ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A7J3XEG4 | MKGYGKALRHVRSLEIEAKKSNRRRIVVLAGEQEAILSFLAEVTKHRKSGLVVVDRDENGKEIAAFLQQVGYEQTSYLDLREKLGRTYESLVIDLRNNLNPDDLVLALETLSGGGVAFLLTPPIREWPWITRFHRELLVPGRSESELRLNFMRRFLERLQKAKGVSIIELFDSEAKLVKSGVIGVKGRKRTTPSLPRRSRLDLRSYAVCATKDQTRALRRLEHFWLKEEKRYFVLLSDRGRGKSALLGIFLAAILKLESKTRHSLRIALTSPSFEGLATLLDFLKLGLKRMGVRFEKEENKITVGGRLVVSWLPPPRVLE... | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Catalytic Activity: acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O = ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) + phosphate... |
A0A368BN19 | MIFVYNLIYILALPLIIIRDFLTKRVKGINFFKSKFGFIDKSQDEHIWIHGVSLGEVRALSGIVSSLLNEEKRILFTSSTNTGLTEILKKYSTDSVVVMPFPYDLNFLHQKIISNFNVSKIILFESEFWPNLIFSKPNNVQLISLNTTISQKTLKKMRLFKPFSDQLIKRFDLFLAQTDEIKSNLLEFQASNIKVTGNIKLSSENYRLNEEKANEIASKLAKNRLKVVAGSTHEGEEDFIIEALKSLHDMQLIIAPRHPERFHALSGTFQNQRLNYSIYSHQNNHESSDIVLFDRVGDLYELYSACDIAIVGGSIIFTKG... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A3G3BHZ5 | VTAHAFIMIFFMVMPIMIGGFGNWLLPLMIGAPDMAFPRMNNMSFWLLPPSLTLLTMSSMVEMGAGTGWTVYPPLXANIAHSGPSVDLAIFSLHLAGISSILGAVNFITTVINMRTPTMTLDRTSLFVWSVXITAV | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A066W5R2 | MNLPPGTEGIRLRKPTNTTETPLAARKPRHTGLLQDQLRRSSRAPWCPSLTTAFRMLVLIRVAAATWSNIQDCDEVFNFWEPLHYLDQGHGFQTWETSPAYALRSWAYILLHIFPAKFPIWVASFDKRHTFFGLRMVFAFVSSFCEARLFRTVAEHVNDRIGRYMLFMLMFNAGMWNASTEDIHSDAPFFTATGAIIGWPFSLLLAVPFVIEELTIYGGDIVSGSSLPGWVKNRWKYLFGSGAVAASLFIPVTLIDTYAYGRLALTPWNIVRYNIFSNSSGRSPDLYGTEPWYFYIFNLILNFNILAPLALGSLPALLVT... | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 579
Sequence Mass (Da): 65509
Location Topology: Multi-pass membrane protein
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A0A066W6G8 | MFAIWGHPFLEHTYLYHLTRRDHRHNFSPYFYPIYLNYDRNDSPNSLPSRMLQTPLFSFVPQMALCAVSGLLLGKRDLSFAWFIQTMIFVTFNKVCTSQYFMWYLWFLPLVLPSLQMSAKRGTSVLLVWIIAQVGAHSNCSSSATEHIMKAIWLGAAFRLELLGHGVYIWVWAASVVFLVSNTFVLGELITAYNPKLTHTV | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly. Required for cell wall integrity.
EC: 2.4.1.-
Subcellular L... |
A0A066VQF6 | MRTGAIIAALAAASTAHAHATFQYLWVNGVDKGSTCVRPPLNNSPISDLSSKINVTGGGSANPATVKFPGAYSPTDPGILFDLYGGYTSYTIPGPAVYVPGSPTGGGGTPTTTTTRAATTTTSSAAPVSTGPVVVKYGQCGGQGWTGGTTCAAGSTCTVVNAFYSQCL | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
EC: 3.2.1.4
Subcellular Location: Secre... |
A0A485D9Z2 | MSDQIENRIIEAKSRGIYEAPGMALLHIAYERLLTGIHNEDTIEQYHAHGRQLGRLLYQGRWFDSQALMLRDALQRWVASAITGEVTLELRRGNDYSILNTVSDNLTYKAERLTMEKGDSMFSAEDRIGPTDHA | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3.
Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+)
EC: 6.3.4.5
Subcellular Location: Cytoplasm
Sequence Length: 134
Sequence Mass (Da)... |
A0A7C3RGB3 | MQNNFEIKNFILDILYSFCLIFFNILKDYWHLIILLAIIFLAYEVRLTTSSTKLILDYDPWWFYRHAKVLLENNFVPPKWDYLSYYPPGRPYDFQLGWSYTIAFFYLLFKFFIPNFMDFACRWVAIFAALCTIPAYLVGRVISNKYGALATAFLATTTPTFITVSMYGYVDSDVVVVFYTFLVIGMIFYTIKNYKGIKSKRTWFAISLAVLANWLFAFNWNSSWYVYYLFLISIPAYLIFKIFIYLIQGLAWNETKEKIKKEGKRITLPILIIGVIAGILTQITSGWPFNTYSPIRQLLDGLALLTGRSLIVNISVAELQ... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
EC: 2.4.99.21
Subcellular Locat... |
A0A327X5K9 | MLDNTSQLLLRHPILTPDSWLINANDALSHQAPGLPTLRAHFVYAHAAYRADDPMHTLAAELPSQTIPHAVVYVPKEKALLHMLMDNLAQYTTSGTTVHLVGHNKGGIKSVVKQLGGYWQQSEKLASGNHCLLYACTRSDQVAPPFTLASYRHSYRLAEYSNLEVFNLPGVFSEQKLDQGTQLLLDYLHQKPRPKSPQRVLDFACGTGIIGAYLRAHYPVAHLTACDISSLALNCSQHTLAAQPNTCDFELVASDGLQRIQHRYDWIVSNPPFHTGQKTDYSIAAQFFAAAKQRLHKNGRLTLVANSFLGYKDMLSPHFA... | Function: Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle.
Catalytic Activity: guanosine(1207) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1207) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.172
Subcellular Location: Cytoplasm
Sequence Length: 340
Sequenc... |
A0A7V7RJK3 | MKLRYPLFIFMVLLMLSACSNENENAAAPEKDQPETETAGVDKELENVKAMFEPLGEMPIPADNEMTDEKVELGKTLYFDPRLSGNNKLSCMTCHAPGAGYGDGLGTFIGFEGAQGSRNSPTIINSGYYPEYFWDGRAGSLEEQALGPIQSEVEMNQDLDELVIELNGVPTYVEQFNTVFNDPISANNIAKAIAAFERTIVISDTAFDRYLQGQEDAISADAKEGMKLFAGKASCITCHAGPMLSDYSYHNLGMTGDEGRYEVTKNEEDKGKFRTTGLRGVAHTAPFMHDGSFATLEDVVNYYNDGGGDHVNKSDLINPL... | PTM: Binds 2 heme groups per subunit.
Cofactor: Binds 2 heme groups.
Subcellular Location: Periplasm
Sequence Length: 350
Sequence Mass (Da): 38282
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Q6XEV2 | LLPPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGVSSILGAINFITTIINMRINNLSFDQMSLFIWAVGITALLLLLSLPVLAGAITMLLXXRNLNTSFFDPAGGGDPIXYQ | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A177ZKU6 | MKTIILAGGQSRRMGQNKSLMKLEGIRLIDRIIHECMPISEKVILVSNHDLADIPEEVLMVADFPPFKGEGPLAGIWTGLTLAKEGTCLVVACDMPFISKSFARKFEKMMLEKKVDAVIPVIAGRMHPLFAVYHTRIKDQIYQTLLNGKRSVRSMIADIHVEFYPMDEYEKILWNMNTMNDYIQAGKMTDRGVLDEL | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
A0A8U0QEV9 | TVCLFPPQESDYFTPQGEFRVDKEGSPILLNCLMYKMSYYRFGEMQLDFRTPPGFDRTRNAEIGNKDIKLKHLEEAFTSEHWLVRIYKVKKEENRDPLEHSPRSSSSSRQKYTSKKTAKRKRGHVKNKLALKKGKKLNNKKSV | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: a dolichyl diphosphooligosaccharide + L-asparaginyl-[protein] = a dolichyl diphosphate + H(+) + N(4)-(oligosaccharide-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)-L-asparaginy-[protein]
EC: 2.4.99.18
Subcellular Locati... |
S0DF79 | MVLSGGIGLVSLVLVVLHSNKYISGAFMWFWLSVYWWVCVVVCVVEFLGGFFGGFFGGLSYKMGYDGLSMFFIVLALLVTLVSFLSMAPSGGVLNAIGGRGLATSFILLGTLLVWFFIISSGIEFFICFELCVIPIFFLIGYWGSQRERIFSNYYFLFYSLMAPVPFLFLMISSVSRGMGTYFYTTHSGGWVASLGGEALGPWVVFGLVLGFLTKLPIYGFHIWLPKAHVDAPVGGSMVLAGVMLKMGSYGLMRLSVFEWVVASPVIMFIVGLGMWGFFVTSVLCLRLVDFKVIVAFSSVSHMSIAIVGVLSAVGWGVLG... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 ... |
A0A1V5GQB9 | MSRSLFRRTFISTIASLVVTASVPVIPSGVFDSAYAASAGQTLSVGNGRNQHKEDNVDGYSYEIWIDTTGGSGSMTLGSGGSFSTEWSAQVSAGNFLARRGRNYDASKKATQYGDIVMDYSAEYSASAQGNSRLCVYGWFKDPLVEYYIIEDWVNWCPSGQSKTVTVDGAQYDIFQTPHTGPTILGDTRTFQQYFSVRKQKRTSGTITVSDRFKAWENAGWNIGNLTEVALNVEGWESSGKANVSKLTIGTESSGQQNDTPVTTQPVQQGSTDNGQGWTMPGNGNGQGFDWSSFDWSNFQLPGNGDNGQNWQMPGNNNQQ... | Pathway: Glycan degradation; xylan degradation.
