSPNYSNAATATDALTQTIRNALTLADTKSIKTIAFPSIGSGNNHFP... | null | null | chromatin organization [GO:0006325]; negative regulation of protein ADP-ribosylation [GO:0010836]; regulation of NAD metabolic process [GO:1902688] | nucleosome [GO:0000786]; nucleus [GO:0005634] | ADP-D-ribose binding [GO:0072570]; ADP-D-ribose modification-dependent protein binding [GO:0160002]; DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211;PF01661; | 1.10.20.10;3.40.220.10; | Histone H2A family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75367}. Chromosome {ECO:0000250|UniProtKB:O75367}. | null | null | null | null | null | FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regula... | Capsaspora owczarzaki (strain ATCC 30864) |
A0A0D2Y5A7 | ODP2_FUSO4 | MLSAALRRRVLAPTHSALRTGFAAHVVRHYASFPEHQVIKMPALSPTMQAGNIGAWQKKPGDSIAPGDVLVEIETDKAQMDFEFQEEGVIAKILKDAGEKDIPVGSPIAVLVEEGTDISAFEKFSIEDAGGDAAKPAAPKKEEKSESKSESASAPEPTPEPQQYQSQGRLQTALDRLPNISASAKRLAREKGISIDGLKGTGKNGQITEEDVKKAISSPAASSAPSATYEDIPISGMRKTIANRLVESTQTNPHFYVTSSISVSKLLKLRQALNSSADGKYKLSVNDFLIKAIAVASRKVPQVNSSWRDGNIRQFNNVDV... | 2.3.1.12 | COFACTOR: Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000255|PROSITE-ProRule:PRU01066}; Note=Binds 1 lipoyl cofactor covalently. {ECO:0000255|PROSITE-ProRule:PRU01066}; | acetyl-CoA biosynthetic process from pyruvate [GO:0006086]; aerobic respiration [GO:0009060] | mitochondrial pyruvate dehydrogenase complex [GO:0005967]; mitochondrion [GO:0005739] | dihydrolipoyllysine-residue acetyltransferase activity [GO:0004742] | PF00198;PF00364;PF02817; | 2.40.50.100;3.30.559.10;4.10.320.10; | 2-oxoacid dehydrogenase family | PTM: Decrotonylated at 'Lys-148' by SIR5, which inhibits the activity of the pyruvate dehydrogenase complex (PDC). {ECO:0000269|PubMed:34927582}. | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:34927582}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein]; Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100, ChEBI:CHEBI:83111; EC=2.3.1.12; Evidence={ECO:000... | null | null | null | null | FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2) (PubMed:34927582). High pyruvate dehydrogenase complex activity is required for sufficient energy production during germination of conidia (PubMed:34927582). {ECO:0000269|PubMed:34927582}. | Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936) (Fusarium vascular wilt of tomato) |
A0A0D4WTV1 | B1D1_LOXAR | EGAEQDGSERTDGGRPIWNIAHMVNNKQAIDKYLDKGANSVESDVSFDSDGKPEKMLHGIPCDCGRKCLNQMSFTDYLDYMRQLTTPGDPKFRENLILIMLDLKLKSVAANLAYSSGQEVALQMLNTYWKRGESGARAYIVLSIPTIKRVTFVRGFYDKLHSEGFDQYREKVGVDFSGNEDLDETGRILSSQNILDHIWQSDGITNCIFRVMTRLKKAINKRDSNGYMVKVYYWSVDKYTIMRKTLRAGADGMITNFPDRLVSVLNEREFSGKFRLATYDDNPWERYKA | 4.6.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8I914}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8I914}; | killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | lyase activity [GO:0016829]; metal ion binding [GO:0046872]; phosphoric diester hydrolase activity [GO:0008081]; toxin activity [GO:0090729] | null | 3.20.20.190; | Arthropod phospholipase D family, Class II subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25752604}. | CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60652, ChEBI:CHEBI:15354, ChEBI:CHEBI:64583, ChEBI:CHEBI:143892; Evidence={ECO:0000269|PubMed:25752604}; CATALYTIC ACTIVITY: Reaction=N-hexanoyl-sphing-4-enine-1-phosphocholine = cho... | null | null | null | null | FUNCTION: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (PubMed:25752604). This toxin acts on sphingomyelin (SM) and on ceramide phosphoethanolamine (C... | Loxosceles arizonica (Arizona brown spider) |
A0A0D4WV12 | BIB11_SICTE | GDSRRPIWNIAHMVNDLDLVDEYLDDGANSLELDVEFSKSGTALRTYHGVPCDCFRSCTRSEKFSKYLDYIRQLTTPGNSKFRSRLILLVLDLKLNPLSSSAAYNAGADVARNLLDNYWQRGDSKARAYIVLSLETIAGAEFITGFKDTMKKEGFDEKYYDKIGWDFSGNEDLGKIRDVLESHGIREHIWQGDGITNCLPRDDNRLKQAISRRYSPTYVYADKVYTWSIDKESSIENALRLGVDGVMTNYPARVISVLGEREFSGKLRLATYDDNPWEK | 4.6.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25752604, ECO:0000312|PDB:4Q6X}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:25752604, ECO:0000312|PDB:4Q6X}; | killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | lyase activity [GO:0016829]; metal ion binding [GO:0046872]; phosphoric diester hydrolase activity [GO:0008081]; toxin activity [GO:0090729] | PF13653; | 3.20.20.190; | Arthropod phospholipase D family, Class II subfamily, Class IIb sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25752604}. | CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60652, ChEBI:CHEBI:15354, ChEBI:CHEBI:64583, ChEBI:CHEBI:143892; Evidence={ECO:0000269|PubMed:25752604}; CATALYTIC ACTIVITY: Reaction=N-hexanoyl-sphing-4-enine-1-phosphocholine = cho... | null | null | null | null | FUNCTION: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (PubMed:25752604). This toxin acts on lysophosphatidylethanolamine (LPE) and ceramide phosphoet... | Sicarius terrosus (Cave spider) |
A0A0D9S1R0 | APOE_CHLSB | MKVLWAALLVTFLAGCQAAADAPIKVEQPVEPETEPELRPQTEWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSPQVTQELTTLMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRSEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLASQPLQERAQALGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTAPVPS... | null | null | cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process... | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; multivesicular body, internal vesicle ... | amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus) |
A0A0E3D8M9 | JANG_PENJA | MLYFLAETIFGFICQYVPIGFWNGYSPAPTDRYRRLDLKSSQGFRAEPNLAPLPTTKPRRERYYGPNQIIRAPLDYLLSIPGKDIRGKLINAFNEWLQLPDDKLAIVKEVINLLHTASLLIDDIQDGSRLRRGRPVAHEVFGVAQTINAANYAYFLQQERLSEIGDPRAFHIFTNALLDLHRGQGMDLYWREAVVCPTEEEYIRMVIYKTGGLFRLALELMQVQSNSTTDFSELVELLGIIFQIRDDYMNLQSGLYAEKKGSMEDLTEGKFSYPVIHSIHAAPENSMLVDILKQRTEDNVVKVRAVHYMESTGSFQYCRE... | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | alcohol biosynthetic process [GO:0046165]; isoprenoid biosynthetic process [GO:0008299]; ketone biosynthetic process [GO:0042181]; mycotoxin biosynthetic process [GO:0043386] | null | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl dip... | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:26213965}.; PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:26213965}. | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes janthitremanes such as shearinine K or shearinine A (PubMed:26213965). The geranylgeranyl diphosphate (GGPP) synthase janG catalyzes the first step in janthitremane biosynthesis via conversi... | Penicillium janthinellum (Penicillium vitale) |
A0A0E3D8P4 | PENG_PENCR | MLFLAPGYIFPNVATPVTVAIDFAQAVKQGAYNVLDLKASPIPNPELFQPPSRIIRGPLNYLLSLPGKDIRGKLIDALNEWFRVPEDKLNIIKEIVVILHTASLLIDDIQDSSELRRGNPVAHRIFGVAQTINSANYAYFLAQAKLADLNDSRAFDIFTKGLLKLHRGQGMELYWRDNLICPTEEEYVEMVSCKTGGLFYLAVQLMQLNSEVTVNFSNFINLLGIIFQIRDDYMNLQSGTMTKTKGFSEDLTEGKFGYPIIHSIHAAPNDSQLIQILKLKTKDEVIKQYAVRYIESTGSFVYCREKLDMYLEEANETFRG... | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | alcohol biosynthetic process [GO:0046165]; isoprenoid biosynthetic process [GO:0008299]; ketone biosynthetic process [GO:0042181]; mycotoxin biosynthetic process [GO:0043386] | null | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl dip... | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:26213965}. | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems (PubMed:26213965). The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyro... | Penicillium crustosum (Blue mold fungus) |
A0A0E3JXD9 | DAO_UNKP | MTEQMLDYFIVGAGLGGVAFAEVALQHQKSIFVFAGDKPPSSVAAAGVYNAVILKRFTLVSQAQEQINLLKVFYPEIEKRIQKNIIFDLPTYRRLASVEEQNNFIVASDRPLFQLFLSPKIISDKFKAVISPFGFGLMKQTGYVDTKLLLQSYRNYLQQNGCISAETFNYAELIIHPDFVEYKGQKAKQIIFAEGFQMKHNPFFKDLPLEGAKGELLVIRSENLDVNVLLKAGVFVLPIGNDLYKVGATYNWTDKTNKPTQSAKDELISELKELISCDFEVVEHLAGIRPTVKDRKPLVGRHPFHKNIYLLNGLGTRGVM... | 1.4.3.3 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q1AYM8}; | amino acid catabolic process [GO:0009063] | cytoplasm [GO:0005737]; peptidoglycan-based cell wall [GO:0009274] | D-amino-acid oxidase activity [GO:0003884] | PF01266; | 3.30.9.10;3.50.50.60; | DAMOX/DASOX family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A5U3S4}. Secreted, cell wall {ECO:0000250|UniProtKB:A5U3S4}. | CATALYTIC ACTIVITY: Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59871; EC=1.4.3.3; Evidence={ECO:0000269|PubMed:25900453}; PhysiologicalDirection=left-to-ri... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.96 mM for D-methionine (at 37 degrees Celsius and at pH 8.0) {ECO:0000269|PubMed:25900453}; Note=kcat is 10.9 sec(-1) with D-methionine as substrate (at 37 degrees Celsius and at pH 8.0). {ECO:0000269|PubMed:25900453}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:25900453}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:25900453}; | FUNCTION: Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. {ECO:0000269|PubMed:25900453}. | Unknown prokaryotic organism |
A0A0E3KBH3 | OFOB_SACSO | MAGLKVEWNDWCPGCGNFGILSAEQQAIQELGLDPKKVVLVSGIGCSGKIPHFIRLPASGVHTLHGRALTFAIGIKLANPSLEVIVNGGDGDQLGIGVGHFVSAGRRNVDLTVIVHNNGVYGLTKGQASPTLKLGVKTKSLPKPNINSDINPIALAISSGYTFVARGYAYDVKHLKEIIKKAIKHKGLAMIDVLQPCPTYNDIHTKEYYDKRVYKLDEDPSWDPIVKKPEEMDDKMSKAILKSMEWGDRTPIGIFYQNELVSTYEQRIAERSPSYLDNPPAHDVIEFEGKPTTDVEDILKERRVT | 1.2.7.11 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:Q96XT4}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250|UniProtKB:Q96XT4}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250|UniProtKB:Q96XT4}; Note=Binds 1 thiamine pyrophosphate per subun... | null | null | 2-oxobutyrate synthase activity [GO:0018491]; 2-oxoglutarate synthase activity [GO:0047553]; 4 iron, 4 sulfur cluster binding [GO:0051539]; magnesium ion binding [GO:0000287]; pyruvate synthase activity [GO:0019164]; thiamine pyrophosphate binding [GO:0030976] | PF12367;PF02775; | 3.40.50.970; | null | null | null | CATALYTIC ACTIVITY: Reaction=a 2-oxocarboxylate + CoA + 2 oxidized [2Fe-2S]-[ferredoxin] = an acyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:42316, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:35179, ChEBI:CH... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=163 uM for 2-oxoglutarate {ECO:0000269|PubMed:16466637}; KM=275 uM for pyruvate {ECO:0000269|PubMed:16466637}; KM=516 uM for 2-oxobutyrate {ECO:0000269|PubMed:16466637}; Note=kcat is 452 min(-1) for 2-oxoglutarate as substrate. kcat is 144 min(-1) for pyruvate as s... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 7-8. {ECO:0000269|PubMed:16466637}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. {ECO:0000269|PubMed:16466637}; | FUNCTION: Catalyzes the coenzyme A-dependent oxidative decarboxylation of different 2-oxoacids such as 2-oxoglutarate, pyruvate and 2-oxobutyrate to form their CoA derivatives. {ECO:0000269|PubMed:16466637}. | Saccharolobus solfataricus (Sulfolobus solfataricus) |
A0A0E3T3B5 | AADH2_MALDO | MAIQIPSRQLFIDGEWREPVLKKRIPIINPATEQIIGDIPAATAEDVEIAVEAARKALARNKGRDWALAPGAVRAKYLRAIAAKIAERKSEIAKLEAIDCGKPLDEAAWDIDDVSGCFEYYADLAEGLDAQQKTPISLPMEQFKSHVLKEPIGVVGLITPWNYPLLMATWKVAPALAAGCAAILKPSELASVTCLELADVCREVGLPPGVLNILTGLGHEAGAPLASHPHVDKIAFTGSTMTGSKIMTAAAQLVKPVSLELGGKSPIVVFDDVDIDKAAEWTAFGIFWTNGQICSATSRLIIHENIAAKFLDRLVQWCKN... | 1.2.1.-; 1.2.1.19 | null | cellular detoxification of aldehyde [GO:0110095]; glycine betaine biosynthetic process from choline [GO:0019285] | peroxisome [GO:0005777] | 1-pyrroline dehydrogenase activity [GO:0033737]; aminobutyraldehyde dehydrogenase activity [GO:0019145]; metal ion binding [GO:0046872] | PF00171; | null | Aldehyde dehydrogenase family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:26296314}. | CATALYTIC ACTIVITY: Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264, ChEBI:CHEBI:59888; EC=1.2.1.19; Evidence={ECO:0000269|PubMed:26296314}; PhysiologicalDirection=left-to-right... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=160 uM for 4-aminobutanal {ECO:0000269|PubMed:26296314}; KM=8.2 uM for 3-aminopropanal {ECO:0000269|PubMed:26296314}; KM=82.8 uM for NAD(+) with 3-aminopropanal as substrate {ECO:0000269|PubMed:26296314}; Vmax=1.9 umol/min/mg enzyme with 4-aminobutanal as substrate... | PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. {ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.75 with 4-aminobutanal as substrate. {ECO:0000269|PubMed:26296314}; | null | FUNCTION: Dehydrogenase that catalyzes the oxidation of several aminoaldehydes (PubMed:26296314). Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively (P... | Malus domestica (Apple) (Pyrus malus) |
A0A0E3T552 | AADH1_MALDO | MAIQIPSRLLFIDGEWREPVLKKRIPIINPATEEIIGHIPAATAEDVELAVEAARRALSRNKGRDWASAPGAVRAKYLRAIAAKIGERKPEIAKLEAIDCGKPLDEAAWDIDDVSGCFEYYAELAEGLDAQQKAPISLPMEQFKSHVLKEPIGVVGLITPWNYPLLMATWKVAPALAAGCAAILKPSELASVTCLELADVCREVGLPPGVLNILTGLGHEAGAPLVSHPHVDKIAFTGSTMTGSKIMTAAAQLVKPVSLELGGKSPIVVFDDVDIDKAAEWTAFGCFWTNGQICSATSRLILHENIATEFLDRLLKWCKN... | 1.2.1.-; 1.2.1.19 | null | cellular detoxification of aldehyde [GO:0110095]; glycine betaine biosynthetic process from choline [GO:0019285] | cytosol [GO:0005829] | 1-pyrroline dehydrogenase activity [GO:0033737]; aminobutyraldehyde dehydrogenase activity [GO:0019145]; metal ion binding [GO:0046872] | PF00171; | null | Aldehyde dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26296314}. | CATALYTIC ACTIVITY: Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264, ChEBI:CHEBI:59888; EC=1.2.1.19; Evidence={ECO:0000269|PubMed:26296314}; PhysiologicalDirection=left-to-right... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=84.8 uM for 4-aminobutanal {ECO:0000269|PubMed:26296314}; KM=16 uM for 3-aminopropanal {ECO:0000269|PubMed:26296314}; KM=33.8 uM for NAD(+) with 3-aminopropanal as substrate {ECO:0000269|PubMed:26296314}; Vmax=1.2 umol/min/mg enzyme with 4-aminobutanal as substrate... | PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. {ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.75 with 4-aminobutanal as substrate. {ECO:0000269|PubMed:26296314}; | null | FUNCTION: Dehydrogenase that catalyzes the oxidation of several aminoaldehydes (PubMed:26296314). Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively (P... | Malus domestica (Apple) (Pyrus malus) |
A0A0E4AZP0 | FSA1_FUSSF | MDASEPIAVIGSACRFPGGSDSPSKLWELLKEPRDLLSKVPPERYNADAFYHADATHHGTTNVRHSYFLSEDPSSFDNNFFNIQPGEAEAIDPQQRLLMEVVYQGLCSAGQTIEGLRGSPTAVYVGVMCDDWSGIITRDLEVFPRYGATGMARSIMSNRISYFFDWHGPSMTIDTACSSSLVAVHQAIQTLRSGESEVAIAAGANLILTPGMYVAESKLSMLSPSGRSKMWDQDVDGYARGEGIAAVVLKPLSAAIRDNDHIDCIIRATGINQDGRTPGLTMPSATAQADLIRSTYARAGLDINKAEDRPQFFHAHGTGT... | 2.3.1.-; 6.3.2.- | null | amide biosynthetic process [GO:0043604]; fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; methylation [GO:0032259]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; toxin biosynthetic process [GO:0009403] | null | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.30.70.3290;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150; | NRP synthetase family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + 11 H(+) + L-serine + 7 malonyl-CoA + 8 NADPH + 2 S-adenosyl-L-methionine = (5S)-3-[(2E,6R,8E,10E,12E)-2,6-dimethyltetradeca-2,8,10,12-tetraenoyl]-5-(hydroxymethyl)pyrrolidine-2,4-dione + AMP + 7 CO2 + 8 CoA + diphosphate + 6 H2O + 8 NADP(+) + 2 S-adenosyl-L-homocysteine; ... | null | PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:25770422}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of HIV-1 integrase inhibitor equisetin and of fusarisetin A, both trans-fused decalin-containing tetramic acids showing also antimicrobial activity (PubMed:25770422). The PKS module of fsa1 together with the enoylreductase fsa... | Fusarium sp. (strain FN080326) |
A0A0F5HNH9 | IMEF_BACTR | MKEELDAFHQIFTTTKEAIERFMAMLTPVIENAEDDHERLYYHHIYEEEEQRLSRLDVLIPLIEKFQDETDEGLFSPSNNAFNRLLQELNLEKFGLHNFIEHVDLALFSFTDEERQTLLKELRKDAYEGYQYVKEKLAEINARFDHDYADPHAHHDEHRDHLADMPSAGSSHEEVQPVAHKKKGFTVGSLIQ | 1.16.3.1 | null | intracellular iron ion homeostasis [GO:0006879] | encapsulin nanocompartment [GO:0140737] | ferroxidase activity [GO:0004322] | null | null | null | null | SUBCELLULAR LOCATION: Encapsulin nanocompartment {ECO:0000269|PubMed:31194509, ECO:0000269|PubMed:31282860}. | CATALYTIC ACTIVITY: Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; Evidence={ECO:0000269|PubMed:31282860, ECO:0000305|PubMed:31194509}; PhysiologicalDirection=left-to-right; Xref=Rhea:R... | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: The empty encapsulin nanocompartment is stable until 86.6 degrees Celsius, when loaded with cargo protein is stable until 88.9 degrees Celsius and when grown in high-iron conditions is stable until 91.8 degrees Celsius. {ECO:0000269|PubMed:31282860}; | FUNCTION: Cargo protein of a type 1 encapsulin nanocompartment. A ferritin-like iron-binding protein probably involved in iron mineralization in the encapsulin nanocompartment. Has ferroxidase activity even when encapsulated, the rate is probably controlled by the rate of Fe flux across the nanocompartment pores (PubMe... | Bacillus thermotolerans (Quasibacillus thermotolerans) |
A0A0G2JDV3 | GBP6_MOUSE | MTQPQMAPICLVENHNEQLSVNQEAIEILDKISQPVVVVAIVGLYRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLDTEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMITINHQALEQLQYVTELTELIRAKSSPNPAGIKNSTEFVSFFPDFVWTVRDFMLELKLNGEDITSDDYLENALKLIPGDKPRMQASNSCRECIRLFFPNRKCFVFDRPTHDKELLQKLDSITEDQLDPKFQEVTKAFVSYIFTYAKIKTLKEGIKVTGNRLGILVTTYVNAINSGAVPCLDDAVTTLAQRE... | 3.6.5.- | null | adhesion of symbiont to host [GO:0044406]; cellular response to interferon-beta [GO:0035458]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to type II interferon [GO:0071346]; defense response to Gram-positive bacterium [GO:0050830]; defense response to protozoan [GO:0042832]; response to bact... | cytoplasmic vesicle [GO:0031410]; symbiont-containing vacuole membrane [GO:0020005] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF02263;PF02841; | 1.20.1000.10;3.40.50.300; | TRAFAC class dynamin-like GTPase superfamily, GB1/RHD3 GTPase family, GB1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:18025219}. | 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:0000250|UniProtKB:P32455}; | null | null | null | null | FUNCTION: Interferon (IFN)-inducible GTPase that plays important roles in innate immunity against a diverse range of bacterial, viral and protozoan pathogens, such as bacterial pathogens Listeria monocytogenes and Mycobacterium bovis BCG as well as the protozoan pathogen Toxoplasma gondii (PubMed:18025219, PubMed:21551... | Mus musculus (Mouse) |