EC: 3.2.1.8
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Sequence Length: 685
Sequence Mass (Da): 73750
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A0A8T4DYK3 | MVFNDLDFLIELAKVTNGTVSTTEIAKKTRLSQQSASRKVIILEKEGMIKRDILGSGQKIRLTEKGIDVLEKTYSDLENVLENEKSERFVFSGTVFTGDGEGKYYMSLKGYADQIREKMGFVPYKGTLNLRLGTRTEIEEKNVMARSGGIVLEGFSDGERSFGEVRCFPCRINGTLCGAVIIPKRTHYPKDIIEIISKENLRKRFSIKNGDTIEIEVSQ | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1.
Function: Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
EC: 2.7.1.161
Catalytic Activity: CTP + riboflavin = CDP + FMN + H(... |
A0A367YIA0 | MNSITKHSIRFLSDKAARFVPKSGVYPKGYAVGGIHCGVKKDGKTLDLAILQNTFGKEASTAGVFTKNNIQENSQGKDGAGINSFVINSGNANAVTGAQGLKDAEEMVIVTDSVLENPLDSTLVMSTGQFKIGDDTYTLAGLCKGAGMICPNMATLLGFFVTDAPVSPAALQQILRYAVDRSFNSITVDGDMSTNDTIVAMANGAAGGELIENTSSSAERFAALQTEIVDFAQQLAQLVVRDGEGATKFITLKVNDALSYKDAKSIASSDANWGRILCAIGYANVTTDQSVIPEKTSVKFVPVDGSEHLQLLVNGEPEKV... | PTM: The alpha and beta chains are autoproteolytically processed from a single precursor protein within the mitochondrion.
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Function: Catalyzes two activities w... |
A0A368BNW4 | MNLVIYNLLILILLPVFGFRIIIKSISDKDYRRNFLQRFGYNLSPIVRTNKKVIWFHAVSLGEVIGSQGIINKLLKDFEVIITTTTPSGHRRAKEIFNDDIVINYMPWDFYPFINRFINFYKPQGILIFETEIWPSMISCAYKKDIPLYLVNGRLSQKSYKAYSMFFWLVKKILSQVTFYFVQTENHMQRFLKLGVDRDKIKTVGSVKFDISGLETKQIDSPPFILGGSTHHGEEKLLLKAFNKFSKKKDLKLYLCPRHPERADQIVKQAIDMGFETQLFSTINSQSFDVCVIDSIGLLPSFYAASSMAFVGGSLVPRGG... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A8T3X728 | MKKIIIITVVMIFVLIVMNFYYFSPAAFIAKNQGTVLDDNWYNALTWVNKNTEKCAVIATYWDPGHFITGIARRPVVFDGASQGDTIYSTDTKYSGLEPGEIVTEKYDNGIVQIIRKINEPYIVDYISKHYPQYSNGTERARIKDIAISLFTSNESLALKYLKDYRQAGCKEFYYIASSDLIGKSTWWTYFATWNPEGSEKPCSGELNKGSCYNYMTVGLGQARPAPSENAIVYTYPFGTQQAFLIYEVNSTRRAFLQQGSQIARVSNLMFFTQSQGLITTEEGAEVNGLLVQSPDKGSIIFMPPELQNSMFTRLMFFDG... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
EC: 2.4.99.21
Subcellular Locat... |
A0A6P8WZB5 | MRSRKVQVMVIGFFIMWTFITYYVLLRTSNAQLSRKQQQQLKRLVPEALAEQSKGLQLTRNLIEFLKYKYSSNEQPGTTTTTPRISIVAAEISNEIPAPESGVKATAESKSTPSQIPTQTHLANGEPVIPILVFACNRVSVVKCLDNLVQYRPSVEQFPIIVSQDCGDVLTKEAIQTFGKQLTLIEQPDLSDIVVLPKEKKFKGYYKISRHYGWALNTTFQIGFDFVVIVEDDLNVAPDFFEYFLATHKLLKQDPSLWCVSAWNDNGKANVVDTTRPDLLYRTDFFPGLGWMLTKELWQELSVKWPKSFWDDWIRHPEQR... | Cofactor: The cofactor is mostly bound to the substrate.