A0A0G2JTR4 | ABR_RAT | MEPLSHRGLPRLSWIDTLYSNFSYGAEDYDAEGHEEQKGPPEGSETMPYIDESPTMSPQLSARSQGGGESISPTPPEGLAPGVEAGKGLEMRKLVLSGFLASEEIYINQLEALLLPMKPLKATATTSQPVLTIQQIETIFYKIQDIYEIHKEFYDNLCPKVQQWDSQVTMGHLFQKLASQLGVYKAFVDNYKVALETAEKCSQSNNQFQKISEELKVKGPKDSKDSHTSVTMEALLYKPIDRVTRSTLVLHDLLKHTPVDHPDYPLLQDALRISQNFLSSINEDIDPRRTAVTTPKGETRQLVKDGFLVEMSESSRKLRH... | null | null | actin cytoskeleton organization [GO:0030036]; brain development [GO:0007420]; cell migration [GO:0016477]; establishment of localization in cell [GO:0051649]; inner ear morphogenesis [GO:0042472]; intracellular signal transduction [GO:0035556]; macrophage migration [GO:1905517]; modulation of chemical synaptic transmis... | axon [GO:0030424]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; plasma membrane [GO:0005886]; postsynaptic density, intracellular component [GO:0099092]; Schaffer collateral - CA1 synapse [GO:0098685] | GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085] | PF00168;PF19057;PF00620;PF00621; | 2.60.40.150;1.20.900.10;2.30.29.30;1.10.555.10; | null | null | SUBCELLULAR LOCATION: Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q5SSL4}. Cell projection, axon {ECO:0000250|UniProtKB:Q5SSL4}. Synapse {ECO:0000269|PubMed:20962234}. | null | null | null | null | null | FUNCTION: Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-regulati... | Rattus norvegicus (Rat) |
A0A0G2JTY4 | NFAC3_RAT | MTTANCGAHDELDFKLVFGEDGAPTPVSQVSRPADLEPDDCASIYIFNVDPPPSTLNSSLGLPHHGLLQSHSSVLSPSFQLQGFKNYEGTDDISESKYSSLSGPKPFECPSIQITSISPNCHQETDAHEDDLHVNDPEREYLERPSRDHLYLPLEPSYRESSLSPSPASSVSSRSWFSDASSCESLSHIYDDVDSELNEAAARFTLGSPLTSPGGSPGGCPGEESWHQQYGPGHSLSPRQSPCHSPRSSITDENWLSPRPASGPSSRPTSPCGKRRHSSAEVCYAGSLSPHHSPVPSPGHSPRGSVTEDTWLTAPVHTGS... | null | null | blood vessel remodeling [GO:0001974]; branching involved in blood vessel morphogenesis [GO:0001569]; calcineurin-NFAT signaling cascade [GO:0033173]; cardiac muscle hypertrophy in response to stress [GO:0014898]; cellular respiration [GO:0045333]; cellular response to calcium ion [GO:0071277]; cellular response to lith... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polyme... | PF16179;PF00554; | 2.60.40.10;2.60.40.340; | null | PTM: Phosphorylated by NFATC-kinase; dephosphorylated by calcineurin. {ECO:0000250|UniProtKB:Q12968}.; PTM: Ubiquitinated by STUB1/CHIP, leading to proteasomal degradation. {ECO:0000250|UniProtKB:Q12968}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19538478, ECO:0000269|PubMed:30980393}. Nucleus {ECO:0000269|PubMed:19538478, ECO:0000269|PubMed:30980393}. Note=The subcellular localization of NFATC plays a key role in the regulation of gene transcription (By similarity). Rapid nuclear exit of NFATC is thought to b... | null | null | null | null | null | FUNCTION: Acts as a regulator of transcriptional activation. Binds to the TNFSF11/RANKL promoter region and promotes TNFSF11 transcription (By similarity). Binding to the TNFSF11 promoter region is increased by high levels of Ca(2+) which induce NFATC3 expression and may lead to regulation of TNFSF11 expression in oste... | Rattus norvegicus (Rat) |
A0A0G2JTZ2 | SOX6_RAT | MSSKQATSPFACTVDGEETMTQDLTSREKEEGSDQHPASHLPLHPIMHNKPHSEELPTLVSTIQQDADWDSVLSSQQRMESENNKLCSLYSFRNTSTSPHKPDEGSREREIMNSVTFGTPERRKGSLADVVDTLKQKKLEEMTRTEQEDSSCMEKLLSKDWKEKMERLNTSELLGEIKGTPESLAEKERQLSTMITQLISLREQLLAAHDEQKKLAASQIEKQRQQMDLARQQQEQIARQQQQLLQQQHKINLLQQQIQVQGHMPPLMIPIFPHDQRTLAAAAAAQQGFLFPPGITYKPGDNYPVQFIPSTMAAAAASGL... | null | null | astrocyte differentiation [GO:0048708]; brain development [GO:0007420]; cardiac muscle cell differentiation [GO:0055007]; cartilage condensation [GO:0001502]; cartilage development [GO:0051216]; cell fate commitment [GO:0045165]; cell morphogenesis [GO:0000902]; cellular response to transforming growth factor beta stim... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity [GO:0001217]; DNA-binding transcription rep... | PF00505; | 1.10.30.10; | null | PTM: Sumoylation inhibits the transcriptional activity. {ECO:0000250|UniProtKB:P35712}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40645, ECO:0000255|PROSITE-ProRule:PRU00267}. Cytoplasm {ECO:0000250|UniProtKB:P40645}. | null | null | null | null | null | FUNCTION: Transcription factor that plays a key role in several developmental processes, including neurogenesis, chondrocytes differentiation and cartilage formation (By similarity). Specifically binds the 5'-AACAAT-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for cho... | Rattus norvegicus (Rat) |
A0A0G2JUG7 | IQEC1_RAT | MACRRRYLSSLETGSSLSTDRYSVEGEAPSSETGTSLDSPSAYHQGPLVPGSSLSPDHYEHTSVGAYGLYAGPGPQQRTRRPRLQHSTSVLRKQAEEEAIKRSRSLSESYELSSDLQDKQVEMLERKYGGRLVTRHAARTIQTAFRQYQMNKNFERLRSSMSENRMSRRIVLSNMRMQFSFEGPEKVHSSYFEGKQVSVTNDGSQLGALVPSECGDLSDPALKSPAPSSDFADAITELEDAFSRQVKSLAESIDDALNCRSLHSEEVPASDTARARDTEPKPGLHGMDHRKLDEMTASYSDVTLYIDEEELSPPLPLSQA... | null | null | actin cytoskeleton organization [GO:0030036]; dendritic spine development [GO:0060996]; positive regulation of focal adhesion disassembly [GO:0120183]; positive regulation of keratinocyte migration [GO:0051549]; positive regulation of synapse assembly [GO:0051965]; postsynaptic modulation of chemical synaptic transmiss... | glutamatergic synapse [GO:0098978]; nucleus [GO:0005634]; postsynapse [GO:0098794]; postsynaptic density, intracellular component [GO:0099092]; Schaffer collateral - CA1 synapse [GO:0098685]; synaptic vesicle [GO:0008021] | guanyl-nucleotide exchange factor activity [GO:0005085]; lipid binding [GO:0008289]; protein kinase binding [GO:0019901] | PF16453;PF01369; | 1.10.220.20;1.10.1000.11;2.30.29.30; | BRAG family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6DN90}. Nucleus {ECO:0000250|UniProtKB:Q6DN90}. Postsynaptic density {ECO:0000250|UniProtKB:Q8R0S2}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q8R0S2}. Note=At steady state, may be preferentially cytosolic. {ECO:0000250|UniPro... | null | null | null | null | null | FUNCTION: Guanine nucleotide exchange factor for ARF1 and ARF6. Guanine nucleotide exchange factor activity is enhanced by lipid binding. Accelerates GTP binding by ARFs of all three classes. Guanine nucleotide exchange protein for ARF6, mediating internalization of beta-1 integrin. Involved in neuronal development (By... | Rattus norvegicus (Rat) |
A0A0G2JV04 | GGA3_RAT | MAEAEGESLESWLNKATNPSNRQEDWEYIIGFCDQINKELEGPQIAVRLLAHKIQSPQEWEAVQALTVLEACMKNCGRRLHNEVGKFRFLNELIKVVSPKYLGDRVSEKVKAKVIELLFSWTLALPEEAKIKDAYHMLKRQGIVQSDPPIPMDRTLIPSPPPRPKNPVFDDEEKSKLLAKLLRSKNPDDLQEANQLIKSMVKEDEARIQKVTKRLHTLEEVNNNVKLLHEMLLHYSQEFSSEADKELMKELFDRCENKRRTLFKLASETEDNDNSLGDILQASDNLSRVINSYKTIIEGQIINGEVTTSTVPDSEGNSHC... | null | null | endocytic recycling [GO:0032456]; Golgi to plasma membrane protein transport [GO:0043001]; Golgi to plasma membrane transport [GO:0006893]; negative regulation of amyloid-beta formation [GO:1902430]; positive regulation of protein catabolic process [GO:0045732]; protein catabolic process [GO:0030163]; protein destabili... | early endosome [GO:0005769]; early endosome membrane [GO:0031901]; lysosome [GO:0005764]; protein-containing complex [GO:0032991]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; trans-Golgi network [GO:0005802] | phosphatidylinositol binding [GO:0035091]; protein-containing complex binding [GO:0044877]; small GTPase binding [GO:0031267]; ubiquitin binding [GO:0043130] | PF02883;PF03127;PF18308;PF00790; | 1.20.5.170;1.20.58.160;1.25.40.90;2.60.40.1230; | GGA protein family | PTM: Phosphorylated by CK2 and dephosphorylated by PP2A (By similarity). Phosphorylation of GGA3 allows the internal DXXLL motif to bind the VHS domain and to inhibit the recognition of cargo signals. {ECO:0000250}.; PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q9NZ52}.; PTM: Proteolytically cleaved during apoptosis by C... | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9NZ52}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NZ52}. Endosome membrane {ECO:0000250|UniProtKB:Q9NZ52}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NZ52}. Early endosome membrane {ECO:0000269|PubMed:264468... | null | null | null | null | null | FUNCTION: Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (DXXLL) motif. Mediates export of the GPCR ... | Rattus norvegicus (Rat) |
A0A0G2JXN2 | TRI46_RAT | MAEGEDMQTFTSIMDALVRISTSMKNMEKELLCPVCQEMYKQPLVLPCTHNVCQACAREVLGQQGYIGHGGDPSSEPTSPASTPSTRSPRLSRRTLPKPDRLDRLLKSGFGTYPGRKRGALHPQTILFPCPACQGDVELGERGLSGLFRNLTLERVVERYRQSVSVGGAILCQLCKPPPLEATKGCSECRATFCNECFKLFHPWGTQKAQHEPTLPTLSFRPKGLMCPDHKEEVTHYCKTCQRLVCQLCRVRRTHSGHKITPVLSAYQALKDKLTKSLAYILGNQDTVQTQICELEETIRHTEVSGQQAKEEVSQLVRGL... | null | null | anterograde synaptic vesicle transport [GO:0048490]; axonogenesis [GO:0007409]; microtubule bundle formation [GO:0001578]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of axon extension [GO:0030517]; neuron migration [GO:0001764]; positive regulation of anterograde dense core granule transpor... | axon cytoplasm [GO:1904115]; axon initial segment [GO:0043194]; cytoskeleton [GO:0005856]; main axon [GO:0044304]; proximal neuron projection [GO:1990769] | zinc ion binding [GO:0008270] | PF18568;PF00643;PF13445; | 1.20.5.170;2.60.120.920;4.10.830.40;3.30.160.60;2.60.40.10;3.30.40.10; | TRIM/RBCC family | null | SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:26671463}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26671463}. Note=Microtubule-associated. Localizes to the proximal part of the axon. {ECO:0000269|PubMed:26671463}. | null | null | null | null | null | FUNCTION: Microtubule-associated protein that is involved in the formation of parallel microtubule bundles linked by cross-bridges in the proximal axon. Required for the uniform orientation and maintenance of the parallel microtubule fascicles, which are important for efficient cargo delivery and trafficking in axons. ... | Rattus norvegicus (Rat) |
A0A0G2JXT6 | MTMR6_RAT | MEHIRTTKVEQVKLLDRFSTNNKSLTGTLYLTATHLLFIDAHQKETWILHHHIASVEKLALTTSGCPLVIQCKNFRIVHFIVPRERDCHDIYNSLLQLSKQAKYEDLYAFSYNPKQNDTERLNGWQLIDLAAEYERMGVPNANWQLSDANREYKVCETYPRELYVPRTASRPVIVGSSNFRSKGRLPVLSYCQQGTEAAICRCSQPLSGFSARCLEDEHLLQAISKANPGNRYMYVVDTRPKLRMQSWWDTQKDIGRIIVRISSKIWNDEKIRESDEKKRLNAMANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQ... | 3.1.3.64; 3.1.3.95 | null | endocytosis [GO:0006897]; phosphatidylinositol dephosphorylation [GO:0046856] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; nuclear envelope [GO:0005635]; perinuclear region of cytoplasm [GO:0048471]; ruffle membrane [GO:0032587] | phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity [GO:0052629]; phosphatidylinositol-3,5-bisphosphate phosphatase activity [GO:0106018]; phosphatidylinositol-3-phosphate phosphatase activity [GO:0004438] | PF06602;PF21098; | 2.30.29.30; | Protein-tyrosine phosphatase family, Non-receptor class myotubularin subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23188820}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y217}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q8VE11}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:00002... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:39019, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57795, ChEBI:CHEBI:57923; EC=3.1.3.95; Evidence={ECO:0000250|UniP... | null | null | null | null | FUNCTION: Phosphatase that acts on lipids with a phosphoinositol headgroup. Dephosphorylates phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 3,5-bisphosphate. Binds with high affinity to phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) but also to phosphatidylinositol 3-phosphate (PtdIns(3)P... | Rattus norvegicus (Rat) |
A0A0G2JZ79 | SIR1_RAT | MIGTDPRTILKDLLPETIPPPELDDMTLWQIVINILSEPPKRKKRKDINTIEDAVKLLQECKKIIVLTGAGVSVSCGIPDFRSRDGIYARLAVDFPDLPDPQAMFDIEYFRKDPRPFFKFAKEIYPGQFQPSLCHKFIALSDKEGKLLRNYTQNIDTLEQVAGIQRIIQCHGSFATASCLICKYKVDCEAVRGDIFNQVVPRCPRCPADEPLAIMKPEIVFFGENLPEQFHRAMKYDKDEVDLLIVIGSSLKVRPVALIPSSIPHEVPQILINREPLPHLHFDVELLGDCDVIINELCHRLGGEYAKLCCNPVKLSEITE... | 2.3.1.-; 2.3.1.286 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8IXJ6}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q8IXJ6}; | angiogenesis [GO:0001525]; behavioral response to starvation [GO:0042595]; cardiac muscle cell apoptotic process [GO:0010659]; cellular response to amyloid-beta [GO:1904646]; cellular response to antibiotic [GO:0071236]; cellular response to curcumin [GO:1904644]; cellular response to glucose starvation [GO:0042149]; c... | axon [GO:0030424]; chromatin [GO:0000785]; chromatin silencing complex [GO:0005677]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; eNoSc complex [GO:0061773]; ESC/E(Z) complex [GO:0035098]; euchromatin [GO:0000791]; growth cone [GO:0030426]; heterochromatin [GO:0000792]; mitochondrion [GO:0005739]; nuclear envelope [GO... | bHLH transcription factor binding [GO:0043425]; deacetylase activity [GO:0019213]; DNA-binding transcription factor binding [GO:0140297]; enzyme binding [GO:0019899]; histone binding [GO:0042393]; histone deacetylase activity [GO:0004407]; histone H3K deacetylase activity [GO:0141050]; histone H4K12 deacetylase activit... | PF02146; | 3.30.1600.10;3.40.50.1220; | Sirtuin family, Class I subfamily | PTM: Methylated on multiple lysine residues; methylation is enhanced after DNA damage and is dispensable for deacetylase activity toward p53/TP53. {ECO:0000250|UniProtKB:Q96EB6}.; PTM: Phosphorylated. Phosphorylated by STK4/MST1, resulting in inhibition of SIRT1-mediated p53/TP53 deacetylation. Phosphorylation by MAPK8... | SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000250|UniProtKB:Q96EB6}. Cytoplasm {ECO:0000250|UniProtKB:Q96EB6}. Nucleus {ECO:0000250|UniProtKB:Q96EB6}. Note=Recruited to the nuclear bodies via its interaction with PML. Colocalized with APEX1 in the nucleus. May be found in nucleolus, nuclear euchromatin, heterochroma... | 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=... | null | null | null | null | FUNCTION: NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metabolism, apoptosis and autophagy. Can modulate chromatin function through dea... | Rattus norvegicus (Rat) |
A0A0G2K047 | ACSS3_RAT | MKPSWLQCRKVTGAGTLGAPLPGSPSVRGAGVARRALVAGFGGRGCRALTTSSGGGEYKTHFAASVADPERFWGKAAEQISWYKPWTKTLENRYPPSTSWFVEGMLNICYNAIDRHIENGQGDKIAIIYDSPVTDTKATISYKEVLEQVSKLAGVLVKQGVKKGDTVVIYMPMIPQAIYAMLACARIGAIHSLIFGGFASKELSTRIDHVKPKVVVTASFGIEPGRKVEYMPLLEEALRIGQHKPDRLLIYNRPNMEKVPLMSGRDLDWEEEMAKAQSHDCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTM... | 6.2.1.1; 6.2.1.17 | null | lipid metabolic process [GO:0006629] | mitochondrial matrix [GO:0005759] | acetate-CoA ligase activity [GO:0003987]; ATP binding [GO:0005524]; butyrate-CoA ligase activity [GO:0047760]; propionate-CoA ligase activity [GO:0050218] | PF16177;PF00501;PF13193; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:28003429}. | CATALYTIC ACTIVITY: Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:456215; EC=6.2.1.1; Evidence={ECO:0000269|PubMed:28003429}; PhysiologicalDirection=left-to-right; Xref=Rhea:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.4 mM for acetate {ECO:0000269|PubMed:28003429}; KM=3.7 mM for butyrate {ECO:0000269|PubMed:28003429}; KM=0.19 mM for propionate {ECO:0000269|PubMed:28003429}; | null | null | null | FUNCTION: Catalyzes the synthesis of acetyl-CoA from short-chain fatty acids (PubMed:28003429). Propionate is the preferred substrate but can also utilize acetate and butyrate with a much lower affinity (PubMed:28003429). {ECO:0000269|PubMed:28003429}. | Rattus norvegicus (Rat) |
A0A0G2K1Q8 | ABCA3_RAT | MVVLRQLRLLLWKNYTLKKRKVLVTVLELFLPLLFSGILIWLRLKIQSENVPNATVYPDQHIQELPLFFSFPPPGGSWELAYVPSHSDAARTITEAVRREFMIKMRVHGFSSEKDFEDYVRYDNHSSNVLAAVVFEHTFNHSKDPLPLAVRYHLRFSYTRRNYMWTQTGNLFLKETEGWHTASLFPLFPSPGPREPSSPDGGEPGYIREGFLAVQHAVDKAIMHYHANASAHQLFQKLTVITKRFPFPPYISDPFLIAIQYQLPLLLMLSFTYTSLTIIRAVVQEKEKKLKEYMRMMGLSSWLHWSAWFLMFLLFSLIVV... | 7.6.2.1; 7.6.2.2 | null | lipid transport [GO:0006869]; lung development [GO:0030324]; organelle assembly [GO:0070925]; phosphatidylcholine metabolic process [GO:0046470]; phosphatidylglycerol metabolic process [GO:0046471]; phospholipid homeostasis [GO:0055091]; phospholipid transport [GO:0015914]; positive regulation of cholesterol efflux [GO... | alveolar lamellar body [GO:0097208]; alveolar lamellar body membrane [GO:0097233]; cytoplasmic vesicle membrane [GO:0030659]; intracellular membrane-bounded organelle [GO:0043231]; lamellar body [GO:0042599]; lamellar body membrane [GO:0097232]; late endosome [GO:0005770]; lysosomal membrane [GO:0005765]; multivesicula... | ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; lipid transporter activity [GO:0005319]; phosphatidylcholine flippase activity [GO:0140345]; phosphatidylcholine transfer activity [GO:01... | PF12698;PF00005; | 3.40.50.300; | null | PTM: N-glycosylated. Localization at intracellular vesicles is accompanied by processing of oligosaccharide from high mannose type to complex type. N-linked glycosylation at Asn-124 and Asn-140 is required for stability and efficient anterograde trafficking and prevents from proteasomal degradation. {ECO:0000250|UniPro... | SUBCELLULAR LOCATION: Endosome, multivesicular body membrane {ECO:0000250|UniProtKB:Q99758}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q99758}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q99758}. Late endosome membrane {ECO:0000250|UniProtKB:Q99758}. Lysosome membrane {ECO:0000250|UniProtKB:Q99758}. N... | CATALYTIC ACTIVITY: Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000250|UniProtKB:Q99758}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ADP + H(+) + phosphate; Xref=Rhea:... | null | null | null | null | FUNCTION: Catalyzes the ATP-dependent transport of phospholipids such as phosphatidylcholine and phosphoglycerol from the cytoplasm into the lumen side of lamellar bodies, in turn participates in the lamellar bodies biogenesis and homeostasis of pulmonary surfactant. Transports preferentially phosphatidylcholine contai... | Rattus norvegicus (Rat) |