Pathway: Protein modification; protein glycosylation.
Function: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
EC: 2.4.1.101
Subcellular Location: Golgi apparatus membrane
Catalytic... |
M4MDW2 | CDPKADSTRLILHAKAQNTIMEMAAEAGSVEDLELEDVLRVGYAGIRCVESGGPEPGVGCAGRGVITAINFLEEEGAYGEDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVVSGEMMA | Function: The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.
EC: 1.18.6.1
Catalytic Activity: 16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[... |
A0A132NVR9 | MLNSSIFVFAFLTRCILIYLGAYASDPPAVSMTDIDYLVIWDGVCSASAPSKRPTYRYSPIFKLVLWPICRWPAYGKVLYSLSDLAFALLAYRITGRSRAVYHLWLMNPFVIALSVRGSFDSMIQLLLAWMLLAIKQHRYLISGALLGLCIHLRIYPIIFAPFIILYALVDRGLLQKELLARIVQTGLFIFAVTISFSTATLISMLMDNDYLSTGLLYHVSGRIDHRHNLSVLWAVQLACSKGKEVFCWPFAKIFQAGILAILIIRRTMVLTAPTVSKNEQDQSVDKPKYPYCHLLNDLDQACRVFVAFNSVVTAQYFSW... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum mem... |
A0A2A4MSA6 | MVYQVSKLAIKTAGKFLSSGAVIAYPTEAVWGLGCDPQNFQAVDRILRLKCRSVDKGLILVVSCFSQVEQLCRHLTQQQRERLNAETNRPTTWLIPDPQNTFPYWIKGRYESVAVRCIKHPLVEALCENFGAIVSTSANNSSGREIRSRLNIQKQYSETLDYILPGRVGVHSKPSQICDLVSGQVIR | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosp... |
A0A066VY92 | MLVAGKAANANKKPVIFDPVGVGATRFRRETANELLNSWQASIIKGNAGEIGALLGSSEVVARGVDSTGPGFSDPGNIVRTLAKRERCIVVMTGKTDYISDGYTAVAVSNGHSMLGDITGSGCIVGTAITAFAAASRLVATDCVEDQGKLVRGDMFQAAVAGVLAITIASEIAAARPDVKGTGTFMSALIDELYNLKPQTIADRAMVEIL | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
EC: 2.7.1.50
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Length: 210
Sequence Mass... |
A0A7C0YCL0 | MVVYLYTVKLDYVNRNSTSVGSKAVNLGEMINAGLPVPPGFVVTNDCFEKFLRANKLENKISEILSKLNFKSYHLVKQASSEIHNLITNATFPDYLEKPIKDEYEELSVGREAKEIGGIALDLIKAGRGEAFVA | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 134
Sequence Mass (Da): 14868
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B0BQR8 | MFTKNILPAIQHDQYILLMRDEFPVAFCSWANLTLTNEVKYVRDVTSLTFEDWNSGERKWLIDWIAPFGDNNTLYRYMRKKFPNEVFRAIRVYPGSTEAKIIHVQGGQINKFTAKKLIQQYQEELIQVLNNHKKIVRG | Function: Involved in fatty acylation of protoxin at internal lysine residues, thereby converting it to the active toxin.