A0A0G2K2P5 | ZO1_RAT | MSARAAAAKSTAMEETAIWEQHTVTLHRAPGFGFGIAISGGRDNPHFQSGETSIVISDVLKGGPAEGQLQENDRVAMVNGVSMDNVEHAFAVQQLRKSGKNAKITIRRKKKVQIPVSHPDPDPVSDNEDDSYDEDVHDPRSGRGALANRRGEKSWARDRSASRDRSLSPRSDRRSVASSQPAKPTKVTLVKSRKNEEYGLRLASHIFVKEISQDSLAARDGNIQEGDVVLKINGTVTENMSLTDAKTLIERSKGKLKMVVQRDERATLLNVPDLSDSIHSANASERDDISEIQSLASDHSVRSHDRPPRRSQSRSPDQRS... | null | null | actin cytoskeleton organization [GO:0030036]; actomyosin structure organization [GO:0031032]; adherens junction maintenance [GO:0034334]; blastocyst formation [GO:0001825]; cell-cell adhesion [GO:0098609]; cell-cell junction organization [GO:0045216]; cellular response to glucose stimulus [GO:0071333]; establishment of... | adherens junction [GO:0005912]; apical junction complex [GO:0043296]; apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; apicolateral plasma membrane [GO:0016327]; basolateral plasma membrane [GO:0016323]; bicellular tight junction [GO:0005923]; cell junction [GO:0030054]; cell-cell junction [GO:000... | ATP binding [GO:0005524]; beta-catenin binding [GO:0008013]; cell adhesion molecule binding [GO:0050839]; connexin binding [GO:0071253]; kinase activity [GO:0016301]; protein domain specific binding [GO:0019904]; transmembrane transporter binding [GO:0044325] | PF00625;PF00595;PF07653;PF00791; | 2.30.42.10;2.60.220.30;3.40.50.300;2.30.30.40; | MAGUK family | PTM: Phosphorylated at tyrosine redidues in response to epidermal growth factor (EGF) (By similarity). This response is dependent on an intact actin microfilament system (By similarity). Dephosphorylated by Ptprj (By similarity). {ECO:0000250|UniProtKB:Q07157}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q07157}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q07157}; Cytoplasmic side {ECO:0000250|UniProtKB:Q07157}. Cell junction, tight junction {ECO:0000269|PubMed:3528172, ECO:0000269|PubMed:9707407}. Cell junction {ECO:0000250|UniProtKB:P12830}. Cell junc... | null | null | null | null | null | FUNCTION: TjpP1, Tjp2, and Tjp3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:9707407). The tight junction acts to limit movement of substances through the paracellular space a... | Rattus norvegicus (Rat) |
A0A0G2K309 | ORNT1_RAT | MKSNPAIQAAIDLTAGAAGGTACVLTGQPFDTMKVKMQTFPDLYRGLTDCCLRTYSQVGFRGFYKGTSPALIANIAENSVLFMCYGFCQQVVRKVVGLDRQAKLSDLQNAAAGSFASAFAALVLCPTELVKCRLQTMYEMETSGKIAASQNTVWSVVKEIFRKDGPLGFYHGLSSTLLREVPGYFFFFGGYELSRSFFASGRSKDELGPIPLMLSGGFGGICLWLAVYPVDCIKSRIQVLSMTGKQTGLIRTFLSIVKNEGITALYSGLKPTMIRAFPANGALFLAYEYSRKLMMSQLEAC | null | null | L-arginine transmembrane transport [GO:1903826]; L-lysine transmembrane transport [GO:1903401]; mitochondrial L-ornithine transmembrane transport [GO:1990575] | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | antiporter activity [GO:0015297]; L-arginine transmembrane transporter activity [GO:0061459]; L-lysine transmembrane transporter activity [GO:0015189]; L-ornithine transmembrane transporter activity [GO:0000064] | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q12375}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:15057822}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) + L-citrulline(in) + L-ornithine(out) = H(+)(out) + L-citrulline(out) + L-ornithine(in); Xref=Rhea:RHEA:70787, ChEBI:CHEBI:15378, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743; Evidence={ECO:0000269|PubMed:10417335, ECO:0000269|PubMed:9359400}; CATALYTIC ACTIVITY: Reaction=L-arginine(out) +... | null | null | null | null | FUNCTION: Mitochondrial ornithine-citrulline antiporter. Catalyzes the exchange between cytosolic ornithine and mitochondrial citrulline plus an H(+), the proton compensates the positive charge of ornithine thus leading to an electroneutral transport. Plays a crucial role in the urea cycle, by connecting the cytosolic ... | Rattus norvegicus (Rat) |
A0A0G2K344 | PK3CA_RAT | MPPRPSSGELWGIHLMPPRILVECLLPNGMIVTLECLREATLVTIKHELFKEARKYPLHQLLQDESSYIFVSVTQEAEREEFFDETRRLCDLRLFQPFLKVIEPVGNREEKILNREIGFVIGMPVCEFDMVKDPEVQDFRRNILNVCKEAVDLRDLNSPHSRAMYVYPPNVESSPELPKHIYNKLDKGQIIVVIWVIVSPNNDKQKYTLKINHDCVPEQVIAEAIRKKTRSMLLSSEQLKLCVLEYQGKYILKVCGCDEYFLEKYPLSQYKYIRSCIMLGRMPNLMLMAKESLYSQLPIDSFTMPSYSRRISTATPYMNG... | 2.7.1.137; 2.7.1.153; 2.7.11.1 | null | actin cytoskeleton organization [GO:0030036]; adipose tissue development [GO:0060612]; angiogenesis [GO:0001525]; autosome genomic imprinting [GO:0141068]; cardiac muscle cell contraction [GO:0086003]; cell migration [GO:0016477]; cellular response to glucose stimulus [GO:0071333]; cellular response to hydrostatic pres... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; intercalated disc [GO:0014704]; lamellipodium [GO:0030027]; phosphatidylinositol 3-kinase complex [GO:0005942]; phosphatidylinositol 3-kinase complex, class IA [GO:0005943]; phosphatidylinositol 3-kinase complex, class IB [GO:0005944]; plasma membrane [GO:0005886] | 1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity [GO:0046934]; 1-phosphatidylinositol-4-phosphate 3-kinase activity [GO:0035005]; ATP binding [GO:0005524]; insulin receptor substrate binding [GO:0043560]; kinase activity [GO:0016301]; protein kinase activa... | PF00454;PF00792;PF02192;PF00794;PF00613; | 2.60.40.150;1.10.1070.11;1.25.40.70; | PI3/PI4-kinase family | null | null | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + ADP + H(+); Xref=Rhea:RHEA:21292, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57836, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.1... | null | PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis. {ECO:0000250|UniProtKB:P42336}. | null | null | FUNCTION: Phosphoinositide-3-kinase (PI3K) phosphorylates phosphatidylinositol (PI) and its phosphorylated derivatives at position 3 of the inositol ring to produce 3-phosphoinositides. Uses ATP and PtdIns(4,5)P2 (phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 p... | Rattus norvegicus (Rat) |
A0A0G2KQY6 | S39AE_DANRE | MTLRRASGCRQLTLTIGLALTLGLLQWPIGDVRGQDGASPAQVLQELLTRYGDNASISVPQLRSLLVRLNGGQSEDHDSKTQPTRTNASKCLAADTLAVYGMSEQSRIDERGLQQICPTMIQQLDSQACKTQPNQESESSPRPTEAEVWGYGLLCVTVISLCSLVGASVVPFMRKTFYKRLLLYFIALAIGTLYSNALFQLIPEAFGFDPMEDYYVPKSAVVFGGFYLFFFTEKILKMILKPKDTGGHGHGHSHFPAERYANSNGDLEDGVMEKLQNGEAGGAALPRAEADGRGVGEDDKMLSTGQTVQDTQSSGGGGTG... | null | null | cellular response to glucose stimulus [GO:0071333]; cellular response to insulin stimulus [GO:0032869]; import across plasma membrane [GO:0098739]; inorganic cation transmembrane transport [GO:0098662]; intracellular zinc ion homeostasis [GO:0006882]; iron import into cell [GO:0033212]; iron ion transmembrane transport... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; early endosome membrane [GO:0031901]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886] | cadmium ion transmembrane transporter activity [GO:0015086]; iron ion transmembrane transporter activity [GO:0005381]; manganese ion transmembrane transporter activity [GO:0005384]; monoatomic anion:monoatomic cation symporter activity [GO:0015296]; monoatomic cation:bicarbonate symporter activity [GO:0140410]; zinc io... | PF02535; | null | ZIP transporter (TC 2.A.5) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27231142}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Early endosom... | CATALYTIC ACTIVITY: Reaction=2 hydrogencarbonate(out) + Zn(2+)(out) = 2 hydrogencarbonate(in) + Zn(2+)(in); Xref=Rhea:RHEA:62252, ChEBI:CHEBI:17544, ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q75N73}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62253; Evidence={ECO:0000250|UniProtKB:Q75N73}; CATALYTIC ... | null | null | null | null | FUNCTION: Broad-scope metal ion transporter with a preference for zinc uptake. Also mediates cellular uptake of nontransferrin-bound iron. {ECO:0000269|PubMed:27231142}.; FUNCTION: Electroneutral transporter of the plasma membrane mediating the cellular uptake of the divalent metal cations zinc, manganese and iron that... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A0G2KTI4 | S12A2_DANRE | MSASPPISAGDYLSAPEPDALKPAGPTPSQSRFQVDLVTESAGDGETTVGFDSSPPEYVAEPPPDGLRDSVSGGEEAKGRFRVVNFAASSPDAAPAETAQNGDTVMSEGSLHSSTGGQQHHHYDTHTNTYYLRTFGHNTIDAVPKIDFYRQTAAPLGEKLIRPTLSELHDELDKEPFEDGFANGEELTPAEESAAKDVSESKGVVKFGWIKGVLVRCMLNIWGVMLFIRMTWIVGQAGIAYSCIIVIMATVVTTITGCSTSAIATNGFVRGGGAYYLISRSLGPEFGGSIGLIFAFANAVAVAMYVVGFAETVVELLMDS... | null | null | cell volume homeostasis [GO:0006884]; chloride ion homeostasis [GO:0055064]; chloride transmembrane transport [GO:1902476]; ear development [GO:0043583]; inner ear morphogenesis [GO:0042472]; potassium ion homeostasis [GO:0055075]; potassium ion import across plasma membrane [GO:1990573]; sodium ion homeostasis [GO:005... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323] | ammonium transmembrane transporter activity [GO:0008519]; chloride:monoatomic cation symporter activity [GO:0015377]; identical protein binding [GO:0042802]; salt transmembrane transporter activity [GO:1901702]; sodium:potassium:chloride symporter activity [GO:0008511] | PF00324;PF08403;PF03522; | 1.20.1740.10; | SLC12A transporter family | PTM: Phosphorylated at Thr-125, Thr-129 and Thr-134 by OXSR1/OSR1 and STK39/SPAK downstream of WNK kinases (WNK1, WNK2, WNK3 or WNK4), promoting its activity. {ECO:0000250|UniProtKB:P55013}. | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:19633174, ECO:0000305|PubMed:31367042}; Multi-pass membrane protein {ECO:0000305|PubMed:31367042}. | CATALYTIC ACTIVITY: Reaction=2 chloride(out) + K(+)(out) + Na(+)(out) = 2 chloride(in) + K(+)(in) + Na(+)(in); Xref=Rhea:RHEA:72395, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P55011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72396; Evidence={ECO:0000250|UniProt... | null | null | null | null | FUNCTION: Cation-chloride cotransporter which mediates the electroneutral transport of chloride, potassium and/or sodium ions across the membrane (PubMed:31367042). Plays a vital role in the regulation of ionic balance and cell volume (PubMed:31367042). Important for maintenance of endolymph volume in the otic vesicle,... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A0G2L7I0 | SPRTN_DANRE | MMEDEDFLLALRLQEQFDQETPAAGWPDEDCPSSKRRRVDPSGGLDVIPFTQPRAERPLSIVDESWETLDPNPDVRAMFLQFNDKFFWGKLSGVEVKWSPRMTLCAGVCSYEGRGGLCSIRLSEPLLKLRPRKDLVQTLLHEMIHALLFVTQNNRDRDGHGPEFCKHMNRINQASGTNITIYHSFHDEVDVYRQHWWRCNGPCQNRRPFFGYVKRAMNRPPSARDPWWADHQRSCGGTYTKIKEPENYGKTGKSDKQRDKMPATEMPKKSKPPSSTSSSGSQDIRNIIPFSGRGFVLGGNAQIPTNKQIQSPPKAPPEPL... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9H040}; | DNA damage response [GO:0006974]; protein autoprocessing [GO:0016540]; protein-DNA covalent cross-linking repair [GO:0106300]; proteolysis [GO:0006508] | chromatin [GO:0000785]; nucleus [GO:0005634] | double-stranded DNA binding [GO:0003690]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; polyubiquitin modification-dependent protein binding [GO:0031593]; single-stranded DNA binding [GO:0003697] | PF10263; | 3.30.160.60; | Spartan family | PTM: Autocatalytically cleaved in response to double-stranded DNA-binding: autocatalytic cleavage takes place in trans and leads to inactivation. {ECO:0000250|UniProtKB:Q9H040}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H040}. Chromosome {ECO:0000250|UniProtKB:A0A1L8G2K9}. Note=Localizes to sites of UV damage via the PIP-box. Recruited to stalled replication forks at sites of replication stress. {ECO:0000250|UniProtKB:Q9H040}. | null | null | null | null | null | FUNCTION: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity. DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication an... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A0G2Q9D6 | GYRB_MYCBP | MGKNEARRSALAPDHGTVVCDPLRRLNRMHATPEESIRIVAAQKKKAQDEYGAASITILEGLEAVRKRPGMYIGSTGERGLHHLIWEVVDNAVDEAMAGYATTVNVVLLEDGGVEVADDGRGIPVATHASGIPTVDVVMTQLHAGGKFDSDAYAISGGLHGVGVSVVNALSTRLEVEIKRDGYEWSQVYEKSEPLGLKQGAPTKKTGSTVRFWADPAVFETTEYDFETVARRLQEMAFLNKGLTINLTDERVTQDEVVDEVVSDVAEAPKSASERAAESTAPHKVKSRTFHYPGGLVDFVKHINRTKNAIHSSIVDFSGK... | 5.6.2.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01898, ECO:0000269|PubMed:7503546}; 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 ... | 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 DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. Relaxes negatively supercoiled DNA in an ATP-independent ma... | Mycobacterium bovis (strain BCG / Pasteur 1173P2) |
A0A0G2Q9F8 | GYRA_MYCBP | MTDTTLPPDDSLDRIEPVDIQQEMQRSYIDYAMSVIVGRALPEVRDGLKPVHRRVLYAMFDSGFRPDRSHAKSARSVAETMGNYHPHGDASIYDTLVRMAQPWSLRYPLVDGQGNFGSPGNDPPAAMRYTEARLTPLAMEMLREIDEETVDFIPNYDGRVQEPTVLPSRFPNLLANGSGGIAVGMATNIPPHNLRELADAVFWALENHDADEEETLAAVMGRVKGPDFPTAGLIVGSQGTADAYKTGRGSIRMRGVVEVEEDSRGRTSLVITELPYQVNHDNFITSIAEQVRDGKLAGISNIEDQSSDRVGLRIVIEIKR... | 5.6.2.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:7503546}; Note=Reaction requires Mg(2+). {ECO:0000269|PubMed:7503546}; | DNA topological change [GO:0006265]; DNA-templated DNA replication [GO:0006261]; response to antibiotic [GO:0046677] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex [GO:0009330] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA negative supercoiling activity [GO:0034335] | PF03989;PF00521; | 3.30.1360.40;2.120.10.90;3.90.199.10;1.10.268.10; | Type II topoisomerase GyrA/ParC subunit family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897}. | CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01897}; | null | null | null | null | FUNCTION: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and... | Mycobacterium bovis (strain BCG / Pasteur 1173P2) |
A0A0G2QC33 | ATG4B_RAT | MDAATLTYDTLRFAEFEDFPETSEPVWILGRKYSIFTEKDEILSDVASRLWFTYRRNFPAIGGTGPTSDTGWGCMLRCGQMIFAQALVCRHLGRDWRWTQRKRQPDSYFSVLNAFLDRKDSYYSIHQIAQMGVGEGKSIGQWYGPNTVAQVLKKLAVFDTWSSLAVHIAMDNTVVMEEIRRLCRASLPCAGAAALSMESERHCNGLPAGAEVTNRPLAWRPLVLLIPLRLGLTDINEAYVETLKHCFMMPQSLGVIGGKPNSAHYFIGYVGEELIYLDPHTTQPAVELTDSCFIPDESFHCQHPPCRMGIGELDPSIAVG... | 3.4.22.- | null | aggrephagy [GO:0035973]; autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; cellular response to starvation [GO:0009267]; microautophagy [GO:0016237]; mitophagy [GO:0000423]; otolith mineralization completed early in development [GO:0031173]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regu... | autophagosome membrane [GO:0000421]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739] | cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; endopeptidase activity [GO:0004175]; peptidase activity [GO:0008233]; protein-phosphatidylethanolamide deconjugating activity [GO:0019786]; scaffold protein binding [GO:0097110] | PF20166;PF03416; | null | Peptidase C54 family | PTM: Phosphorylation at Ser-383 and Ser-392 promotes autophagy by increasing protein delipidation activity without affecting proteolytic activation of ATG8 proteins. Phosphorylation at Ser-316 by ULK1 inhibits autophagy by decreasing both proteolytic activation and delipidation activities. Phosphorylation at Ser-316 is... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4P1}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y4P1}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q9Y4P1}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y4P1}. Mitochondrion {ECO:0000250|UniProtKB:Q9Y4P1}. Note=Mainly localizes to the cytoplasm... | CATALYTIC ACTIVITY: Reaction=[protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:67548, Rhea:RHEA-COMP:17323, Rhea:RHEA-COMP:17324, ChEBI:CHEBI:15377, ChEBI:CHEBI:64612, ChEBI:CHEBI:172940, Ch... | null | null | null | null | FUNCTION: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. Required for canonical autophagy (macroautophagy), non-canonical autophagy as well as for mitophagy. The protease activity is required for proteolytic activation of ATG8 fami... | Rattus norvegicus (Rat) |
A0A0G2UGT2 | LEC_MYTTR | MTTFLIKHKASGKYFHPKGGTSNPPNGTNLVLHSDIHERMYFQFEVVNERWRYIKHVASEKIVHPFGGKADPLNGTNMVLHQDRHDRALFAMDFFNDNIRHKGGKYIHPKGGSKNPSNGNLTVMHGDEHGAMEFIFVSPKNKDKRVLVYA | null | null | aggregation of unicellular organisms [GO:0098630]; defense response to fungus [GO:0050832]; defense response to Gram-positive bacterium [GO:0050830]; detection of bacterium [GO:0016045]; erythrocyte aggregation [GO:0034117]; innate immune response [GO:0045087]; protein homooligomerization [GO:0051260]; response to Gram... | null | galactose binding [GO:0005534]; peptidoglycan binding [GO:0042834] | null | 2.80.10.50; | null | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:26802895}. | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9-10 for hemagglutinating activity. The activity is decreased by 25% at pH 6.0 and by 50% at pH 4.0. {ECO:0000269|Ref.2}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermally labile. Complete loss of hemagglutinating activity after incubation at 60 degrees Celsius for 30 minutes. {ECO:0000269|Ref.2}; | FUNCTION: D-galactose-binding lectin (PubMed:26802895, Ref.2). Binds both alpha and beta anomer of galactose (Gal). Binds strongly to branched beta-Gal-terminated glycans and weakly to unbranched glycans with alpha-Gal on the end of chains (PubMed:31905927). Has strong affinity for both Gal and GalNAc. Binds glycoprote... | Mytilus trossulus (Blue mussel) |
A0A0H2UNG0 | PULA_STRPN | MRKTPSHTEKKMVYSIRSLKNGTGSVLIGASLVLLAMATPTISSDESTPTTNEPNNRNTTTLAQPLTDTAAGSGKNESDISSPGNANASLEKTEEKPAASPADPAPQTGQDRSSEPTTSTSPVTTETKAEEPIEDNYFRIHVKKLPEENKDAQGLWTWDDVEKPSENWPNGALSFKDAKKDDYGYYLDVKLKGEQAKKISFLINNTAGKNLTGDKSVEKLVPKMNEAWLDQDYKVFSYEPQPAGTVRVNYYRTDGNYDKKSLWYWGDVKNPSSAQWPDGTDFTATGKYGRYIDIPLNEAAREFGFLLLDESKQGDDVKIR... | 3.2.1.41 | null | alpha-glucan biosynthetic process [GO:0030979] | cell surface [GO:0009986]; extracellular region [GO:0005576] | amylopectin binding [GO:2001066]; calcium ion binding [GO:0005509]; glycogen binding [GO:2001069]; limit dextrinase activity [GO:0010303]; polysaccharide binding [GO:0030247]; pullulan binding [GO:2001067]; pullulanase activity [GO:0051060] | PF00128;PF02922;PF00746;PF03714;PF18033;PF04650; | 2.60.40.1110;2.60.40.1220;3.20.20.80;2.60.40.1180;2.60.40.10; | Glycosyl hydrolase 13 family | null | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. Cell surface {ECO:0000250|UniProtKB:Q9F930}. Note=Localizes to cytoplasm in the lung alveolar type II cells of the mouse and human hosts. {ECO:0000269|PubMed:17187076, ECO:00002... | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the alpha- and beta-limit dextrins of amylopectin and glycogen.; EC=3.2.1.41; Evidence={ECO:0000269|PubMed:20497336, ECO:0000269|PubMed:21565699}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=360 uM for para-nitrophenyl-alpha-D-maltopentaoside (pNP-M5) (at 25 degrees Celsius) {ECO:0000269|PubMed:21565699}; Note=kcat is 270 min(-1) for pNP-M5. {ECO:0000269|PubMed:21565699}; | null | null | null | FUNCTION: Virulence factor (By similarity). Involved in the degradation of glycogen of the mammalian host cells (PubMed:21565699). Hydrolyzes the alpha-1,6-branchpoints of glycogen (PubMed:20497336, PubMed:21565699). Hydrolyzes pullulan. Does not hydrolyze dextran (PubMed:20497336). Binds to mouse lung alveolar type II... | Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) |
A0A0H2URG7 | GTFA_STRPN | MTIYNINLGIGWASSGVEYAQAYRAGVFRKLNLSSKFIFTDMILADNIQHLTANIGFDDNQVIWLYNHFTDIKIAPTSVTVDDVLAYFGGEESHREKNGKVLRVFFFDQDKFVTCYLVDENKDLVQHAEYVFKGNLIRKDYFSYTRYCSEYFAPKDNVAVLYQRTFYNEDGTPVYDILMNQGKEEVYHFKDKIFYGKQAFVRAFMKSLNLNKSDLVILDRETGIGQVVFEEAQTAHLAVVVHAEHYSENATNEDYILWNNYYDYQFTNADKVDFFIVSTDRQNEVLQEQFAKYTQHQPKIVTIPVGSIDSLTDSSQGRKP... | 2.4.1.- | null | protein O-linked glycosylation via serine [GO:0018242] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886]; protein N-acetylglucosaminyltransferase complex [GO:0017122] | glycosyltransferase activity [GO:0016757]; nucleotide binding [GO:0000166] | PF00534; | 3.40.50.2000; | Glycosyltransferase group 1 family, Glycosyltransferase 4 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01472}. Cell membrane {ECO:0000250|UniProtKB:A1C3L9, ECO:0000255|HAMAP-Rule:MF_01472}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01472}. Note=Cell membrane association requires GtfB. {ECO:0000250|UniProtKB:A1C3L9, ECO:0000255|HAMAP-Rule:MF_01472}. | CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-[N-acetyl-alpha-D-glucosaminyl]-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:59872, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15471, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:143279; Evidenc... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat for hydrolysis of UDP-N-acetyl-alpha-D-glucosamine with transfer of GlcNAc to PsrP-SSR1 and generation of UDP is 76.0 min(-1) for GtfA-GtfB and 7.35 min(-1) for GtfA alone. {ECO:0000269|PubMed:24936067}; | PATHWAY: Protein modification; protein glycosylation. {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000269|PubMed:24936067, ECO:0000269|PubMed:28246170}. | null | null | FUNCTION: Required for the polymorphic O-glycosylation of serine-rich repeat protein PsrP. Catalyzes the first step in glycosylation by transferring N-acetylglucosamine from UDP-GlcNAc to serine residues in PsrP (PubMed:24936067, PubMed:28246170). Part of the accessory SecA2/SecY2 system specifically required to export... | Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) |
A0A0H2URJ6 | GLYE_STRPN | MRNTKRAVVFAGDYAYIRQIETAMKSLCRHNSHLKIYLLNQDIPQEWFSQIRIYLQEMGGDLIDCKLIGSQFQMNWSNKLPHINHMTFARYFIPDFVTEDKVLYLDSDLIVTGDLTDLFELDLGENYLAAARSCFGAGVGFNAGVLLINNKKWGSETIRQKLIDLTEKEHENVEEGDQSILNMLFKDQYSSLEDQYNFQIGYDYGAATFKHQFIFDIPLEPLPLILHYISQDKPWNQFSVGRLREVWWEYSLMDWSVILNEWFSKSVKYPSKSQIFKLQCVNLTNSWCVEKIDYLAEQLPEVHFHIVAYTNMANELLALT... | null | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:28246170}; | protein glycosylation [GO:0006486] | null | glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166] | PF01501; | null | Glycosyltransferase 8 family | null | null | null | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:28246170}. | null | null | FUNCTION: Involved in the polymorphic O-glycosylation of the serine-rich repeat protein PsrP. Catalyzes the third step in glycosylation of PsrP in this bacteria. Transfers galactose from UDP-galactose to the terminal glucose moiety of already-glycosylated PsrP (using the short substrate PsrP-GlcNAc-Glc). Has a very mar... | Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) |
A0A0H2URK1 | PSRP_STRPN | MTETVEDKVSHSITGLDILKGIVAAGAVISGTVATQTKVFTNESAVLEKTVEKTDALATNDTVVLGTISTSNSASSTSLSASESASTSASESASTSASTSASTSASESASTSASTSISASSTVVGSQTAAATEATAKKVEEDRKKPASDYVASVTNVNLQSYAKRRKRSVDSIEQLLASIKNAAVFSGNTIVNGAPAINASLNIAKSETKVYTGEGVDSVYRVPIYYKLKVTNDGSKLTFTYTVTYVNPKTNDLGNISSMRPGYSIYNSGTSTQTMLTLGSDLGKPSGVKNYITDKNGRQVLSYNTSTMTTQGSGYTWGN... | null | null | cell adhesion [GO:0007155]; single-species biofilm formation [GO:0044010]; symbiont-mediated perturbation of host defense response [GO:0052031] | cell surface [GO:0009986]; extracellular region [GO:0005576]; Gram-positive-bacterium-type cell wall [GO:0009275] | DNA binding [GO:0003677] | PF00746; | null | Serine-rich repeat protein (SRRP) family | PTM: Glycosylated (PubMed:19627498). Only truncated substrates greater than 25 residues long are glycosylated by the Gtf1-Gtf2 complex in vitro; only Ser residues have been seen to be glycosylated. Based on electrophoretic mobility it is probable that most of the Ser residues in SSR1 and SSR2 are O-GlcNAcylated (PubMed... | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000269|PubMed:19627498}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. Cell surface {ECO:0000269|PubMed:19627498}. | null | null | null | null | null | FUNCTION: Protein that allows bacteria to adhere to mammalian host cells. Required for full virulence in mouse infection models when infected intranasally (PubMed:16861665). Required for adhesion to host cells in vitro and for persistence in the lower respiratory tract (PubMed:18507531). Binds host keratin 10 (KRT10) o... | Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) |
A0A0H2URU9 | COMGC_STRPN | MKKMMTFLKKAKVKAFTLVEMLVVLLIISVLFLLFVPNLTKQKEAVNDKGKAAVVKVVESQAELYSLEKNEDASLRKLQADGRITEEQAKAYKEYNDKNGGANRKVND | null | null | establishment of competence for transformation [GO:0030420]; protein secretion by the type II secretion system [GO:0015628] | cell surface [GO:0009986]; extracellular region [GO:0005576]; pilus [GO:0009289]; plasma membrane [GO:0005886]; type II protein secretion system complex [GO:0015627] | null | PF07963; | 3.30.700.10; | ComGC family | PTM: Undergoes proteolytic cleavage. {ECO:0000269|PubMed:24550320, ECO:0000269|PubMed:28659339}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P25955}; Single-pass membrane protein {ECO:0000250|UniProtKB:P25955, ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:P25955}. Fimbrium {ECO:0000250|UniProtKB:Q8DN88}. Secreted {ECO:0000269|PubMed:24550320}. Note=The unprocessed form is an integral membrane pr... | null | null | null | null | null | FUNCTION: Major component of the type IV-like pilus (T4P) that plays a role in transformation (PubMed:28659339). Transformation pili are dynamically extended and retracted, perhaps thereby promoting DNA uptake and transformation (By similarity). Required for transformation (PubMed:24550320). Required for DNA binding (B... | Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) |
A0A0H2US87 | OSPC3_SHIFL | MKIPEAVNHINVQNNIDLVDGKINPNKDTKALQKNISCVTNSSSSGISEKHLDHCADTVKSFLRKSIAAQSYSKMFSQGTSFKSLNLSIEAPSGARSSFRSLEHLDKVSRHYLSEIIQKTHPLSSDERHLLSIIINSDFNFRHQSNANLSNNTLNIKSFDKIKSENIQTYKNTFSEDIEEIANHDFVFFGVEISNHQETLPLNKTHHTVDFGANAYIIDHDSPYGYMTLTDHFDNAIPPVFYHEHQSFFLDNFKEVVDEVSRYVHGNQGKTDVPIFNTKDMRLGIGLHLIDFIRKSKDQRFREFCYNKNIDPVSLDRIIN... | 4.3.99.- | null | modulation by symbiont of defense-related host calcium ion flux [GO:0052162]; symbiont-mediated perturbation of host programmed cell death [GO:0052040]; symbiont-mediated suppression of host calcium or calmodulin-mediated signal transduction [GO:0075135]; symbiont-mediated suppression of host programmed cell death [GO:... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430] | ADP-riboxanase activity [GO:0140740]; calmodulin binding [GO:0005516]; toxin activity [GO:0090729] | PF06128; | null | OspC family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23684308}. Host cytoplasm {ECO:0000305|PubMed:34409271}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000269|PubMed:23684308}. | CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + NAD(+) = ADP-riboxanated L-argininyl-[protein] + H(+) + NH4(+) + nicotinamide; Xref=Rhea:RHEA:69500, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:17719, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:28938, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540, ChEBI:CHEBI:184300; Evidence=... | null | null | null | null | FUNCTION: ADP-riboxanase effector that inhibits host cell pyroptosis (PubMed:23684308, PubMed:34409271, PubMed:34671164, PubMed:36624349). Acts by mediating arginine ADP-riboxanation of host CASP4/CASP11, blocking CASP4/CASP11 autoprocessing (PubMed:34671164, PubMed:35338844, PubMed:35568036, PubMed:36624349, PubMed:37... | Shigella flexneri |
A0A0H2USG1 | IPA14_SHIFL | MIKSTNIQAIGSGIMHQINNVYSLTPLSLPMELTPSCNEFYLKTWSEWEKNGTPGEQRNIAFNRLKICLQNQEAELNLSELDLKTLPDLPPQITTLEIRKNLLTHLPDLPPMLKVIHAQFNQLESLPALPETLEELNAGDNKIKELPFLPENLTHLRVHNNRLHILPLLPPELKLLVVSGNRLDSIPPFPDKLEGLALANNFIEQLPELPFSMNRAVLMNNNLTTLPESVLRLAQNAFVNVAGNPLSGHTMRTLQQITTGPDYSGPQIFFSMGNSATISAPEHSLADAVTAWFPENKQSDVSQIWHAFEHEEHANTFSAF... | 2.3.2.27 | null | protein ubiquitination [GO:0016567]; symbiont-mediated suppression of host NF-kappaB cascade [GO:0085034] | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430] | toxin activity [GO:0090729]; ubiquitin protein ligase activity [GO:0061630] | PF14496;PF12468; | 1.20.58.90;3.80.10.10;1.20.58.360;1.20.1270.130; | LRR-containing bacterial E3 ligase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8VSC3}. Host cytoplasm {ECO:0000250|UniProtKB:Q8VSC3}. Note=Secreted via Mxi-Spa type III secretion system (T3SS), and delivered into the host cytoplasm. {ECO:0000250|UniProtKB:Q8VSC3}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:18997778, ECO:0000269|PubMed:27572974, ECO:0000269|PubMed:352942... | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:18997778, ECO:0000269|PubMed:27572974, ECO:0000269|PubMed:35294289}. | null | null | FUNCTION: E3 ubiquitin-protein ligase effector that inhibits host cell innate immunity during bacterial infection by catalyzing 'Lys-48'-linked polyubiquitination and subsequent degradation of host RNF31/HOIP and RBCK1/HOIL-1 (PubMed:18997778, PubMed:27572974, PubMed:35294289, PubMed:36610722). Host RNF31/HOIP is the c... | Shigella flexneri |
A0A0H2V871 | IROE_ECOL6 | MYAREYRSTRPHKAIFFHLSCLTLICSAQVYAKPDMRPLGPNIADKGSVFYHFSATSFDSVDGTRHYRVWTAVPNTTAPASGYPILYMLDGNAVMDRLDDELLKQLSEKTPPVIVAVGYQTNLPFDLNSRAYDYTPAAESRKTDLHSGRFSRKSGGSNNFRQLLETRIAPKVEQGLNIDRQRRGLWGHSYGGLFVLDSWLSSSYFRSYYSASPSLGRGYDALLSRVTAVEPLQFCTKHLAIMEGSATQGDNRETHAVGVLSKIHTTLTILKDKGVNAVFWDFPNLGHGPMFNASFRQALLDISGENANYTAGCHELSH | 3.1.1.107 | null | null | plasma membrane [GO:0005886] | carboxylic ester hydrolase activity [GO:0052689] | PF00756; | 3.40.50.1820; | Esterase D family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:16076215}; Single-pass membrane protein {ECO:0000255}; Periplasmic side {ECO:0000305|PubMed:16076215}. | CATALYTIC ACTIVITY: Reaction=enterobactin + H2O = N-(2,3-dihydroxybenzoyl)-L-serine trimer; Xref=Rhea:RHEA:60384, ChEBI:CHEBI:15377, ChEBI:CHEBI:77805, ChEBI:CHEBI:143020; EC=3.1.1.107; Evidence={ECO:0000269|PubMed:16076215}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60385; Evidence={ECO:0000269|PubMed:16076... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16 uM for Ent {ECO:0000269|PubMed:16076215}; KM=3.4 uM for Fe-Ent {ECO:0000269|PubMed:16076215}; KM=29 uM for MGE {ECO:0000269|PubMed:16076215}; KM=4.8 uM for Fe-MGE {ECO:0000269|PubMed:16076215}; KM=39 uM for DGE {ECO:0000269|PubMed:16076215}; KM=4.6 uM for Fe-DGE... | null | null | null | FUNCTION: Catalyzes the hydrolysis of both the apo and Fe3(+)-bound forms of enterobactin (Ent), monoglucosyl-C-Ent (MGE), diglucosyl-C-Ent (DGE) and triglucosyl-C-Ent (TGE). It prefers apo siderophores as substrates and hydrolyzes the Fe3(+)-bound siderophores very inefficiently. Tends to hydrolyze the trilactone just... | Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) |
A0A0H2V8B5 | TCPC_ECOL6 | MIAYENIEFFICLVNVLGNNMYNILFFIFLSIAIPFLLFLAWKQHLKTKEIRSYLLKEGYNIIFNGEGNSYLAFNISNATFRAGNLTSNDYFQASISYIHDYRWEWKEVEAKKINNIFIIYISNIDFPSQKLFYRNNKSLAEIDWAKLQAIFHQPYEIQNDVMQDNNNTHYDFFISHAKEDKDTFVRPLVDELNRLGVIIWYDEQTLEVGDSLRRNIDLGLRKANYGIVILSHNFLNKKWTQYELDSLINRAVYDDNKIILPIWHNINAQEVSKYSHYLADKMALQTSLYSVKEIARELAEIAYRRR | 3.2.2.-; 3.2.2.6 | null | NAD catabolic process [GO:0019677]; negative regulation of MyD88-dependent toll-like receptor signaling pathway [GO:0034125]; signal transduction [GO:0007165] | extracellular region [GO:0005576]; membrane [GO:0016020] | NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; NADP+ nucleosidase activity [GO:0050135] | PF13676; | 3.40.50.10140; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18327267}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence={ECO:0000269|PubMed:29395922}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence={E... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=196 uM for NAD(+) {ECO:0000269|PubMed:29395922}; | null | null | null | FUNCTION: Virulence factor that suppresses host Toll-like receptor (TLR)-mediated cytokine production upon infection, thereby increasing bacterial burden in the urinary tract and promoting renal tissue damage (PubMed:18327267, PubMed:20886104). Acts as a NAD(+) hydrolase (NADase) by catalyzing cleavage of NAD(+) into A... | Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) |
A0A0H2VDN9 | ESIB_ECOL6 | MKKSLLAVMLTGLFALVSLPALGNVNLEQLKQKAESGEAKAQLELGYRYFQGNETTKDLTQAMDWFRRAAEQGYTPAEYVLGLRYMNGEGVPQDYAQAVIWYKKAALKGLPQAQQNLGVMYHEGNGVKVDKAESVKWFRLAAEQGRDSGQQSMGDAYFEGDGVTRDYVMAREWYSKAAEQGNVWSCNQLGYMYSRGLGVERNDAISAQWYRKSATSGDELGQLHLADMYYFGIGVTQDYTQSRVLFSQSAEQGNSIAQFRLGYILEQGLAGAKEPLKALEWYRKSAEQGNSDGQYYLAHLYDKGAEGVAKNREQAISWYT... | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:24099525}; Note=The physiological metal is unknown. {ECO:0000305|PubMed:24099525}; | ERAD pathway [GO:0036503]; negative regulation of immune response [GO:0050777]; negative regulation of neutrophil activation [GO:1902564] | cell surface [GO:0009986] | IgA binding [GO:0019862]; metal ion binding [GO:0046872] | PF08238; | 1.25.40.10; | null | null | SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:23882011}. Note=Accumulates at 1 cell pole in the bladder of mice infected with this strain, in overexpressing bacteria the protein is found all over the cell surface but not in the secreted fraction (PubMed:23882011). Human blood sera from clinical patients with u... | null | null | null | null | null | FUNCTION: Upon host (human neutrophil) infection interferes with productive FCAR signaling, inhibiting secreted IgA (SIgA) effector functions and probably avoiding neutrophil activation. Inhibits the SIgA-mediated oxidative burst by neutrophils, decreases generation of ROS (reactive oxygen species) by neutrophils and r... | Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) |
A0A0H2VG78 | GLCP_STAES | MKANKYLIFILGALGGLLYGYDNGVISGALLFIHKDIPLNSTTEGIVVSSMLIGAIVGAGSSGPLADKLGRRRLVMLIAIVFIIGALILAASTNLALLIIGRLIIGLAVGGSMSTVPVYLSEMAPTEYRGSLGSLNQLMITIGILAAYLVNYAFADIEGWRWMLGLAVVPSVILLVGIYFMPESPRWLLENRNEEAARQVMKITYDDSEIDKELKEMKEINAISESTWTVIKSPWLGRILIVGCIFAIFQQFIGINAVIFYSSSIFAKAGLGEAASILGSVGIGTINVLVTIVAIFVVDKIDRKKLLVGGNIGMIASLLI... | null | null | null | plasma membrane [GO:0005886] | glucose transmembrane transporter activity [GO:0005355]; symporter activity [GO:0015293] | PF00083; | 1.20.1250.20; | Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24127585}; Multi-pass membrane protein {ECO:0000269|PubMed:24127585}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=29 uM for glucose {ECO:0000269|PubMed:24127585}; Vmax=160 nmol/min/mg enzyme {ECO:0000269|PubMed:24127585}; | null | null | null | FUNCTION: Transporter highly specific for glucose uptake. {ECO:0000269|PubMed:24127585}. | Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) |
A0A0H2WWV6 | TARM_STAAC | MKKIFMMVHELDVNKGGMTSSMFNRSKEFYDADIPADIVTFDYKGNYDEIIKALKKQGKMDRRTKMYNVFEYFKQISNNKHFKSNKLLYKHISERLKNTIEIEESKGISRYFDITTGTYIAYIRKSKSEKVIDFFKDNKRIERFSFIDNKVHMKETFNVDNKVCYQVFYDEKGYPYISRNINANNGAVGKTYVLVNKKEFKNNLALCVYYLEKLIKDSKDSIMICDGPGSFPKMFNTNHKNAQKYGVIHVNHHENFDDTGAFKKSEKYIIENANKINGVIVLTEAQRLDILNQFDVENIFTISNFVKIHNAPKHFQTEKI... | 2.4.1.70 | null | cell wall organization [GO:0071555]; teichoic acid biosynthetic process [GO:0019350] | cytoplasm [GO:0005737] | poly(ribitol-phosphate) N-acetylglucosaminyltransferase activity [GO:0047269] | PF00534; | 3.40.50.2000; | Glycosyltransferase group 1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:20185825}. | CATALYTIC ACTIVITY: Reaction=4-O-[(D-ribitylphospho)(n)-di{(2R)-glycerylphospho}]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + n UDP-N-acetyl-alpha-D-glucosamine = 4-O-([2-N-acetyl-alpha-D-glucosaminyl-1-D-ribitylphospho](n)-di{[2R]-1-glycerylphospho})-N... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=65 uM for UDP-GlcNAc {ECO:0000269|PubMed:25624472}; KM=390 uM for WTA {ECO:0000269|PubMed:25624472}; Note=kcat is 126 min(-1). {ECO:0000269|PubMed:25624472}; | PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid biosynthesis. {ECO:0000269|PubMed:20185825}. | null | null | FUNCTION: Attaches N-acetyl-alpha-D-glucosamine residues to poly(RboP)-wall teichoic acids (WTAs). {ECO:0000269|PubMed:20185825, ECO:0000269|PubMed:25624472, ECO:0000269|PubMed:25697358}. | Staphylococcus aureus (strain COL) |
A0A0H2WZ38 | GATD_STAAC | MHELTIYHFMSDKLNLYSDIGNIIALRQRAKKRNIKVNVVEINETEGITFDECDIFFIGGGSDREQALATKELSKIKTPLKEAIEDGMPGLTICGGYQFLGKKYITPDGTELEGLGILDFYTESKTNRLTGDIVIESDTFGTIVGFENHGGRTYHDFGTLGHVTFGYGNNDEDKKEGIHYKNLLGTYLHGPILPKNYEITDYLLEKACERKGIPFEPKEIDNEAEIQAKQVLIDRANRQKKSR | 3.5.1.2; 6.3.5.13 | null | cell wall organization [GO:0071555]; cobalamin biosynthetic process [GO:0009236]; glutamine metabolic process [GO:0006541]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360] | null | carbon-nitrogen ligase activity on lipid II [GO:0140282]; glutaminase activity [GO:0004359] | PF07685; | 3.40.50.880; | CobB/CobQ family, GatD subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H2O + L-glutamine = ADP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + L-glutamate + phosph... | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02213, ECO:0000269|PubMed:22303291}. | null | null | FUNCTION: The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide (PubMed:22303291). The GatD subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia. The resulting ammonia molecule is channeled to the active site of MurT (PubMed:... | Staphylococcus aureus (strain COL) |