Catalytic Activity: a fatty acyl-[ACP] + L-lysyl-[protein] = H(+) + holo-[ACP] + N(6)-(fatty acyl)-L-lysyl-[protein]
EC: 2.3.1.-
Subcellular Location: Cytoplasm
Sequence Length: 138
Sequence Mass (D... |
U3C5R0 | MDRECMEFDVIIVGAGPSGLSAACRLAQLNQNRESPLSICVVDKGSELGAHIVSGAILETKALDELFPDWRNMGAPISASVQSDQFLYLTNELNSLSIPSWLTPNPMHNNSDNYVISLANFCRWLGQQAESLGVDVYPGFAASSINYDPSGQVIGVNTSDMGLDKSGHEKPNFEAGIELRARYTIFAEGCRGHLGKELIQQFDLAKDKQPQHYALGLKEIWELPEDHHFQPGDVLHSAGWPLSKSQTTGGGFLYHLENRQVAVGLIVDLNYSNPYLSPFDEFQRFKQHPAIKIHLQGAQRISYGARAIAKGGLSSLPKQQ... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
EC: 1.5.5.1
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Length: 552
Sequence Mass (Da): 61054
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A0A2M6P011 | MKILILGANGYVGKRCKESWSDAVASDKKIHSTQDVLDLLEEHKPNAVLNAAGVRGKPNVDWCEDHQLVTILGNTKLPIIIAEACQQKGVYLLHIGSGCIFYGDSPHEDKEWREEDMGNPTEVTYSRTKWAADLVLSTLPNVGIARIRMPIDWIPSNQNMIDKLATYPKVIDVENSVTIVDDMVDVFHQLLEKKAEGIFHVTNPGKLKHKEIVALYEEMIDPTHT | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 225
Sequence Mass (Da): 25224
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W2QDA0 | MRLSCVLLIAVVVLLSSCDDTSANNTGQALKTKTMESGDALVPDTTQRLLRTQQISGTDAVASNDEERAPLSLKNLLNVVRFKAATNDFARSNLDKMLSDPIFKMEMFQRWNAKYSADKVIRILDISKTKNIPYGAMLQEFLNTYGRRPIKTQ | Function: Effector that suppresses plant defense responses during the early stages of pathogen infection.
Subcellular Location: Secreted
Sequence Length: 153
Domain: The RxLR-dEER motif is required for the delivery of the effector to the host cell cytoplasm.
Sequence Mass (Da): 17132
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A0A7C0YWP8 | MTTGFFIDKSIELKGGNLITISFYNASFDEISDLKDRLQKEYKVAAYTTTSAIETQLSVECSGIDTNRLIKDINKTLEIKNYEISRIDPKLSANILNDIIYSIIFAFVAIAIIIFILFRTLIPSFAMVLCAFSDIVITLFLMNIFGIPLSIATFTALLMMLGYSVDSDILLTTRVLKSHENFDKQYKSAMKTGLTMSATSIVGLIAILLITGYSSVFGQLASVLIISLLVDIPNTWIQNATILDIYLEKRKR | Function: Involved in protein export.
Subcellular Location: Cell membrane
Sequence Length: 252
Sequence Mass (Da): 28132
Location Topology: Multi-pass membrane protein
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A0A011PXD6 | MQGNSRVPSSAQSDVHEHLATVVARHASAPFRKPYADYNRAAFATSFARYQRLAPGAPLILDAGCGVGESSVALATAYPTHYVIGVDQSAARLQRGQRGEHRRGESHESHDGQHAGPANVDLVRADLVDYWRLLLDAGVRLDRHYLLYPNPWPKIGHLRRRWHGHPVFPALLALGGVLECRSNWPIYIAEHCLAVQQLTGRAAVLEPFVPAQPMTPFERKYLDSGHQLFRTVTDLT | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
EC: 2.1.1.33
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 236
Sequence Mass (Da): 26221
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A0A8T3XX37 | MQAKKEWVYWTDKLAKDVIDKEKKLRRGNKVFRTESGLGASGFPHIGSFGDVVRSYSVSLALKDAGVKSEYIAYSDDFDGLRKVPLTLPDTLEKFIGVPVAYIPDPFKCHDSYGEHMSSLLIDAIEKAGIDYTFQSAAENYRKGVLDEAIETILLKSEKVGQIVKNLTGQEKFIETLPYFPVCEKCGKIYTTRAYKMIEDEHKVLYVCDQEFQGKNLNDDKKIVIKGCGHKGEASYFKGNGKLSWKPEFAARWKSLKILFEPYGKDIKDSVLINDAICREILDFEPPTHVMYEMFLDKSGKKISKSYGNVFTPQVWFNYG... | Catalytic Activity: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys)
EC: 6.1.1.6
Subcellular Location: Cytoplasm
Sequence Length: 538
Sequence Mass (Da): 61593
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W2PM93 | MSVKWLVLAIAAAIILTASNVASITTSSTTSKKSTLDFPSLPRVSSRYHALKGRSLRSGASGDDVKTDEDRAFNTFATADDAGRNFLNAANSNPILKKLDNFMLKLRYKWWLMRGKTPENIRVKLGLHFVTNDKTHPNYKKWLGYLYAFNKKHKISG | Function: Effector that suppresses plant defense responses during the early stages of pathogen infection.
Subcellular Location: Secreted
Sequence Length: 157
Domain: The RxLR-dEER motif is required for the delivery of the effector to the host cell cytoplasm.
Sequence Mass (Da): 17622
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W2Q781 | MRLSFIIFVLVSVCFAPSVNSNTTGQTTHGAGNRSLRGDETADVEERAQAIIGKWLWGPFSSATWKKMLVDTEYQRIMFKKWDGYSLDTIKERIGRAIIQDDNNLAKMMLDYVENHRVYK | Function: Effector that suppresses plant defense responses during the early stages of pathogen infection.