A0A0H2Z7X0 | TPBB_PSEAB | MNRRRRYTGSNPSLRRVLYRAHLGVALVAVFTAGLAVTLVGLLTLRAYADPNQQLIARSISYTVEAAVVFGDAQAAEESLALIASSEEVSSAIVYDRQGQPLASWHRESTGPLHLLEQQLAHWLLSAPTEQPILHDGQKIGSVEVKGSGGSLLRFLLTGFAGMVLCLLLTALGAFYLSRRLVRGIVGPLDQLAKVAHTVRRERDFEKRVPEAGIAELSQLGEDFNALLDELESWQARLQDENASLAHQAHHDSLTSLPNRAFFEGRLSRALRDASEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRE... | 2.7.7.65 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9I4L5}; Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000250|UniProtKB:Q9I4L5}; | signal transduction [GO:0007165] | plasma membrane [GO:0005886] | GTP binding [GO:0005525]; metal ion binding [GO:0046872]; transferase activity [GO:0016740] | PF17152;PF00990;PF00672; | 3.30.70.270;6.10.340.10; | null | PTM: Phosphorylated at both Tyr residues and Ser/Thr residues (PubMed:20946878). Dephosphorylated and inactivated by TpbA (PubMed:20946878). {ECO:0000269|PubMed:20946878}. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=2 GTP = 3',3'-c-di-GMP + 2 diphosphate; Xref=Rhea:RHEA:24898, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58805; EC=2.7.7.65; Evidence={ECO:0000269|PubMed:20946878}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24899; Evidence={ECO:0000269|PubMed:20946878}; | null | PATHWAY: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules (PubMed:20946878). Important for the regulation of biofilm maintenance when exposed to peroxide (PubMed:34694901). {ECO:0000269|PubMed:20946878, ECO:0000269|PubMed:34694901}.; FUNCTION: Part of the YfiB-TpbB-YfiR (or y... | Pseudomonas aeruginosa (strain UCBPP-PA14) |
A0A0H2ZFK2 | TPBA_PSEAB | MHRSPLAWLRLLLAAVLGAFLLGGPLHAAETAAPRSPAWAQAVDPSINLYRMSPTLYRSALPNAQSVALLQRLQVKTVVSFIKDDDRAWLGQAPVRVVSLPTHADRVDDAEVLSVLRQLQAAEREGPVLMHCKHGNNRTGLFAAMYRIVVQGWDKQAALEEMQRGGFGDEDDMRDASAYVRGADVDGLRLAMANGECSPSRFALCHVREWMAQALDRP | 3.1.3.16; 3.1.3.48 | null | dephosphorylation [GO:0016311] | periplasmic space [GO:0042597] | phosphoprotein phosphatase activity [GO:0004721] | PF03162; | 3.90.190.10; | Protein-tyrosine phosphatase family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:19543378}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000269|PubMed:19543378, ECO:0000269|PubMed:2094687... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.21 mM for pNPP {ECO:0000269|PubMed:23524133}; Note=kcat is 0.00162 sec(-1) with pNPP as substrate. {ECO:0000269|PubMed:23524133}; | null | null | null | FUNCTION: Phosphatase that regulates diverse phenotypes in P.aeruginosa via regulation of the concentration of cellular c-di-GMP (PubMed:19543378). Acts by dephosphorylating the membrane-anchored diguanylate cyclase TpbB at tyrosine and serine/threonine sites, leading to inactivation of TpbB and reduced c-di-GMP produc... | Pseudomonas aeruginosa (strain UCBPP-PA14) |
A0A0H2ZL64 | PULA_STRP2 | MRKTPSHTEKKMVYSIRSLKNGTGSVLIGASLVLLAMATPTISSDESTPTTNEPNNRNTTTLAQPLTDTAADSGKNESDISSPRNANASLEKTEEKPATEPTTSTSPVTTETKAEEPIEDNYFRIHVKKLPEENKDAQGLWTWDDVEKPSENWPNGALSFKDAKKDDYGYYLDVKLKGEQAKKISFLINNTAGKNLTGDKSVEKLVPKMNEAWLDQDYKVFSYEPQPAGTVRVNYYRTDGNYDKKSLWYWGDVKNPSSAQWPDGTDFTATGKYGRYIDIPLNEAAREFGFLLLDESKQGDDVKIRKENYKFTDLKNHSQI... | 3.2.1.41 | null | carbohydrate metabolic process [GO:0005975] | cell surface [GO:0009986]; extracellular region [GO:0005576] | carbohydrate binding [GO:0030246]; metal ion binding [GO:0046872]; pullulanase activity [GO:0051060] | PF00128;PF02922;PF00746;PF03714;PF18033;PF04650; | 2.60.40.1110;2.60.40.1220;3.20.20.80;2.60.40.1180;2.60.40.10; | Glycosyl hydrolase 13 family | null | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. Cell surface {ECO:0000250|UniProtKB:Q9F930}. Note=Localizes to cytoplasm in the lung alveolar type II cells of the mouse and human hosts. {ECO:0000250|UniProtKB:A0A0H2UNG0}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the alpha- and beta-limit dextrins of amylopectin and glycogen.; EC=3.2.1.41; Evidence={ECO:0000250|UniProtKB:A0A0H2UNG0}; | null | null | null | null | FUNCTION: Virulence factor (PubMed:17041037). Involved in the degradation of glycogen of the mammalian host cells. Hydrolyzes the alpha-1,6-branchpoints of glycogen. Hydrolyzes pullulan. Does not hydrolyze dextran. Binds to mouse lung alveolar type II cells that are rich in glycogen stores. Is an alpha-glucan-specific ... | Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
A0A0H2ZMF9 | PBP2A_STRP2 | MKLDKLFEKFLSLFKKETSELEDSDSTILRRSRSDRKKLAQVGPIRKFWRRYHLTKIILILGLSAGLLVGIYLFAVAKSTNVNDLQNALKTRTLIFDREEKEAGALSGQKGTYVELTDISKNLQNAVIATEDRSFYKNDGINYGRFFLAIVTAGRSGGGSTITQQLAKNAYLSQDQTVERKAKEFFLALELSKKYSKEQILTMYLNNAYFGNGVWGVEDASKKYFGVSASEVSLDQAATLAGMLKGPELYNPLNSVEDSTNRRDTVLQNMVAAGYIDKNQETEAAEVDMTSQLHDKYEGKISDYRYPSYFDAVVNEAVSK... | 2.4.99.28; 3.4.16.4 | null | cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; proteolysis [GO:0006508]; regulation of cell shape [GO:0008360]; response to antibiotic [GO:0046677] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | acyltransferase activity [GO:0016746]; penicillin binding [GO:0008658]; peptidoglycan glycosyltransferase activity [GO:0008955]; serine-type D-Ala-D-Ala carboxypeptidase activity [GO:0009002] | PF00912;PF00905; | 6.20.370.110;1.10.3810.10;3.40.710.10; | Glycosyltransferase 51 family; Transpeptidase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29487215}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8DNB6}. Secreted, cell wall {ECO:0000305}. Note=Localizes to sites of new peptidoglycan (PG) synthesis at midcell independently of MacP. {ECO:0000269|PubMed:29487215}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000250|UniProtKB:Q8DNB6}; CATALYTIC ACTIVITY: Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](... | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan (PG) from the lipid intermediates (By similarity). Binds dansylated lipid II and catalyzes the polymerization of glycan chains. Hydrolyzes S2d (N-benzoyl-D-alanylmercaptoacetic acid) molecule, a synthetic thiolester analog of cell wall stem peptide.... | Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
A0A0H2ZNH9 | WALK_STRP2 | MLDLLKQTIFTRDFIFILILLGFILVVTLLLLENRRDNIQLKQINQKVKDLIAGDYSKVLDMQGGSEITNITNNLNDLSEVIRLTQENLEQESKRLNSILFYMTDGVLATNRRGQIIMINDTAKKQLGLVKEDVLNRSILELLKIEENYELRDLITQSPELLLDSQDINGEYLNLRVRFALIRRESGFISGLVAVLHDTTEQEKEERERRLFVSNVSHELRTPLTSVKSYLEALDEGALCETVAPDFIKVSLDETNRMMRMVTDLLHLSRIDNATSHLDVELINFTAFITFILNRFDKMKGQEKEKKYELVRDYPINSIW... | 2.7.13.3; 3.9.1.- | null | cellular response to phosphate starvation [GO:0016036]; regulation of DNA-templated transcription [GO:0006355]; signal transduction [GO:0007165] | plasma membrane [GO:0005886] | phosphoprotein phosphatase activity [GO:0004721]; phosphorelay sensor kinase activity [GO:0000155]; protein histidine kinase activity [GO:0004673] | PF02518;PF00512;PF00989; | 1.10.287.130;1.10.8.500;3.30.565.10;3.30.450.20; | null | PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q8DPL8}. | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type III membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:23013245}; | null | null | null | null | FUNCTION: Member of the two-component regulatory system WalK/WalR that regulates genes involved in cell wall metabolism (By similarity). Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to WalR (By similarity). In turn, WalR binds to the upstream ... | Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
A0A0H2ZQ76 | PCSB_STRP2 | MKKKILASLLLSTVMVSQVAVLTTAHAETTDDKIAAQDNKISNLTAQQQEAQKQVDQIQEQVSAIQAEQSNLQAENDRLQAESKKLEGEITELSKNIVSRNQSLEKQARSAQTNGAVTSYINTIVNSKSITEAISRVAAMSEIVSANNKMLEQQKADKKAISEKQVANNDAINTVIANQQKLADDAQALTTKQAELKAAELSLAAEKATAEGEKASLLEQKAAAEAEARAAAVAEAAYKEKRASQQQSVLASANTNLTAQVQAVSESAAAPVRAKVRPTYSTNASSYPIGECTWGVKTLAPWAGDYWGNGAQWATSAAAA... | 3.2.1.- | null | null | cell septum [GO:0030428]; extracellular region [GO:0005576]; plasma membrane [GO:0005886] | hydrolase activity [GO:0016787] | PF05257; | 6.10.250.3150;3.90.1720.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17449619}; Peripheral membrane protein {ECO:0000305|PubMed:22006325}; Extracellular side {ECO:0000305|PubMed:22006325}. Cell septum {ECO:0000269|PubMed:22006325}. Secreted {ECO:0000269|PubMed:17449619}. Note=Localizes to outer membrane surface, probably due to hyd... | null | null | null | null | null | FUNCTION: Peptidoglycan-hydrolase activity (PubMed:24804636). Required in maintaining normal growth and cellular morphology (PubMed:19270090, PubMed:22006325). Involved in splitting of the septum during cell division (By similarity). {ECO:0000250|UniProtKB:Q8DMY4, ECO:0000269|PubMed:19270090, ECO:0000269|PubMed:2200632... | Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
A0A0H2ZQB9 | EGTUB_STRP2 | MTNLIATFQDRFGDWLTALSQHLQLSLLTLLLAILLAIPLAVYLRYHEKLADWVLQIAGIFQTIPSLALLGLFIPLMGIGTLPALTALVIYAIFPILQNTITGLKGIDPSLQEAGIAFGMTRWERLKKFEIPLAMPVIMSGIRTAAVLIIGTATLATLIGAGGLGSFILLGIDRNNASLILIGALSSAVLAIAFNFLLKVMEKAKLRTIFSGFALMALLLGLSYSPALLAQKEKENLIIAGKIGPEPEILANMYKLLIEENTSMTATVKPNFGTTSFLYEALKKGDIDIYPEFTGTVTESLLQPSPKVSHEPEQVYQVAR... | null | null | amino acid transport [GO:0006865]; glycine betaine transport [GO:0031460]; quaternary ammonium group transport [GO:0015697] | ATP-binding cassette (ABC) transporter complex [GO:0043190] | ABC-type quaternary ammonium compound transporting activity [GO:0015418] | PF00528;PF04069; | 1.10.3720.10;3.40.190.10; | Binding-protein-dependent transport system permease family; OsmX family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|RuleBase:RU363032}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU363032}. | null | null | null | null | null | FUNCTION: Part of an ABC transporter complex EgtU required for the uptake of ergothioneine (EGT), a natural low-molecular weight (LMW) thiol antioxidant (PubMed:36481738). Responsible for the translocation of the substrate across the membrane (PubMed:36481738). Also contains a C-terminal periplasmic solute-binding doma... | Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
A0A0H2ZQL5 | CCRZ_STRP2 | MDLGDNELTLTPIPGKSGKAYMGSYPDGKRIFVKMNTSPILPGLAREQIAPQLLWSRRLADGRDMCAQEWLTGKILTPYDMNRKQIVNILTRLHRSRPLMTQLSRLGYAMETPVDLLQSWQETAPDALRKNHFISEVMADLRQTIPGFREDHATIVHGDVRHSNWIETDSGLIYLVDWDSVRLTDRMFDVAHMLCHYISEHQWKEWLTYYGYKYNQTVLSKLYWYGQLSYLSQISKYYMNQDLENVNREIHGLRHFRDKYGKRR | 2.7.1.15; 2.7.1.229 | null | cell cycle [GO:0007049]; cell division [GO:0051301]; DNA damage response [GO:0006974]; DNA replication initiation [GO:0006270]; regulation of cell cycle [GO:0051726] | cell division site [GO:0032153]; cytoplasm [GO:0005737] | ATP binding [GO:0005524]; carbohydrate kinase activity [GO:0019200]; phosphotransferase activity, alcohol group as acceptor [GO:0016773]; ribokinase activity [GO:0004747] | PF01636; | 3.90.1200.10; | Aminoglycoside phosphotransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:34373624}. Note=Localizes at mid-cell, forming a patchy ring. Disassembles from the old septum to assemble at the newly formed division site. Colocalizes with FtsZ during the full cell cycle. Colocalizes with DnaA in newborn cells. {ECO:0000269|PubMed:34373624}. | 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:0000250|UniProtKB:C0SPC1}; CATALYTIC ACTIVITY: Reaction=2-deoxy-D-ribose + ATP = 2-deoxy-D-rib... | null | null | null | null | FUNCTION: Plays a role in cell cycle regulation and chromosome integrity. Activates DnaA-dependent chromosomal DNA replication initiation ensuring that the chromosome is replicated at the right time during the cell cycle (PubMed:34373624). May regulate replication initiation through phosphorylation of a possible second... | Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
A0A0H3AIG7 | VGRG1_VIBC3 | MATLAYSIEVEGLEDETLVVRGFHGQESLSNSVFLGQACYGFRYEVQLASRVSNLTAEQMVDKRAELKLYRNSQLVQRVHGIVRAFSQGDIGHHHTFYQLTLVPALERLSLRHNSRIFQKQTVPEILSILLQEMGINDYAFALKRDGVQREFCVQYRESDIDFLHRLAAEEGLVYSFVHEAGKHTLYFSDASDSLSKLPEPIPYNALVGGAIDTPYIHGLTYRTQAEVSEVQLKDYSFKKPAYSFLQTVQGTELDYQQTRYQHFDAPGRYKDDVNGAAFSQIRLDYLRRHAHTATGQSNEPLLRAGYKFDLQEHLDPAMN... | 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22898822}; Note=Binds 2 Mg(2+) ions per subunit. Can also use Mn(2+) ions instead of Mg(2+). {ECO:0000269|PubMed:22898822}; | actin filament depolymerization [GO:0030042]; isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine [GO:0018153] | extracellular region [GO:0005576]; host cell cytosol [GO:0044164] | acid-amino acid ligase activity [GO:0016881]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; toxin activity [GO:0090729] | PF16671;PF04717;PF05954; | 2.30.110.50;4.10.220.110;1.10.3680.20;3.55.50.10;2.40.50.230; | VgrG protein family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9KS45}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:22898822}. Note=Secreted via the type VI secretion system. {ECO:0000250|UniProtKB:Q9KS45}. | null | null | null | null | null | FUNCTION: Part of the type VI secretion system (T6SS) specialized secretion system, which delivers several virulence factors in both prokaryotic and eukaryotic cells during infection (By similarity). Forms the spike at the tip of the elongating tube probably formed by hemolysin co-regulated protein/Hcp. Allows the deli... | Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) |
A0A0H3AMJ9 | CHEY3_VIBC3 | MEAILNKNMKILIVDDFSTMRRIVKNLLRDLGFNNTQEADDGLTALPMLKKGDFDFVVTDWNMPGMQGIDLLKNIRADEELKHLPVLMITAEAKREQIIEAAQAGVNGYIVKPFTAATLKEKLDKIFERL | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:24066084}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:24066084}; | archaeal or bacterial-type flagellum-dependent cell motility [GO:0097588]; chemotaxis [GO:0006935]; phosphorelay signal transduction system [GO:0000160] | cytoplasm [GO:0005737] | metal ion binding [GO:0046872] | PF00072; | 3.40.50.2300; | null | PTM: Phosphorylated by CheA-2 and to a lesser extend by VieS. {ECO:0000269|PubMed:18676667}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Acts as a response regulator to control chemotaxis (PubMed:16321945, PubMed:24066084). Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors (PubMed:16321945, PubMed:24066084). Switches the flagellar rotation by binding to the flagellar motor switch protein FliM (PubM... | Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) |
A0A0H3GDH9 | PGDA_LISM4 | MKIRWIRLSLVAILIIAVVFIGVIGFQKYQFSKSRNKVIMQMDRLMKDQDGGNFRRLDKKENGVEIISYIPKTTEKKDNEIIQKEIGKATDAEVKKLNRDKETQGIIFYTYQKHRMAEQAISYKAVQSEYVKEGRTKFVLKDKKDICKNIVTDAETGALLTLGEVLIKSNQTKLNLKTAVEEELIKTGDFSLKDVGNLGKIKSLVKWNQTDFEITNSEIILPVKIPGAPEPKKVKVKLADIASSVNKRYLPSSVKVPEVPKAKTNKRIALTFDDGPSSSVTPGVLDTLKRHNVKATFFVLGSSVIQNPGLVKRELEEGHQ... | 3.5.1.104 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8DP63}; | autolysis [GO:0001896]; carbohydrate metabolic process [GO:0005975]; cell wall modification [GO:0042545]; evasion of host immune response [GO:0042783]; evasion of host innate immune recognition [GO:0141043]; negative regulation of lysozyme activity [GO:1903591] | extracellular region [GO:0005576]; Gram-positive-bacterium-type cell wall [GO:0009275]; plasma membrane [GO:0005886] | chitin deacetylase activity [GO:0004099]; lysozyme inhibitor activity [GO:0060241]; N-acetylglucosamine deacetylase activity [GO:0050119]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270] | PF01522; | 3.20.20.370; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8Y9V5}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8Y9V5, ECO:0000255}; Extracellular side {ECO:0000250|UniProtKB:Q8Y9V5}. Secreted, cell wall {ECO:0000250|UniProtKB:A0A3Q0NBH7}. | CATALYTIC ACTIVITY: Reaction=peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-glucosamine + acetate.; EC=3.5.1.104; Evidence={ECO:0000250|UniProtKB:A0A3Q0NBH7}; | null | null | null | null | FUNCTION: Catalyzes the deacetylation of N-acetylglucosamine (GlcNAc) residues in peptidoglycan (PG). Deacetylates also N-acetylated PG. Does not deacetylate N-acetylmuramic acid (By similarity). Confers host lysozyme resistance. Critical for virulence and escape from innate immune response of the host (PubMed:21768286... | Listeria monocytogenes serotype 1/2a (strain 10403S) |
A0A0H3GGY3 | PGPH_LISM4 | MKLAKKWRDWYIESGKKYLFPLLLVCFAVIAYFLVCQMTKPESYNVKLFQVAEKTIRSPQTVEDTEKTKEERTKASDAVEDVYVYNRETGQNRVALIQSLFAYVNEVNAEAQEKDTKNKEKAKKENKPAPAPTSTEDKLKNLKDKLSSNVSEKITSNISDEVFTTLIEAKSKDFNVMEDVVTTEVEKSMENKIRDENLNSVKIRARDDIELSAIPAYYKNVSKALVSYAIVPNEVYDEEQTDARRKEAAQSVVPVKILQGQVIVQEGQIVDRETYRQLKMLHLLDQKMPVKQYAGFAIFIIALAAILFLYTKKQTQPKAK... | 3.1.4.59 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:25583510}; Note=Able to bind Fe(2+), but has only very weak PDE activity. {ECO:0000269|PubMed:25583510}; | null | plasma membrane [GO:0005886] | cyclic-di-AMP phosphodiesterase activity [GO:0106409]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166] | PF07698;PF07697;PF01966; | 1.10.3210.10; | PgpH phosphodiesterase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=3',3'-c-di-AMP + H2O = 5'-O-phosphonoadenylyl-(3'->5')-adenosine + H(+); Xref=Rhea:RHEA:54420, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:71500, ChEBI:CHEBI:138171; EC=3.1.4.59; Evidence={ECO:0000269|PubMed:25583510}; | null | null | null | null | FUNCTION: A phosphodiesterase (PDE) that hydrolyzes cyclic di-3',5'-adenylate (c-di-AMP); there are at least 2 PDEs for c-di-AMP in this bacteria (this and pdeA), this may be the major PDE for growth in liquid culture (PubMed:25583510). During host infection c-di-AMP is secreted into the host cytoplasm which leads to i... | Listeria monocytogenes serotype 1/2a (strain 10403S) |
A0A0H3JN63 | GATD_STAAN | MHELTIYHFMSDKLNLYSDIGNIIALRQRAKKRNIKVNVVEINETEGITFDECDIFFIGGGSDREQALATKELSKIKTPLKEAIEDGMPGLTICGGYQFLGKKYITPDGTELEGLGILDFYTESKTNRLTGDIVIESDTFGTIVGFENHGGRTYHDFGTLGHVTFGYGNNDEDKKEGIHYKNLLGTYLHGPILPKNYEITDYLLEKACERKGIPFEPKEIDNEAEIQAKQVLIDRANRQKKSR | 3.5.1.2; 6.3.5.13 | null | cell wall organization [GO:0071555]; cobalamin biosynthetic process [GO:0009236]; glutamine metabolic process [GO:0006541]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360] | null | carbon-nitrogen ligase activity on lipid II [GO:0140282]; glutaminase activity [GO:0004359] | PF07685; | 3.40.50.880; | CobB/CobQ family, GatD subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H2O + L-glutamine = ADP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + L-glutamate + phosph... | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02213, ECO:0000269|PubMed:22291598}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-7.8 for isoglutaminyl synthase activity. {ECO:0000269|PubMed:22291598}; | null | FUNCTION: The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide (PubMed:22291598, PubMed:30154570). The GatD subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia. The resulting ammonia molecule is channeled to the active site... | Staphylococcus aureus (strain N315) |
A0A0H3JNB0 | TARP_STAAN | MKKVSVIMPTFNNGEKLHRTISSVLNQTMKSTDYELIIIDDHSNDNGETLNVIKKYKGLVRFKQLKKNSGNASVPRNTGLKMSKAEYVFFLDSDDLLHERALEDLYNYGKENNSDLIIGKYGVEGKGRSVPKAIFEKGNVAKADIIDNSIFYALSVLKMFKKSVIDKNKIKFKTFSKTAEDQLFTIEFLMNSKNYSIKTDYEYYIVVNDFESSNHLSVNKSTGNQYFATINEIYKAIYKSPIYKNQEKRHQLAGKYTTRLLRHGQKKNFANSKMKYEDKIEWLNNFSKTINKVPRDSDKYVTQIFNLKLEAIRQNDLLAV... | 2.4.1.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:30464342}; | cell wall organization [GO:0071555]; teichoic acid biosynthetic process [GO:0019350] | null | glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872] | PF00535; | null | Glycosyltransferase 2 family | null | null | CATALYTIC ACTIVITY: Reaction=4-O-[(D-ribitylphospho)(n)-di{(2R)-glycerylphospho}]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + n UDP-N-acetyl-alpha-D-glucosamine = 4-O-([3-N-acetyl-beta-D-glucosaminyl-1-D-ribitylphospho](n)-di{[2R]-1-glycerylphospho})-N-... | null | PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid biosynthesis. {ECO:0000269|PubMed:30464342}. | null | null | FUNCTION: Attaches beta-O-GlcNAc (beta-O-N-acetyl-D-glucosamine) residues to the C3 position of poly(RboP)-wall teichoic acids (WTAs). Attenuates immunogenicity of WTA and protects S.aureus against adaptative host defenses by allowing bacteria to evade recognition by preexisting anti-S.aureus antibodies. Also protects ... | Staphylococcus aureus (strain N315) |
A0A0H3JPC6 | TARS_STAAM | MMKFSVIVPTYNSEKYITELLNSLAKQDFPKTEFEVVVVDDCSTDQTLQIVEKYRNKLNLKVSQLETNSGGPGKPRNVALKQAEGEFVLFVDSDDYINKETLKDAAAFIDEHHSDVLLIKMKGVNGRGVPQSMFKETAPEVTLLNSRIIYTLSPTKIYRTALLKDNDIYFPEELKSAEDQLFTMKAYLNANRISVLSDKAYYYATKREGEHMSSAYVSPEDFYEVMRLIAVEILNADLEEAHKDQILAEFLNRHFSFSRTNGFSLKVKLEEQPQWINALGDFIQAVPERVDALVMSKLRPLLHYARAKDIDNYRTVEESY... | 2.4.1.355 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:27973583}; Note=Can also use Mg(2+). {ECO:0000269|PubMed:27973583}; | cell wall organization [GO:0071555]; response to antibiotic [GO:0046677]; teichoic acid biosynthetic process [GO:0019350] | null | glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872] | PF00535;PF18674; | null | Glycosyltransferase 2 family | null | null | CATALYTIC ACTIVITY: Reaction=4-O-[(D-ribitylphospho)(n)-di{(2R)-glycerylphospho}]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + n UDP-N-acetyl-alpha-D-glucosamine = 4-O-([2-N-acetyl-beta-D-glucosaminyl-1-D-ribitylphospho](n)-di{[2R]-1-glycerylphospho})-N-... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=45 uM for UDP-GlcNAc {ECO:0000269|PubMed:27973583}; KM=1240 uM for poly(RboP) {ECO:0000269|PubMed:27973583}; | PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid biosynthesis. {ECO:0000269|PubMed:27973583}. | null | null | FUNCTION: Attaches beta-O-GlcNAc (beta-O-N-acetyl-D-glucosamine) residues to the C4 position of poly(RboP)-wall teichoic acids (WTAs). Mediates beta-lactam resistance in methicillin resistant Staphylococcus aureus (MRSA) strains. {ECO:0000269|PubMed:27973583}. | Staphylococcus aureus (strain Mu50 / ATCC 700699) |
A0A0H3JRU9 | PYC_STAAM | MKQIKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYLVGSDLGPAESYLNIERIIDVAKQANVDAIHPGYGFLSENEQFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMIKATSGGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNPKHIEVQVIGDEHGNIVHLFERDCSVQRRHQKVVEVAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLVSGDEFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAAG... | 6.4.1.1 | COFACTOR: Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000269|PubMed:19523900, ECO:0000269|PubMed:23286247}; | gluconeogenesis [GO:0006094]; pyruvate metabolic process [GO:0006090] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; pyruvate carboxylase activity [GO:0004736] | PF02785;PF00289;PF00364;PF02786;PF00682;PF02436; | 2.40.50.100;3.20.20.70;3.30.470.20;3.10.600.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.4.1.1; Evidence={ECO:0000269|PubMed:19523900, ECO:0000... | null | null | null | null | FUNCTION: Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. {ECO:0000269|PubMed:19523900, ECO:0000269|PubMed:23286247}. | Staphylococcus aureus (strain Mu50 / ATCC 700699) |
A0A0H3JUU7 | MURT_STAAN | MRQWTAIHLAKLARKASRAVGKRGTDLPGQIARKVDTDVLRKLAEQVDDIVFISGTNGKTTTSNLIGHTLKANNIQIIHNNEGANMAAGITSAFIMQSTPKTKIAVIEIDEGSIPRVLKEVTPSMMVFTNFFRDQMDRFGEIDIMVNNIAETISNKGIKLLLNADDPFVSRLKIASDTIVYYGMKAHAHEFEQSTMNESRYCPNCGRLLQYDYIHYNQIGHYHCQCGFKREQAKYEISSFDVAPFLYLNINDEKYDMKIAGDFNAYNALAAYTVLRELGLNEQTIKNGFETYTSDNGRMQYFKKERKEAMINLAKNPAGM... | 6.3.5.13 | null | cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360] | null | acid-amino acid ligase activity [GO:0016881]; ATP binding [GO:0005524]; carbon-nitrogen ligase activity on lipid II [GO:0140282]; zinc ion binding [GO:0008270] | PF08245;PF08353; | 3.40.1190.10; | MurCDEF family, MurT subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H2O + L-glutamine = ADP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + L-glutamate + phosph... | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000269|PubMed:22291598}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-7.8 for isoglutaminyl synthase activity. {ECO:0000269|PubMed:22291598}; | null | FUNCTION: The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide (PubMed:22291598, PubMed:30154570). The MurT subunit catalyzes the ATP-dependent amidation of D-glutamate residue of lipid II, converting it to an isoglutamine residue (PubMed:222... | Staphylococcus aureus (strain N315) |
A0A0H3K686 | SPA_STAAE | MKKKNIYSIRKLGVGIASVTLGTLLISGGVTPAANAAQHDEAQQNAFYQVLNMPNLNADQRNGFIQSLKDDPSQSANVLGEAQKLNDSQAPKADAQQNNFNKDQQSAFYEILNMPNLNEAQRNGFIQSLKDDPSQSTNVLGEAKKLNESQAPKADNNFNKEQQNAFYEILNMPNLNEEQRNGFIQSLKDDPSQSANLLSEAKKLNESQAPKADNKFNKEQQNAFYEILHLPNLNEEQRNGFIQSLKDDPSQSANLLAEAKKLNDAQAPKADNKFNKEQQNAFYEILHLPNLTEEQRNGFIQSLKDDPSVSKEILAEAKKL... | null | null | null | extracellular region [GO:0005576] | immunoglobulin binding [GO:0019865] | PF02216;PF00746;PF01476;PF03373;PF04650; | 1.20.5.420;3.10.350.10; | Immunoglobulin-binding protein SpA family | null | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000269|PubMed:17416657, ECO:0000269|PubMed:24434550}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000269|PubMed:17416657, ECO:0000269|PubMed:24434550}. Secreted {ECO:0000269|PubMed:24434550}. Note=Released from th... | null | null | null | null | null | FUNCTION: Plays a role in the inhibition of the host innate and adaptive immune responses. Possesses five immunoglobulin-binding domains that capture both the fragment crystallizable region (Fc region) and the Fab region (part of Ig that identifies antigen) of immunoglobulins (By similarity). In turn, Staphylococcus au... | Staphylococcus aureus (strain Newman) |
A0A0H3K6J4 | LYTM_STAAE | MKKLTAAAIATMGFATFTMAHQADAAETTNTQQAHTQMSTQSQDVSYGTYYTIDSNGDYHHTPDGNWNQAMFDNKEYSYTFVDAQGHTHYFYNCYPKNANANGSGQTYVNPATAGDNNDYTASQSQQHINQYGYQSNVGPDASYYSHSNNNQAYNSHDGNGKVNYPNGTSNQNGGSASKATASGHAKDASWLTSRKQLQPYGQYHGGGAHYGVDYAMPENSPVYSLTDGTVVQAGWSNYGGGNQVTIKEANSNNYQWYMHNNRLTVSAGDKVKAGDQIAYSGSTGNSTAPHVHFQRMSGGIGNQYAVDPTSYLQSR | 3.4.24.75 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O33599}; | cell wall organization [GO:0071555]; proteolysis [GO:0006508]; septum digestion after cytokinesis [GO:0000920] | cell division site [GO:0032153]; cell outer membrane [GO:0009279]; extracellular region [GO:0005576] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF01551; | 2.40.50.290;2.70.70.10; | Peptidase M23B family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O33599}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of the -Gly-|-Gly- bond in the pentaglycine inter-peptide link joining staphylococcal cell wall peptidoglycans.; EC=3.4.24.75; Evidence={ECO:0000305|PubMed:24434550}; | null | null | null | null | FUNCTION: Peptidoglycan hydrolase (autolysin) specifically acting on polyglycine interpeptide bridges of the cell wall peptidoglycan (By similarity). Releases SpA, an immunologically active peptide, from the cell wall (PubMed:24434550). {ECO:0000250|UniProtKB:O33599, ECO:0000269|PubMed:24434550}. | Staphylococcus aureus (strain Newman) |
A0A0H3KB22 | QUEE_BURM1 | MTYAVKEIFYTLQGEGANAGRPAVFCRFAGCNLWSGREEDRAQAVCRFCDTDFVGTDGENGGKFKDADALVATIAGLWPAGEAHRFVVCTGGEPMLQLDQPLVDALHAAGFGIAIETNGSLPVLESIDWICVSPKADAPLVVTKGNELKVVIPQDNQRLADYAKLDFEYFLVQPMDGPSRDLNTKLAIDWCKRHPQWRLSMQTHKYLNIP | 4.3.99.3 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:24362703}; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:24362703}; COFACT... | queuosine biosynthetic process [GO:0008616] | null | 4 iron, 4 sulfur cluster binding [GO:0051539]; carbon-nitrogen lyase activity [GO:0016840]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; S-adenosyl-L-methionine binding [GO:1904047] | null | 3.20.20.70; | Radical SAM superfamily, 7-carboxy-7-deazaguanine synthase family | null | null | CATALYTIC ACTIVITY: Reaction=6-carboxy-5,6,7,8-tetrahydropterin + H(+) = 7-carboxy-7-deazaguanine + NH4(+); Xref=Rhea:RHEA:27974, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:61032, ChEBI:CHEBI:61036; EC=4.3.99.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:24362703}; | null | PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000305|PubMed:24362703}. | null | null | FUNCTION: Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:24362703}. | Burkholderia multivorans (strain ATCC 17616 / 249) |
A0A0H3LKL4 | 6HN3M_BORBR | MQGKPRIAVIGAGLGGTAGAALMARAGFNVRLYEQAPAFSRLGAGIHLGPNVMKIMRRIGIEDELNRQGSHPDYWYSRDWQSGAELARIPLGDYAVSHYGATYLTVHRGDFHALMTAALPAGLLQFNKRLTRVDEDDDVVRLHFADGSVEEAEIVIGADGVNSRLREHLLGAELPKYTGYVAHRAVFPTPLDSGSLPFDMCVKWWSDDRHMMVYFVTGKRDEIYYVTGVPEQQWDMGKSWVPSSKAEMRAAFAGWHPTVQALIEATPEVSKWPLLERDPLPLWSRGRIVLLGDACHPMKPHMAQGAAMAIEDAAMLTRIF... | 1.14.13.114 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:30810301}; Note=Binds 1 FAD molecule per subunit. {ECO:0000250|UniProtKB:Q88FY2}; | aromatic compound catabolic process [GO:0019439] | null | 6-hydroxynicotinate 3-monooxygenase activity [GO:0043731]; FAD binding [GO:0071949] | PF01494; | 3.50.50.60; | 6-hydroxynicotinate 3-monooxygenase family | null | null | CATALYTIC ACTIVITY: Reaction=6-hydroxynicotinate + 2 H(+) + NADH + O2 = 2,5-dihydroxypyridine + CO2 + H2O + NAD(+); Xref=Rhea:RHEA:27333, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16364, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57664, ChEBI:CHEBI:57945; EC=1.14.13.114; Evidence={ECO:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=85 uM for 6-hydroxynicotinate (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:27218267}; KM=6 uM for NADH (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:27218267}; KM=118 uM for 6-hydroxynicotinate (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubM... | PATHWAY: Cofactor degradation; nicotinate degradation. {ECO:0000305|PubMed:27218267, ECO:0000305|PubMed:30810301}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 7-8. {ECO:0000269|PubMed:27218267}; | null | FUNCTION: Flavin-dependent monooxygenase (FMO) that catalyzes the decarboxylative hydroxylation of 6-hydroxynicotinic acid (6-HNA) to 2,5-dihydroxypyridine (2,5-DHP) with concomitant oxidation of NADH, a step in the aerobic nicotinate degradation pathway (PubMed:27218267, PubMed:30810301). Is also active on the non-nat... | Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus) |
A0A0H3LM39 | ZIP_BORBR | MNQPSSLAADLRGAWHAQAQSHPLITLGLAASAAGVVLLLVAGIVNALTGENRVHVGYAVLGGAAGFAATALGALMALGLRAISARTQDAMLGFAAGMMLAASAFSLILPGLDAAGTIVGPGPAAAAVVALGLGLGVLLMLGLDYFTPHEHERTGHQGPEAARVNRVWLFVLTIILHNLPEGMAIGVSFATGDLRIGLPLTSAIAIQDVPEGLAVALALRAVGLPIGRAVLVAVASGLMEPLGALVGVGISSGFALAYPISMGLAAGAMIFVVSHEVIPETHRNGHETTATVGLMAGFALMMFLDTALG | null | null | null | plasma membrane [GO:0005886] | zinc ion transmembrane transporter activity [GO:0005385] | PF02535; | null | ZIP transporter (TC 2.A.5) family | null | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351, ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:20876577}; CATALYTIC ACTIVITY: Reaction=Cd(2+)(in) = Cd(2+)(out); Xref=Rhea:RHEA:28707, ChEBI:CHEBI:48775; Evidence={ECO:0000269|PubMed:20876577}; | null | null | null | null | FUNCTION: Selective electrodiffusional channel that mediates the uptake of Zn(2+). Exploits in vivo zinc concentration gradients (maintained by cellular zinc homeostasis) to passively move zinc ions into the cytoplasm. ZIPB-mediated zinc flux is dependent upon pH, but independent of the proton motive force. Is also abl... | Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus) |
A0A0H3M5A8 | PPMNT_MYCBP | MKLGAWVAAQLPTTRTAVRTRLTRLVVSIVAGLLLYASFPPRNCWWAAVVALALLAWVLTHRATTPVGGLGYGLLFGLVFYVSLLPWIGELVGPGPWLALATTCALFPGIFGLFAVVVRLLPGWPIWFAVGWAAQEWLKSILPFGGFPWGSVAFGQAEGPLLPLVQLGGVALLSTGVALVGCGLTAIALEIEKWWRTGGQGDAPPAVVLPAACICLVLFAAIVVWPQVRHAGSGSGGEPTVTVAVVQGNVPRLGLDFNAQRRAVLDNHVEETLRLAADVHAGLAQQPQFVIWPENSSDIDPFVNPDAGQRISAAAEAIGA... | 2.3.1.269; 2.4.1.-; 2.4.1.83 | null | lipoprotein biosynthetic process [GO:0042158] | plasma membrane [GO:0005886] | dolichyl-phosphate beta-D-mannosyltransferase activity [GO:0004582]; hydrolase activity [GO:0016787]; N-acyltransferase activity [GO:0016410] | PF00795;PF00535;PF20154; | 3.60.110.10; | CN hydrolase family, Apolipoprotein N-acyltransferase subfamily; Glycosyltransferase 2 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | 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:136... | null | PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl transfer). | null | null | FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. {ECO:0000269|PubMed:24093492}.; FUNCTION: Transfers mannose from GDP-mannose to lipid acceptors to form polyprenol monophosphomannose (PPM). PMM is an alkai-stable sugar dono... | Mycobacterium bovis (strain BCG / Pasteur 1173P2) |
A0A0H3MDW1 | CHXR_CHLT2 | MAGPKHVLLVSEHWDLFFQTKELLNPEEYRCTIGQQYKQELSADLVVCEYSLLPREIRSPKSLEGSFVLVLLDFFDEETSVDLLDRGFWYLIRPITPRILKSAISLFLSQHSLHSVPESIRFGPNVFYVLKLTVETPEGSVHLTPSESGILKRLLINKGQLCLRKHLLEEIKNHAKAIVARNVDVHIASLRKKLGAYGSRIVTLRGVGYLFSDDGDKKFSQQDTKLS | null | null | phosphorelay signal transduction system [GO:0000160]; positive regulation of DNA-templated transcription [GO:0045893] | null | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976] | PF00486; | 3.40.50.2300;1.10.10.10; | null | null | null | null | null | null | null | null | FUNCTION: May be a global positive regulator of transcription (PubMed:21057008). Binds a cis-acting element of its own promoter DNA sequence and is hence probably also involved in its own transcription activation (PubMed:21057008, PubMed:21775428, PubMed:24646934). The recognition sequence is 5'-WHGAWNH-N(3-5)-WHGAWNH-... | Chlamydia trachomatis serovar L2 (strain ATCC VR-902B / DSM 19102 / 434/Bu) |
A0A0H3NK84 | SSEK1_SALTS | MIPPLNRYVPALSKNELVKTVTNRDIQFTSFNGKDYPLCFLDEKTPLLFQWFERNPARFGKNDIPIINTEKNPYLNNIIKAATIEKERLIGIFVDGDFFPGQKDAFSKLEYDYENIKVIYRNDIDFSMYDKKLSEIYMENISKQESMPEEKRDCHLLQLLKKELSDIQEGNDSLIKSYLLDKGHGWFDFYRNMAMLKAGQLFLEADKVGCYDLSTNSGCIYLDADMIITEKLGGIYIPDGIAVHVERIDGRASMENGIIAVDRNNHPALLAGLEIMHTKFDADPYSDGVCNGIRKHFNYSLNEDYNSFCDFIEFKHDNII... | 2.4.1.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:30327479}; | null | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell cytosol [GO:0044164] | manganese ion binding [GO:0030145]; protein-arginine N-acetylglucosaminyltransferase activity [GO:0106362]; toxin activity [GO:0090729] | null | null | Glycosyltransferase NleB family | PTM: Auto-glycosylated: arginine GlcNAcylation is required for activity toward death domain-containing host target proteins. {ECO:0000269|PubMed:32432056}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9L9J3}. Host cytoplasm, host cytosol {ECO:0000305|PubMed:32432056}. Note=Secreted via type III secretion systems 1 and 2 (SPI-1 and SPI-2 T3SS). {ECO:0000250|UniProtKB:Q9L9J3}. | CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(omega)-(N-acetyl-beta-D-glucosaminyl)-L-arginyl-[protein] + UDP; Xref=Rhea:RHEA:66632, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:17079, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:167322... | null | null | null | null | FUNCTION: Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling, apoptosis and necroptosis (PubMed:30327479, PubMed:32766249). Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the... | Salmonella typhimurium (strain SL1344) |
A0A0H3PEK7 | TLYA_CAMJJ | MRFDFFVSKRLNISRNKALELIENEEVLLNGKSFKASFDVKNFLENLKKTQDLNPEDILLTDGLKLDLLSEIYVSRAALKLKNFLEENGIEIKHKNCLDIGSSTGGFVQILLENQALKITALDVGNNQLHLSLRTNEKIILHENTDLRTFKSEEKFELITCDVSFISLINLLYYIDNLALKEIILLFKPQFEVGKNIKRDKKGVLKDDKAILKARMDFEKACAKLGWLLKNTQKSSIKGKEGNVEYFYYYIKN | 2.1.1.226 | null | cell motility [GO:0048870]; cellular response to antibiotic [GO:0071236]; cytosolic ribosome assembly [GO:0042256]; rRNA 2'-O-methylation [GO:0000451]; viral process [GO:0016032] | null | RNA binding [GO:0003723]; rRNA methyltransferase activity [GO:0008649] | PF01728; | 3.10.290.10;3.40.50.150; | TlyA family | null | null | CATALYTIC ACTIVITY: Reaction=cytidine(1920) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1920) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43200, Rhea:RHEA-COMP:10403, Rhea:RHEA-COMP:10404, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; E... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.8 uM for 50S ribosomal subunit (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:24796671}; KM=5.8 uM for S-adenosyl-L-methionine (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:24796671}; Note=kcat is 0.0048 min(-1) for 50S ribosomal subunit. kcat is... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: High methylation activity of the 50S ribosomal subunit at 37 degrees Celsius. Loss of activity at 42 degrees Celsius. {ECO:0000269|PubMed:24796671}; | FUNCTION: Catalyzes the 2'-O-methylation at nucleotide C1920 in 23S rRNA (PubMed:24796671, PubMed:29404277). Enhances motility (PubMed:24796671, PubMed:29404277, PubMed:32134554). Enhances biofilm formation (PubMed:29404277, PubMed:32134554). Involved in the assembly of 70S ribosomes (PubMed:24796671). Involved in viru... | Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) |