Subcellular Location: Secreted
Sequence Length: 120
Domain: The RxLR-dEER motif is required for the delivery of the effector to the host cell cytoplasm.
Sequence Mass (Da): 13794
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A0A1G0N423 | MQAYLPLVLLIVFVLVNAAIMVGGSHLLSWTRPTAVKDQPYESGMPPLGDARERFDVKFYLVAVLFIVFDIETVFMMPWGVAFRQLDLFGLGILGGLIEMAIFVVILAVGYVYVLKRGALEWL | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
A0A1M7ZMK5 | MITGVCSRVRRHVGAAMEFPSVTRNHRAGAILIAAAMLCPPAGTAIAAGLPDEPPAAEPVSFMRACDAQGKGYFLVPGTDTCMRIDGLVYYEFWVYGSNQASGQPGWYSPSKNGVSSYTRGDIKFHTATPTEEGMITTFTELRMSLQSNGPGPEPTQLTLYHAVMTWNGITAGRTQSMFDYFTGTTYASLYEPAWSDTKTNMLAYTYSFGNSGLSVTGSVEDNASRQVGIINGPGFDAGTANGYAGVRAPDLVGQVNLSQSWGGFQWSIASHQVNSYQNNAVGYDKSAMGWATAGGVTVNLPFLGDGDSLVVQAAYGYGA... | Function: Forms passive diffusion pores that allow small molecular weight hydrophilic materials across the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 441
Domain: Consists of 16-stranded beta-barrel sheets, with large surface-exposed loops, that form a transmembrane pore at the center of ... |
A0A368BLC5 | MKIKVCGVTREKDIEALISANIDYIGFNFIESSPRKVSVDWALDMSRKYNLQDKFTCLLENPAAEEITKILDTNEQSNFQLYGNYEKPEKSMCFKPLSATNLQQNDLFQIKPIRNTIFLLDNMAGTLGGSGNKFDWSILGNVNLSNFMIAGGVGVEDLDYLSTLQIFGVDLNSKIEISPGIKDLNQIKLLGMLKYE | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Length: 196
Sequence Mass (Da): 22034
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A0A8U1BTU4 | MSARREDISHIVSAINNSAYYFTTSSCSGRILLIDGHSLAINSGFRNSGLTVDKKGKIITAVRSTHGLEVPLSHKGQVLVKEDYIYFLVEVANQKMEENVKQIQRFYKWLQSAFQPAEPQSPSRQETEEKSVYKERRKRGQTDV | Pathway: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
Function: Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of euka... |
A0A7J4BDD5 | MKFYDLHVHSKYSIGSNTIAEIAEMAEKLGLSVVAITDNFESLEKVKEIKAAIAQVKSSVELIQGVYITAATPQEMHQKIDKVRNLVPLVIVAGGDYQINRAACEDSRVDILAHPELQSFSNGLDEPCLQAAAANNVAIEINFHELLLSYKRSRAAILKKMMTNVDLCQKFKVPFVVCSGAHNIYEMRDGRELVSIATILGADLPKAFDSVTTIPERLIELNKKKLEGQIAAQGVEKIG | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
EC: 3.1.26.5
Subcellular Location: Cytoplasm
Sequence Length: 239
Sequence Mass (Da): 26279
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A0A497SCU2 | MNMKILEKSPKFVKFVLEKTTPAFANALREIMVAEIPTMAIEYVDIEKNTTGLFDELLAHRLGLIPLTFDSRLFNLKEECKCGGKGCSRCEVILTLEKKGPCKVYSGDLKSNEDSVKPTNPNIPVVELLEGRELKLQAVASLGIGKNHAKHQAAVVGYQYLPRIRIDKDKCNNCGVCVEKCPKKILQKKDGKVCIVNSMECSLCMYCVDNCEKRAIAVSGDEKNILFRVETVSGLTAPEIIKQAFNVLNKKLSIFKDGLEKAVK | Cofactor: Binds 1 [3Fe-4S] cluster.
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Subcellular Location: Cytoplasm
Sequ... |
A0A7C2H9E8 | MAVYICAACGKKFEIREKVQCPYCGYRIALKPRPAKEKVVMAR | Cofactor: Binds 1 zinc ion.
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Subcellular Location: Cytoplasm
Sequence Len... |
A0A8T5PJF1 | MKEYIEIIRPSIVFLSALGVMIGAIASKATILNLVLAIASVALISSAGIVTNDYYDYEIDKINAPHRPLPSGRISKKFAKIYALFLFIIGTAIASLINIYCFALAIINSFLEFFYARNLKRIALIGNATDSWFVASTFIYGYLASLGKELIIADNFYLIFIFSLLSFFANIGREIFGDIEDLNGDKKLGLKTLPIITSVKFSRFIASSFIILAVILSPLPFLLGFFSYEYIAIVLIADLLFIYSIFQEPKKNQKISKFAMLIAIIAFLVGILAQS | Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Function: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in th... |
A0A415X7S0 | MSQGILIFQAIVTIACIAFVLAAGIQKSNRLSKLMLIVAFLCLIENAAYLMEIQADSISAILLIMKLRYIGVAFIDTFFLLFCMRYSHKKIPKHLVGVMLVVDILVMISAWTSQYHSLFYRDIYYVTAGSLTYLHRVYGPVIYFNSVYETVQIFACAYLALKGWREAKDEKYRRSCKMLFFCVLLPFVVVPIRLSGLDRGYELIPSLTAVGMILFFSSAMVQDMFDIARVAHNNIFENMHEPIIIVDGNYGFVEANIKAKKLFPSLADQRQGQLLTETKLLSYLRTGIANKMYLGDQVYDVHIDQIYEEDVLMGYSILLM... | Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporula... |
A0A1X4XUZ1 | MSILIDKSTRAIVQGLGKQGILHTKICLDYGTKIVAGVSLGKTHIDGLDIPVFDCVWEALQYVKADTSLIFVPANNAKDAILEAQDAGIKQTIVITEGIPLQDMLIAKAFATKNGMKIIGPNTPGIISPKQCKLGIMPESIFDKGNIGLISRSGTLMYEIALLLKESSFGVSTALGIGGDPVLGMGFAEVLSLFENDDQTDCVVMIGEIGGTLEVAAIDTIKKMSKKVVAYVAGKAAPKQKKMGHAGAIVSSKDESAQAKIEALSNVCYVAQNPLEIVTLIKKILS | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level... |
A0A8U1GZK1 | MANVYSFDGLLVFGLLFICTCAYLKKVPRVKGWLLAEKRGVWGVFYKASVIGTRLHLTVALSCVTMAFYVLFLK | Function: Involved in the early part of the secretory pathway.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 74
Sequence Mass (Da): 8338
Location Topology: Single-pass type I membrane protein
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I6YPK5 | GIWAGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMMGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTMINMRINNMSFDQMINFITTMINMRINNMSFDQMPLFVWAVGITALLLVLSLPVLAGAITMLLTDRNINTSFFDPAGG | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A7S8CAW2 | MLSIIYACDENNTIGLDGDMPWHLPNDLAYFKRVTGGHHVIMGRKTFDSIGKPLPNRKNTIITRQQWDRDEDVSVVHDITEIKQYEKISEEVFIIGGGQIYAYALPFVQKIYQTKIHASFEGDTTFPLVNEEEWEVVFQEFHQSDEKNKYDHTFYVYERMKKE | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tet... |
V5WMZ6 | MTQNRQEVFSEELISSLLQISLEAGKEILEVYSRDFSVDMKQDDSPLTEADRRSHTVMQRGLENLSLSGKDSLEGEEDKNGSDDGGLPVLSEEGDISEYGSRRTWDRYWLIDPLDGTKEFVKRNGEFTTNIALMAPRDAGHKKQSHRVWEPVIGVVYVPVQDIAYVGWRNRAVGEGSPGSGAPGLAYQIDRLSEGVEGWKSRSVALGSSNEELTLTGPGIESPLRVVASRSHLNEATEEFIAGLESAYNEVELTSFGSSLKLCKVASGEADVYPRFAPTMEWDTAAADGVCRAAGLKVVQADNHMPLEYNKEDLLNPWFL... | Function: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
EC: 3.1.3.7
Subcellular Location: Cell membrane
Sequence Length: 330
Sequence Mass (Da): 36494
Location Topology: Peripheral membrane protein
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A0A1B9BAN1 | MSHQEQNPASVPGAGMPRTGVSNTGAGTPNANASNANASNANASNANAPSANASSANAPAASTAPSANMPASTPTASTPDSSVPQPQTVQLPHITAGHFENSLRGRLGIAGAGQRLLPRAQARAGWLVTLATGLVAALVRFVGLAHPHQLIFDETYYVKGANSLLRLGYEADWEGGTENDALFAAGDYSMQQTGADYVVHPPLGKWIMAAGQALFGQQSAFGWRFATALIGVFAVMLLVRVALRLFRSPTLAGFAGLAMALDGMGIVLSRTGLLDNILAFFILAGFWVILRDREATRATLAQRVARSPLRRKPLSVPLAP... | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Locatio... |