A0A0H3PJK4 | DLP2_CAMJJ | MQINLLNDFIKAYENTYSVSFDDSFKGRIQELCKELNEPFMHASYALENELKELVFSLDKNVNIAIIGQFSSGKSSLLNLILGRDCLPTGVVPVTFKPTFLRYAKEYFLRVEFEDGSDIITNIEKLAFYTDQRNEVKQAKSLHIFAPIPLLEKITLVDTPGLNANENDTLTTLDELKNIHGAIWLSLIDNAGKKSEEDAIKANLELLGENSICVLNQKDKLSAEELDNVLNYAKSVFLKYFNELIAISCKEAKDEQSYEKSNFQSLLDFLTQLDTTVLKEKFVKRKILNLCEILEDENQLFVGIFDRLLNQFQSYEKHLL... | null | null | thylakoid membrane organization [GO:0010027] | cytosol [GO:0005829] | hydrolase activity [GO:0016787] | PF00350; | 3.40.50.300; | TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30131557}. | 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:30131557}; | null | null | null | null | FUNCTION: The heterotetrameric DLP1(2)-DLP2(2) complex tethers liposomes and may mediate their fusion. Initial binding is probably mediated by DLP1, while DLP2 couples DLP1 subunits and increases the effective reach of the complex up to 45 nm. The role of the nucleotide is unknown. This subunit alone very weakly binds ... | Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) |
A0A0H3PJL7 | DLP1_CAMJJ | MKELFQKIWQNELQFLNFDAKFQDKSKLDTAECAIILSVNKDNYERYFLLKEFQELCKKIDLRVDIFSMQNAQICILNLFKSGFISKQDLLKALKILEKISKNTEIFDFILQEKVQSIDQKALFQNDFKELNTINLELQKLSFDENLKSRLQKTLEKFQNLEFNIAITGVMNAGKSSLLNALLKEDFLGVSNIPETANLTVLSYGKSEEAKIYFWDKKEWQNILESSHFNADLKEFIDKLDKSVNIEDFIKDKPLIQNIALCELKNFSSAKNKISALIKKIEIKSHLEFLKNNISIVDTPGLDDVVVQREIVTNEYLRES... | null | null | mitochondrial fusion [GO:0008053] | cytosol [GO:0005829] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00350; | 3.40.50.300; | TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30131557}. | 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:30131557}; | null | null | null | null | FUNCTION: The heterotetrameric DLP1(2)-DLP2(2) complex tethers liposomes and may mediate their fusion. Initial binding is probably mediated by DLP1, while DLP2 couples DLP1 subunits and increases the effective reach of the complex up to 45 nm. The role of the nucleotide is unknown. This subunit alone weakly binds to li... | Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) |
A0A0H5BMX5 | TCEB1_TULGE | MSIVSFCSSLPAGPHGFKHGRGTRDMVHMPCIVRRTARSPAQACRLLRWNKYHCAAVPTNSSLSPSPTPLDVEIELDLEPFLIKYKSGRIERLGRFGDRTDYVEASLDPATEVTSRDAITDTGVPVRIYLPKVDDSPPNSLRVLVYFHGGAFLVEDSASPPYHNYLNNLASKANILIVSVNYRLAPEYPLPVAYDDCMEALNWVNKHSDGTGQEDWINKHGDFDHLFISGDSAGGNITHNIAMSTDAPKNIEGIALVHPYFFGKVALETELQDPTNLLLHRKLWSFITPESEGLDDPRVNPLGPTAPSLEKIKCKRAVVF... | 4.2.99.23 | null | defense response [GO:0006952] | amyloplast [GO:0009501] | carboxylic ester hydrolase activity [GO:0052689]; lyase activity [GO:0016829] | PF07859; | 3.40.50.1820; | AB hydrolase superfamily | PTM: Not glycosylated. {ECO:0000269|PubMed:25997073}. | SUBCELLULAR LOCATION: Plastid {ECO:0000269|PubMed:25997073}. Plastid, amyloplast {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=6-tuliposide B = D-glucose + tulipalin B; Xref=Rhea:RHEA:38655, ChEBI:CHEBI:4167, ChEBI:CHEBI:87123, ChEBI:CHEBI:87124; EC=4.2.99.23; Evidence={ECO:0000269|PubMed:25997073}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3 mM for 6-tuliposide A {ECO:0000269|PubMed:25997073}; KM=6.8 mM for 6-tuliposide B {ECO:0000269|PubMed:25997073}; Note=kcat is 8.7 sec(-1) with 6-tuliposide A as substrate. kcat is 2000 sec(-1) with 6-tuliposide B as substrate. {ECO:0000269|PubMed:25997073}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:25997073}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-40 degrees Celsius. {ECO:0000269|PubMed:25997073}; | FUNCTION: Lactone-forming carboxylesterase, specifically catalyzing intramolecular transesterification, but not hydrolysis. Involved in the biosynthesis of tulipalins, defensive chemicals that show antimicrobial activities against a broad range of strains of bacteria and fungi. Substrates are 6-tuliposide B > 6-tulipos... | Tulipa gesneriana (Garden tulip) |
A0A0J5ZXG5 | PYCC_BURCE | MALADDLKKWVGETFTGKWEVQETTSVPNPEDLRLNSNHAKDLKAATVLYADLDGSTDMVNTKKWQFSAQIYKTFLKCASDIIRDEGGNITAYDGDRVMAVFTGNSKNTSAARCALKINSAVLDIIQPAIAKKWQTDFVLRHVVGIDTSQLRTARIGIRGDNDLVWIGRAANYAAKLTNLAGKPTRITADVYNKLADKLKYANGVDMWAPEHWDDMGIWTYTSTWKWTV | 4.6.1.26 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:34644530}; Note=Slightly more active with Mn(2+) than with Mg(2+). {ECO:0000269|PubMed:34644530}; | cyclic nucleotide biosynthetic process [GO:0009190]; defense response to virus [GO:0051607]; intracellular signal transduction [GO:0035556] | cytoplasm [GO:0005737] | adenylate cyclase activity [GO:0004016]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166] | PF00211; | 3.30.70.1230; | Adenylyl cyclase class-4/guanylyl cyclase family, Pyrimidine cyclase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=UTP = 3',5'-cyclic UMP + diphosphate; Xref=Rhea:RHEA:69603, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:184387; EC=4.6.1.26; Evidence={ECO:0000269|PubMed:34644530}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-9.5. {ECO:0000269|PubMed:34644530}; | null | FUNCTION: Pycsar (pyrimidine cyclase system for antiphage resistance) provides immunity against bacteriophage. The pyrimidine cyclase (PycC) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate the adjacent effector, leading to bacterial cell de... | Burkholderia cepacia (Pseudomonas cepacia) |
A0A0J9SZQ5 | HXT1_PLAV1 | MKKSSKEISSSQSLKNGGSDHFFNTSLMYVLAACLASFIFGYQVSVLNTIKNFIVIEFGWCTGNKVECDDSTLKSSFLLASVFIGAVVGSGFSGYLVQHGRRFSLLVIYNFFILVSILTSITHHFHTILFSRLLSGFGIGLITVSVPMYISEMTHKDKKGAYGVLHQLFITFGIFVAVLLGMAMGEAPDAKSVDALGEFQKIWWRLMFFFPCLISILGIVLLTFFYKEETPYYLFENGKIEESKKILKKIYGTDNVDEPLKAIKDAVEQNEAAKKNSISLMRAMQIPSYRNVILLGCILSGLQQFTGINVLVSNSNELYK... | null | null | dehydroascorbic acid transport [GO:0070837]; glucose import [GO:0046323] | membrane [GO:0016020] | D-glucose transmembrane transporter activity [GO:0055056] | PF00083; | 1.20.1250.20; | Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q7KWJ5}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376, ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:12792024, ECO:0000269|PubMed:15107012}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60377; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=D-fructose(out) = D-fructose(in); Xre... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.85 mM for D-glucose {ECO:0000269|PubMed:12792024}; KM=0.77 mM for D-glucose {ECO:0000269|PubMed:15107012}; | null | null | null | FUNCTION: Sodium-independent facilitative hexose transporter (By similarity). Can transport D-glucose and D-fructose (PubMed:12792024, PubMed:15107012). Can transport D-mannose, D-galactose, D-xylose and D-glucosamine (By similarity). {ECO:0000250|UniProtKB:Q700M0, ECO:0000250|UniProtKB:Q7KWJ5, ECO:0000269|PubMed:12792... | Plasmodium vivax (strain Brazil I) |
A0A0J9UVG7 | SIR5_FUSO4 | MRLLRPTPRLSSIFSSKTATSNLRFFTAMAPHNDVGAFHEALRSSKRILALCGAGLSASSGLPTFRGAGGLWRNHDATSLATLSAFKNDPGLVWLFYNYRRHMCLRAEPNPAHYALAALAEKNKDFLCLTQNVDNLSQQAGHPQDQLRTLHGSLFDIKCTNCDWIQRGNYDDPFCPALAPASVDVEPGKPFPLLDASLPLDPISPDDIPKCPQCKIGFQRPGVVWFGENLDEVMMMGITNWLLEDKVDLMLVIGTSAQVYPAAGYIDKAKRKGARIAVINPEAENEEEMYKVKPGDFAFGKDAAEYLPLLLEPVIGKLET... | 2.3.1.-; 2.3.1.286 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9NXA8}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9NXA8}; | negative regulation of cellular respiration [GO:1901856] | chromosome [GO:0005694]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | metal ion binding [GO:0046872]; NAD+ binding [GO:0070403]; NAD-dependent histone deacetylase activity [GO:0017136]; NAD-dependent histone decrotonylase activity [GO:0160012]; NAD-dependent protein decrotonylase activity [GO:0160011]; protein-malonyllysine demalonylase activity [GO:0036054]; protein-succinyllysine desuc... | PF02146; | 3.30.1600.10;3.40.50.1220; | Sirtuin family, Class I subfamily | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:34927582}. Cytoplasm, cytosol {ECO:0000269|PubMed:34927582}. Nucleus {ECO:0000269|PubMed:34927582}. Chromosome {ECO:0000269|PubMed:34927582}. | 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=... | null | null | null | null | FUNCTION: NAD-dependent protein-lysine deacylase that decrotonylates the PDC (pyruvate dehydrogenase complex) subunit LAT1 at 'Lys-148' to inhibit PDC activity and consequently ATP production (PubMed:34927582). Also decrotonylates histone H3 crotonylated at 'Lys-18' (H3K18cr), to repress the expression of genes involve... | Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936) (Fusarium vascular wilt of tomato) |
A0A0J9X285 | HMPK_ACIB6 | MRPTVLCFSGLDPSGGAGLQADIEAIGQSGAHAAIACTALTIQNSQQVFGFEATSKELLLAQANAVVGDLPIKCVKSGMLGTTDNIAALAEFLRAHPDYQYVLDPVLVANSGGSLGDQATLVKAFVELIPLATLITPNTVELRALTGVTDLDQATQKLFEMGAKAVLVKGGHEDTPDFIKNSLYIDGELAASSTCPRLEGEYHGSGCSLASFIAGRLALGDSLKIAVQHAETWLFGVLKNAETPVLNGQKIPKRF | 2.7.1.49 | null | thiamine biosynthetic process [GO:0009228]; thiamine diphosphate biosynthetic process [GO:0009229] | cytosol [GO:0005829] | hydroxymethylpyrimidine kinase activity [GO:0008902]; phosphomethylpyrimidine kinase activity [GO:0008972] | PF08543; | 3.40.1190.20; | ThiD family | PTM: Crystals show a disulfide bond between Cys-195 and Cys-207 (PubMed:38306231). This disulfide is possibly an artifact of the purification and crystallization conditions (PubMed:38306231). However, as it is adjacent to the conserved GSGC of the oxyanion hole, this disulfide may help to orient the backbone amides tow... | null | CATALYTIC ACTIVITY: Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+); Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892, ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.1.49; Evidence={ECO:0000269|PubMed:38306231}; Physiol... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=64 uM for HMP {ECO:0000269|PubMed:38306231}; Note=kcat is 0.19 sec(-1) with HMP as substrate. {ECO:0000269|PubMed:38306231}; | PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine (HMP) to hydroxymethylpyrimidine phosphate (HMP-P) (PubMed:38306231). Unlike other HMPKs, it cannot catalyze the phosphorylation of HMP-P to generate the diphosphate HMP-PP (PubMed:38306231). Shows no activity with pyridoxal, pyridoxamine or pyridoxine ... | Acinetobacter baumannii (strain IS-123) |
A0A0K0JFP3 | HXK_BRUMA | MLGLLTITSVFRNWRNSLQRKEDYDECHMRGINNENEISGKSEKNFKLDEPPISLETVMAEFKLSNETLRRMMAHMSRNMDKGLEGGPENSTISMLPSFVPELPNGTEEGRFIAMDLGGTNLRVMLMDIKPGEELKTEQFNTRIPNWAMRGTGEQLFDYITKCLAEFLIEKGIENDGLPVGFTFSYPCDQKSLRSATLLRWTKGFETTGVVGEDVVELLEQSIARRGDIKVEVVALINDTVGTMVAAAHESGGECHIGVIIATGTNASYMEDTSKIKYGLSKAIAAYNYPEMIIDTEWGGFGDRSEADYILTQYDKIVDS... | 2.7.1.1 | null | glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; hexose metabolic process [GO:0019318]; intracellular glucose homeostasis [GO:0001678] | cytosol [GO:0005829]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; fructokinase activity [GO:0008865]; glucokinase activity [GO:0004340]; glucose binding [GO:0005536]; mannokinase activity [GO:0019158] | PF00349;PF03727; | 3.30.420.40;3.40.367.20; | Hexokinase family | null | null | CATALYTIC ACTIVITY: Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU01084, ECO:0000269|PubMed:18499511}; PhysiologicalDirection=left... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.035 mM for glucose {ECO:0000269|PubMed:18499511}; KM=75 mM for fructose {ECO:0000269|PubMed:18499511}; KM=1.09 mM for ATP {ECO:0000269|PubMed:18499511}; | PATHWAY: Carbohydrate metabolism; hexose metabolism. {ECO:0000269|PubMed:18499511}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4. {ECO:0000269|PubMed:18499511}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.4. {ECO:0000269|PubMed:18499511}; | null | FUNCTION: Active against glucose, fructose, mannose, maltose and galactose. {ECO:0000269|PubMed:18499511}. | Brugia malayi (Filarial nematode worm) |
A0A0K0MJN3 | FABP4_PYGPA | MCDQFVGTWKFLSSENFEDYMKELGVGFATRKMAGVAKPNVTISINGDVITIKTESTFKNTEVSFRLGEEFDETTADDRKTKNVITLDNGILNQVQKWDGKETVIKRKVMDGNLVVECTMNTVTSKRVYERA | null | null | cellular response to linoleic acid [GO:0071399]; long-chain fatty acid transport [GO:0015909] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | linoleic acid binding [GO:0070539]; long-chain fatty acid transporter activity [GO:0005324]; oleic acid binding [GO:0070538]; stearic acid binding [GO:0070540] | PF00061; | 2.40.128.20; | Calycin superfamily, Fatty-acid binding protein (FABP) family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04117}. Nucleus {ECO:0000250|UniProtKB:P04117}. Note=Depending on the nature of the ligand, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus. Subject to constitutive nuclear export. {ECO:0000250|UniProtKB:P... | null | null | null | null | null | FUNCTION: Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus (By similarity). Has the highest binding affinity for linoleic acid and decreasing relative affinity for eicosapentaenoic acid... | Pygoscelis papua (Gentoo penguin) |
A0A0K0PVW1 | UGT10_PANGI | MKSELIFLPVPAFGHLVGMVEMAKLFISRHENLSVTVLISKFFIDTGIDNYNKSLLAKPTPRLTIINLPEIDPQKYLLKPRCAIFPSLIENQKTHVRDVMSRMTQSESTRVVGLLADILFVDIFDIADEFNVPTYVYSPAGAGFLGLAFHLQTLNDDKKQDVTEFRNSDTELLVPSFANPVPAEFLPSIFLEKDGRHDVLLSLYWRCREAKGIIVNTFEELEPYAINSLRMDSMIPPIYPVGPILNLNGEGQNSDEAAVILGWLDDQPPSSVVFLCFGSFGSFPENQVKEIAMGLERSGHRFLWSLRPCISEGETTLQLK... | 2.4.1.367 | null | response to molecule of fungal origin [GO:0002238]; terpenoid biosynthetic process [GO:0016114] | null | hydrolase activity [GO:0016787]; UDP-glycosyltransferase activity [GO:0008194] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=(20S)-protopanaxadiol + UDP-alpha-D-glucose = (20S)-ginsenoside C-K + H(+) + UDP; Xref=Rhea:RHEA:57976, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:75950, ChEBI:CHEBI:77146; Evidence={ECO:0000269|PubMed:26032089}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Component of the dammarane-type triterpene saponins (e.g. PPT-type ginsenosides or panaxosides) biosynthetic pathway (PubMed:26032089, PubMed:27746309, PubMed:29378087). Glycosyltransferase that catalyzes the biosynthesis of ginsenoside Rh1 from protopanaxatriol (PPT) and the conversion of ginsenoside F1 to g... | Panax ginseng (Korean ginseng) |
A0A0K1YW63 | SECP_APICE | MRFQVYILHLCFFILVVLTYLSQGQSYTTTTTTSTTEQPTFLQKIHETFKKVKENAKIHNLYIFDPPTWIYTTTTEKPVESTENFDITNRQLITVPVRCPPNYDFIKGRCREKIP | null | null | antibacterial innate immune response [GO:0140367]; antifungal innate immune response [GO:0061760]; defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]; negative regu... | extracellular region [GO:0005576] | serine-type endopeptidase inhibitor activity [GO:0004867] | PF17521; | null | Secapin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:27208884}. | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Antibacterial activity against P.aeruginosa is retained between 25 and 90 degrees Celsius. {ECO:0000269|Ref.2}; | FUNCTION: Serine protease inhibitor which exhibits antifibrinolytic, antielastolytic and antimicrobial activities (PubMed:27208884). Displays antimicrobial activity against bacteria and fungi (PubMed:27208884). Likely functions in the innate immune response to microbial infection and possibly in the venom, as an antifi... | Apis cerana (Indian honeybee) |
A0A0K2JL82 | CRED_STRCM | MTRPPAPPPGAPGADELLDCGLLSPVRAGTPVEALVCDSAWLQAMLDAEAALTRAQARTGFLPAAAAEAITAAARADRIDLLAVARGARETANPVVGLVAALTAAVRRDDPAAAEYVHRGSTSQDVLDTGAMLVARRALRLIGDDLDRAADALAALAADHRDTPMAGRTLALHAVPTTFGLKAAGWLELVSEAAGRVARLRDGLPFSLGGAAGTLAGYFGDRTDRGDPAVLLDRLLDAYAAETGLARPVLPWHVLRTPVADLAAVLAFTAGALGKIAVDVQSLARTEVAEVAEPAVEGRGASSAMPHKRNPVLSTLIRSA... | 4.3.99.5 | null | 3,4-dihydroxybenzoate catabolic process [GO:0019619]; antibiotic biosynthetic process [GO:0017000] | null | lyase activity [GO:0016829] | PF10397;PF00206; | 1.10.40.30;1.20.200.10;1.10.275.10; | Class-II fumarase/aspartase family | null | null | CATALYTIC ACTIVITY: Reaction=2-nitrobutanedioate = fumarate + H(+) + nitrite; Xref=Rhea:RHEA:69044, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:29806, ChEBI:CHEBI:180682; EC=4.3.99.5; Evidence={ECO:0000269|PubMed:26689788, ECO:0000269|PubMed:29505698}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69045; E... | null | PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:26278892, ECO:0000305|PubMed:26689788}. | null | null | FUNCTION: Part of a gene cluster involved in the biosynthesis of cremeomycin, a light-sensitive o-diazoquinone with antibacterial and antiproliferative effects (PubMed:26278892, PubMed:26689788). Catalyzes the formation of nitrous acid from nitrosuccinic acid (2-nitrobutanedioate) by elimination of its nitro group (Pub... | Streptomyces cremeus |
A0A0K2S4Q6 | CD3CH_HUMAN | MTQRAGAAMLPSALLLLCVPGCLTVSGPSTVMGAVGESLSVQCRYEEKYKTFNKYWCRQPCLPIWHEMVETGGSEGVVRSDQVIITDHPGDLTFTVTLENLTADDAGKYRCGIATILQEDGLSGFLPDPFFQVQVLVSSASSTENSVKTPASPTRPSQCQGSLPSSTCFLLLPLLKVPLLLSILGAILWVNRPWRTPWTES | null | null | neutrophil chemotaxis [GO:0030593] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | transmembrane signaling receptor activity [GO:0004888] | PF07686; | 2.60.40.10; | CD300 family | null | SUBCELLULAR LOCATION: [Isoform 1]: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:26221034}. | null | null | null | null | null | FUNCTION: May play an important role in innate immunity by mediating a signal for the production of a neutrophil chemoattractant. {ECO:0000269|PubMed:26221034}. | Homo sapiens (Human) |
A0A0K3AUE4 | SEA2_CAEEL | MGREYKFTGIAAKLNPLNCRLKLEIAEDLDERVPTTSTSCSVASVAAATATINTTAPTVLTKSELQKTLQKTSSSFSSSLATTTTTSSHLNAPVESMEGHSSLASYSHHHPSSSHHHHPGQQQSSSSSSSSHLQDFQSPPSASHPYYHQQQPQHQHQQAQQYGQATGSTNGGGQQQMTSMYGGNDYDQHQLHHQNQQHQASTSTQQFHHPQRPPPPQYDQPSSSTGSSLPPLHTVRYEQLPPPPSNQRTPTQQLQYPVKVVEAGGQAYAQQVQQAQQSNRSGAAGVNSALQPKPLPPLSSITSISSSAAGSSISAPSTSQ... | null | null | cell differentiation [GO:0030154]; determination of adult lifespan [GO:0008340]; negative regulation of gene expression [GO:0010629]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of development, heterochronic [GO:0040034]; regulation of translation [GO:0006417]; response to heat [G... | cytoplasm [GO:0005737]; mediator complex [GO:0016592]; nucleus [GO:0005634]; PcG protein complex [GO:0031519]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; single-stranded RNA binding [GO:0003727]; transcription coactivator activity [... | PF00096; | 3.30.160.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21471153, ECO:0000269|PubMed:23666922}. Cytoplasm {ECO:0000269|PubMed:21471153}. Note=In embryos, diffusely accumulates in the nucleus at the 20- to 30-cell stage, but nuclear localization decreases after the 200-cell stage (PubMed:23666922). Diffusely localized in the ... | null | null | null | null | null | FUNCTION: RNA-binding protein, which regulates the expression of proteins required to control developmental timing of events during the L2 to L3 larval stage switch (PubMed:21471153). Binds to the 3'UTR of the transcript of the heterochronic protein lin-28 to post-transcriptionally negatively regulate its expression in... | Caenorhabditis elegans |
A0A0K3AUJ9 | PRDX_CAEEL | MSLAPKMSKAFIGKPAPQFKTQAVVDGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAWINQPRKHGGLGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQFVEKHGEVCPAGWTPGSDTIKPGVKESQEYFKKH | 1.11.1.24 | null | cell redox homeostasis [GO:0045454]; cellular response to hydrogen peroxide [GO:0070301]; determination of adult lifespan [GO:0008340]; heat acclimation [GO:0010286]; hydrogen peroxide catabolic process [GO:0042744]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of brood si... | cytoplasm [GO:0005737]; cytosol [GO:0005829] | thioredoxin peroxidase activity [GO:0008379] | PF10417;PF00578; | 3.40.30.10; | Peroxiredoxin family, AhpC/Prx1 subfamily | PTM: The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. {ECO:0000250|UniProtKB:Q06830}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19064914}. | CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000269|PubMed:1... | null | null | null | null | FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (PubMed:15099742). In I2 pharyngeal neurons, required for the inhibition of feeding in response to light and hydrogen peroxide (PubMed:25640076). In the intestine, plays a... | Caenorhabditis elegans |
A0A0K3AV08 | MLK1_CAEEL | MEQASVPSYVNIPPIAKTRSTSHLAPTPEHHRSVSYEDTTTASTSTDSVPEVRIRSESSQVSRESPPIRASKAFVASYEYEAQKDDELNLPLGAIITLVTVETNEDGWYRGELNGKVGLFPSNYAREVTYKDNLVEFKQDEIMLPVAVRTLSDCQIGHGATATVFKMDIKIKKELQNGRMGEAVGDQMKAALKRFNRHASNFRADVVSTDEQLEQLKREANLVNGLSHNNIVRLLGICLEDPYFGLLLELCEGSSLRNVCRNLNSDAAIPLGVLIDWATQVAEGMEYLTKQGYVHRDLKADNVLVKEEVCLCMDEEMFQY... | 2.7.11.25 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P80192}; | axon regeneration [GO:0031103]; defense response to Gram-negative bacterium [GO:0050829]; determination of adult lifespan [GO:0008340]; JNK cascade [GO:0007254]; MAPK cascade [GO:0000165]; p38MAPK cascade [GO:0038066]; phosphorylation [GO:0016310]; positive regulation of axon extension involved in regeneration [GO:0048... | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein kinase C binding [GO:0005080]; protein serine kinase activity [GO:0106310]; receptor tyrosine kinase binding [GO:0030971]; scaffold... | PF07714;PF14604; | 2.30.30.40;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily | PTM: May be phosphorylated on tyrosine residues by svh-2. {ECO:0000269|PubMed:22388962, ECO:0000269|PubMed:27984580}.; PTM: May be ubiquitinated and targeted for proteasomal degradation by E3 ubiquitin ligase rpm-1. {ECO:0000269|PubMed:21670305}. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; Evidence={ECO:0000269|PubMed:15116070, ECO:00002... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase which, by phosphorylating and activating mek-1, plays an important role in the activation of the JNK pathway composed of mlk-1, mek-1 and kgb-1 (PubMed:15116070, PubMed:20008556). Involved in the response to environmental stress such as heavy metals (PubMed:15116070, PubMed:188... | Caenorhabditis elegans |
A0A0K3AWM6 | MOM5_CAEEL | MHRHILILFLFGCLSADQRLSSTSISSMNGFSTTRKCEHITIPMCKNLDYNQTVFPNLLGHTTQSEAGPAIAQFNPLIKVKCSEDIRLFLCTVYAPVCTVLEKPIQPCRELCLSAKNGCESLMKKFGFQWPDQLDCNKFPVTDLCVGKNSSESSNSKNYRSSNDVTFGVSTIANEVVLSPKKCPHHMHTTSGSHFSLPLLSGRLPECSLTCEADNQVPMMFDGRVRRILRIWTAAWSVACFVCSLFTLVTFLVDLSRFAYPVRPILYLAFCYLAISTVYMIGVVGEDGFACGTYGSTPTTLVTQGGENVGCSALAVVHYF... | null | null | canonical Wnt signaling pathway [GO:0060070]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic digestive tract morphogenesis [GO:0048557]; embryonic morphogenesis [GO:0048598]; endodermal cell fate specification [GO:0001714]; engulfment of apoptotic cell [GO:0043652]; establishment of mitotic ... | early endosome [GO:0005769]; plasma membrane [GO:0005886] | Wnt receptor activity [GO:0042813]; Wnt-protein binding [GO:0017147] | PF01534;PF01392; | 1.10.2000.10;1.20.1070.10; | G-protein coupled receptor Fz/Smo family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15620652, ECO:0000269|PubMed:24401370}; Multi-pass membrane protein {ECO:0000255}. Early endosome {ECO:0000269|PubMed:15620652, ECO:0000269|PubMed:24401370}. Note=Uniformaly localized along the cell membrane throughout the cell cycle, but occasionally enriched at ... | null | null | null | null | null | FUNCTION: Receptor for Wnt proteins (PubMed:16930586, PubMed:22022276, PubMed:23295860, PubMed:24401370, PubMed:26292279). Most frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of gsk-3 kinase, nuclear accumulation of beta-c... | Caenorhabditis elegans |
A0A0K3AXH1 | ARID1_CAEEL | MSDDPAFLALGTEVSAKFKGAYCEAKIQKVDRSLKVKVSLKESPFGQMIVQDNDLPNAKFEINELTDVVFQRKFIRCQIQSIKDQSKYHVVFNDGDEKELRRTQLVLKGGKHFAADGNLDSMPLTNPESFSTPVIRGAAKRGAQKIRNAISEASGSRGGAVLLHNDDDENDEEDQEDGENEEDADDDDDDTEEQQQPRERRRAAAISAIGVLKKAIEDTQSEESSADSSEERERARSRRKRKDEASSAVTSDEEDQEDLATTDSENPVINGASSAAALSKTLQRKLEKQAMKREKQRLKEEEREEKLRLKEENREKKRRE... | null | null | defense response to other organism [GO:0098542]; ERAD pathway [GO:0036503]; proteasomal protein catabolic process [GO:0010498]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; response to endoplasmic reticulum stress [GO:0034976] | nucleus [GO:0005634]; SWI/SNF complex [GO:0016514]; transcription repressor complex [GO:0017053] | DNA binding [GO:0003677]; transcription cis-regulatory region binding [GO:0000976] | PF01388; | 2.30.30.140;1.10.150.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000305}. | null | null | null | null | null | FUNCTION: DNA-binding protein which modulates activity of several transcription factors (By similarity). Plays a role in the modulation of endoplasmic reticulum (ER) homeostasis during chemical and pathogen stress, including exposure to the Gram-negative bacterium P.aeruginosa (PubMed:30287474). {ECO:0000250|UniProtKB:... | Caenorhabditis elegans |
A0A0K8P6T7 | PETH_PISS1 | MNFPRASRLMQAAVLGGLMAVSAAATAQTNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGAGTVYYPTNAGGTVGAIAIVPGYTARQSSIKWWGPRLASHGFVVITIDTNSTLDQPSSRSSQQMAALRQVASLNGTSSSPIYGKVDTARMGVMGWSMGGGGSLISAANNPSLKAAAPQAPWDSSTNFSSVTVPTLIFACENDSIAPVNSSALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALIGKKGVAWMKRFMDNDTRYSTFACENPNSTRVSDFRTANCS | 3.1.1.101 | null | cellular response to organic substance [GO:0071310]; xenobiotic catabolic process [GO:0042178] | extracellular region [GO:0005576] | acetylesterase activity [GO:0008126]; carboxylic ester hydrolase activity [GO:0052689] | PF01738; | 3.40.50.1820; | AB hydrolase superfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:26965627}. | CATALYTIC ACTIVITY: Reaction=(ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+); Xref=Rhea:RHEA:49528, Rhea:RHEA-COMP:12420, Rhea:RHEA-COMP:12421, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:131701, ChEBI:CHEBI:131704; EC=3.1.1.101; Evidence={ECO:00002... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.431 mM for pNP-acetate {ECO:0000269|PubMed:30502092}; KM=0.315 mM for pNP-butanoate {ECO:0000269|PubMed:30502092}; KM=0.053 mM for pNP-hexanoate {ECO:0000269|PubMed:30502092}; KM=0.048 mM for pNP-octanoate {ECO:0000269|PubMed:30502092}; KM=2.283 mM for pNP-dodeca... | PATHWAY: Xenobiotic degradation. {ECO:0000305|PubMed:26965627}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9 for PET film hydrolysis (PubMed:26965627). Optimum pH is 9 for PET (commercial drinking bottle) hydrolysis. Optimum pH is 6.5-8.0 for BHET hydrolysis (PubMed:29603535). Optimum pH is 8.0 for the hydrolysis of pNP-esters. The enzyme is active at pH 6-10, has... | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius for PET film hydrolysis (PubMed:26965627). Optimum temperature is 30 degrees Celsius for PET (commercial drinking bottle) hydrolysis and BHET hydrolysis (PubMed:29603535). Optimum temperature is 35-45 degrees Celsius for t... | FUNCTION: Involved in the degradation and assimilation of the plastic poly(ethylene terephthalate) (PET), which allows I.sakaiensis to use PET as its major energy and carbon source for growth. Likely acts synergistically with MHETase to depolymerize PET (PubMed:26965627). Catalyzes the hydrolysis of PET to produce mono... | Piscinibacter sakaiensis (Ideonella sakaiensis) |
A0A0K8P8E7 | MHETH_PISS1 | MQTTVTTMLLASVALAACAGGGSTPLPLPQQQPPQQEPPPPPVPLASRAACEALKDGNGDMVWPNAATVVEVAAWRDAAPATASAAALPEHCEVSGAIAKRTGIDGYPYEIKFRLRMPAEWNGRFFMEGGSGTNGSLSAATGSIGGGQIASALSRNFATIATDGGHDNAVNDNPDALGTVAFGLDPQARLDMGYNSYDQVTQAGKAAVARFYGRAADKSYFIGCSEGGREGMMLSQRFPSHYDGIVAGAPGYQLPKAGISGAWTTQSLAPAAVGLDAQGVPLINKSFSDADLHLLSQAILGTCDALDGLADGIVDNYRAC... | 3.1.1.102 | null | cellular response to organic substance [GO:0071310]; xenobiotic catabolic process [GO:0042178] | cell outer membrane [GO:0009279] | carboxylic ester hydrolase activity [GO:0052689]; metal ion binding [GO:0046872] | PF07519; | null | Tannase family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305|PubMed:26965627}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000305|PubMed:26965627}. | CATALYTIC ACTIVITY: Reaction=4-[(2-hydroxyethoxy)carbonyl]benzoate + H2O = ethylene glycol + H(+) + terephthalate; Xref=Rhea:RHEA:49532, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30043, ChEBI:CHEBI:30742, ChEBI:CHEBI:131704; EC=3.1.1.102; Evidence={ECO:0000269|PubMed:26965627, ECO:0000269|PubMed:30979881}; Phys... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.3 uM for mono(2-hydroxyethyl) terephthalate (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:26965627}; Note=kcat is 31 sec(-1) for the hydrolysis of mono(2-hydroxyethyl) terephthalate (at pH 7 and 30 degrees Celsius). {ECO:0000269|PubMed:26965627}; | null | null | null | FUNCTION: Involved in the degradation and assimilation of the plastic poly(ethylene terephthalate) (PET), which allows I.sakaiensis to use PET as its major energy and carbon source for growth. Likely acts synergistically with PETase to depolymerize PET. Catalyzes the hydrolysis of mono(2-hydroxyethyl) terephthalate (MH... | Piscinibacter sakaiensis (Ideonella sakaiensis) |
A0A0L7KF24 | FCLN_PLAFX | MNLTKLMKVFGYINIITNCVQSFTNRADKKRYNVFAKSFINTINTNLYTFKAVMSKTPEWIHEKSPKHNSYDIIEKRYNEEFKMTYTVYQHKKAKTQVISLGTNDPLDVEQAFAFYVKTLTHSGKGIPHILEHSVLSGSKNYNYKNSIGLLEKGTLHTHLNAYTFNDRTVYMAGSMNNKDFFNIMGVYMDSVFQPNVLENKYIFETEGWTYEVEKLKEDEKGKAEIPQMKDYKVSFNGIVYNEMKGALSSPLEDLYHEEMKYMFPDNVHSNNSGGDPKEITNLTYEEFKEFYYKNYNPKKVKVFFFSKNNPTELLNFVDQ... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10542284}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q76NL8}; | acquisition of nutrients from host [GO:0044002]; protein processing [GO:0016485] | apicoplast [GO:0020011]; chloroplast [GO:0009507]; food vacuole [GO:0020020]; mitochondrial matrix [GO:0005759]; vacuolar membrane [GO:0005774] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF08367;PF00675;PF05193; | 3.30.830.10; | Peptidase M16 family | PTM: Does not require processing for targeting to the food vacuole or maturation. {ECO:0000269|PubMed:12798513, ECO:0000269|PubMed:12876284}. | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10542284}; Peripheral membrane protein {ECO:0000269|PubMed:12876284}. Plastid, apicoplast {ECO:0000250|UniProtKB:Q76NL8}. Vesicle {ECO:0000269|PubMed:12876284}. Note=Localizes to the food (or digestive) vacuole, an acidic vacuole where host hemoglobin is digest... | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5 (food vacuole) (PubMed:12876284). Optimum pH is 7 (PubMed:12876284). {ECO:0000269|PubMed:12876284}; | null | FUNCTION: In the food vacuole, acts downstream of proteases plasmepsins PMI and PMII and falcipains during the catabolism of host hemoglobin by cleaving peptide fragments of alpha and beta hemoglobin subunits generated by PMI and PMII and falcipains (PubMed:10542284, PubMed:12876284). In the apicoplast, degrades apicop... | Plasmodium falciparum (isolate HB3) |
A0A0L8M630 | AMDH_STRVG | MISTVVWGTGNVGRLAIRAVEAHPALQLCAVIVHNPAKVGRDAGELGELDRLLGVEATDDIEAVLAARPRAVVYAASGDVRPDEALADITRAVRSGAVVVSPALYPLYDHRNAPPEFRDPVLAAVTEGGGSLFASGVDPGWGNDVLPLLLSGLGTTIDVIRCQEIFDYSTYDQPDSVRYLVGMGQPMDYEPMMLMPSIPTMVWGGQIRMMARALGVELDEIRETSDRRALDTTVTTRTMGEFGAGTQGAIRFEVQGIVEGEPRIVIEHVTRIHPSCAPDWPVPPDGGDGAHRVVIEGRPRIEVTIEATDEGENRSAGGNA... | 1.4.1.28 | null | lysine biosynthetic process via diaminopimelate [GO:0009089] | null | 4-hydroxy-tetrahydrodipicolinate reductase [GO:0008839] | PF19328;PF01113; | 3.40.50.720; | Amine dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=a secondary alkyl amine + H2O + NAD(+) = a ketone + H(+) + NADH + NH4(+); Xref=Rhea:RHEA:74175, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:28938, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:193112; EC=1.4.1.28; Evidence={ECO:0000269|Ref.2}; CATALYTIC ACTIVITY... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4 mM for serinol {ECO:0000269|Ref.2}; KM=0.84 mM for NAD(+) {ECO:0000269|Ref.2}; KM=2.2 mM for dihydroxyacetone {ECO:0000269|Ref.2}; KM=0.022 mM for NADH {ECO:0000269|Ref.2}; KM=26.5 mM for NH4(+) {ECO:0000269|Ref.2}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 10.0 for the oxidative deamination reaction, while the optimum pH of the reductive amination reaction is rather broad and between 6.5 and 7.0. {ECO:0000269|Ref.2}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius for the deaminating reaction. Is not thermostable. {ECO:0000269|Ref.2}; | FUNCTION: Catalyzes the reversible oxidative deaminations of a broad range of amines, amino alcohols and amino acids. Catalyzes the reversible dehydrogenation of serinol in the presence of NAD(+) to give dihydroxyacetone, ammonium ion and NADH, while NADP(+) shows a slight activity. Is also able to produce 2-amino-1-pr... | Streptomyces virginiae (Streptomyces cinnamonensis) |
A0A0M3Q1Q3 | GTPS1_THYVU | MRRSGNYQAPVWNNDFIQSFSTDKYKDEKFLKKKEELIAQVKVLLNTKMEAVKQLELIEDLRNLGLTYYFEDEFKKILTSIYNEHKGFKNEQVGDLYFTSLAFRLLRLHGFDVSEDVFNFFKNEDGSDFKASLGENTKDVLELYEASFLIRVGEVTLEQARVFSTKILEKKVEEGIKDEKLLAWIQHSLALPLHWRIQRLEARWFLDAYKARKDMNPIIYELGKIDFHIIQETQLQEVQEVSQWWTNTNLAEKLPFVRDRIVECYFWALGLFEPHEYGYQRKMAAIIITFVTIIDDVYDVYDTLDELQLFTDAIRKWDVE... | 4.2.3.114; 4.2.3.115 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:E2E2P0}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:E2E2P0}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:E2E2P0}; | diterpenoid biosynthetic process [GO:0016102]; response to jasmonic acid [GO:0009753]; response to salicylic acid [GO:0009751]; response to UV-C [GO:0010225] | null | gamma-terpinene synthase activity [GO:0102903]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + gamma-terpinene; Xref=Rhea:RHEA:32559, ChEBI:CHEBI:10577, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.114; Evidence={ECO:0000269|PubMed:26750479}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32560; Evidence={ECO:0000269|PubMed:26750479}; ... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:26750479}. | null | null | FUNCTION: Involved in the biosynthesis of phenolic monoterpenes natural products thymol and carvacrol which have a broad range of biological activities acting as antimicrobial compounds, insecticides, antioxidants and pharmaceutical agents (PubMed:26750479). Monoterpene synthase which catalyzes the conversion of gerany... | Thymus vulgaris (Thyme) |
A0A0N7CSQ4 | TX41A_SCOMU | MLKSFCILSVFMVLFLAKFPDLCSGEEISPLKIVVRNSEYLNNPCNGVTCPSGYRCSIVDKQCIKKEK | null | null | null | extracellular region [GO:0005576] | ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729] | null | null | Scoloptoxin-04 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26420335}. | null | null | null | null | null | FUNCTION: [Tau-scoloptoxin(04)-Sm1a]: Extremely potent agonist and potentiator of TRPV1 (EC(50)=470-521.5 nM (mouse)) (PubMed:26420335, PubMed:32097697). It strongly promotes the heat activation process by downshifting the activation threshold temperature (PubMed:26420335). It preferably binds to the activated channel ... | Scolopendra mutilans (Chinese red-headed centipede) (Scolopendra subspinipes mutilans) |
A0A0N7KJT8 | APL25_ORYSJ | MWDLNDSPAAEAAPPPLSPSADDSGASSSSAAAVVEIPDDADDDSAAVVVVTRQFFPPAVPGGGGDPAPGNARAGWLRLAGAAPPVAATGPAASAAVSKKSRRGPRSRSSQYRGVTFYRRTGRWESHIWDCGKQVYLGGFDTAHAAARAYDRAAIKFRGVEADINFSLEDYEDDLKQMSNLTKEEFVHVLRRQSTGFPRGSSKYRGVTLHKCGRWEARMGQFLGKKYVYLGLFDTEEEAARAYDRAAIKCNGKDAVTNFDPSIYAGEFEPPAAATGDAAEHNLDLSLGSSAGSKRGNVDGGGDDEITGGGGGGAGSDQRV... | null | null | regulation of floral organ abscission [GO:0060860]; regulation of flower development [GO:0009909]; regulation of seed development [GO:0080050]; response to cold [GO:0009409]; seed abscission [GO:0097548] | nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976] | PF00847; | 3.30.730.10; | AP2/ERF transcription factor family, AP2 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366, ECO:0000269|PubMed:22408071}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:22408071). Involved in spikelet transition and development (Probable) (PubMed:22408071). Prevents lemma and palea elongation as well as grain growth (PubMed:22408071, PubMed:28066457). Required for seed shattering through specifying abscission zone (AZ) development (PubMed:2240807... | Oryza sativa subsp. japonica (Rice) |
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