D3RRX5 | MDSSLDTQWLRDQRALARARGHRLTLWLRGSPEWTADEARRLVAALPEIDRVCLAERPILAEPSRPLRSAIRLMGMDLDLLILDVHDGFDPDGFGAATGAIRGGGLLALLTPPVAEWLRRPDPQSERISVWPFEPSGLSRRFIARLIAVLESDPTVVRIDQDRAEPMTASVAGVPSTLPHDRTYQPTRTDPARPSTPDQAEAVAAILKTAHGRPRRPLVLTAHRGRGKSAALGLAAGRLLIEGGRRLVVTAPRRDAVETLYRHAGAVLIDVERSTGQTRDGATALQSLVFRSPAELLEYDEPAADLLLVDEAASIPAPLL... | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Catalytic Activity: acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O = ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) + phosphate... |
A0A367YGJ8 | MDRFWTDVPPVTRAWSGAMSLTAALISLQRVKTVTLLFVPDKAFANESWRIFTSFCVSKGISLDLLMEIFYIRSSCGRVEDVFSTTHAILPERTVDAFDDTQRHTLRLFIDRNRAVDFLYFFIQVAASVLVVATVLYYRAGVGLFSLGHLLCRVFMYIDSQNSPHAEMNILGLFAFRRMYFPWVTALVDLVPNRAVREDVVKLIVLGDMAIWGNPKVWFYFTSIALGHFWWTCRELVLSNAHYDDDDQRRGVKRNAMLKYGVYKIDVAREFLMWLFIPPWYWVILAKIKNRR | Function: May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 292
Sequence Mass (Da): 34039
Location Topology: Multi-pass membrane protein
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A0A8T4A4Y2 | MDLWLIAVNAFWLIAPAYGSNAFPPLVGGKRSVDFGRTFRGKRIFGDGKTIEGSLAGILFGLLIGSIQLLFQPALSALISPYGPFIFLTLPLVLLLSMGAIAGDMLGSFIKRQLCIERGKPAPLLDQLDFIVVSILFTYLFFGMALEVIVFIIIVTPVIHYVANIIGFVLRIKKHPW | Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Function: Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal... |
A0A4Z1E1U6 | MTATSGHDPAQASEPDAEPGPAPTLAGRTVLVPRGGSRGAAWAHEVEARGGRAVLAPLVEIVGPVDDAPLRSAVAELTGGVFAWVALTSVNAVHALTALDARLGGARVAVVGEETGRAARTAGWQVDLLPERRTAAGLVEAWRDDVGPPPIDGSATGSRRVLLPLSVQAGDTLAAGLVALGWDPVRVDAYDVAPVPPGRAVVDAVAAGEIDAVIVTSGSVARRVAEVFGPLPDGVAIACIGEPSAQAARAAGLRVAVVATRSTGAGTVDALAQHYGPHRDIRTSLTTHDREDPT | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
A0A327X4Z8 | MFTKITYCLANLPLKRLPWLLLALFSSGLVAYALYTQHGPEQLWPCVQCIYQRTAMIGIALFAWLGFACAPGGGRTSALLRWFALVGWLTSAIAGAYSAYYHSWIQTALNPLFNPCQPHPNFPSWAPLHYWLPQVFDAGGLCGEIDWQWAGLSMPQWLFVIFTTLGTIALVVSMCYALRNRIQPSL | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Subcellular Location: Cell inner membrane
Sequence Length: 186
Sequence Mass (Da): 20863
Location Topology: Multi-pass membrane protein
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A0A482GX13 | AGTGWTVXPPLSAAIAHSGASVDLAIFSLHLAGVSSILGSVNFITTVINMRANGITLDRMPLFVWSVVITTVLLLLSLPVLAGAITMLLTDRNLNTSFFD | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A1M5SR86 | MSKLRMVGATALSLALAVAGPAFAAGIGGGGGGMHVGGIGGGGGMHIGGVGGGGAMHIGGIGGGGAMHIGGVGGSGTMHIGGVGGGGAMHVGGIGGGGGMHIGGIGRGMHVGGGGDGMHVGGGGFRGAQASIGDGRVGSVSGGNFTGHSDGQFAHGGYRGDRDRRHGYDRGVGFAGGLAAGSALGYGYGGYYDPYTYFGYYDPNYYNDGYAYNDPGYDGYSGSVVSSGADPSYCAQHYQSYDPVSGTYLGDDGLRHPCGKNQERAATAAIAQPAGSGNPAAAPSMNSDQQLLPEAPVGQRQPPADQVTSEKNLMNPNDPV... | Function: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport.
Subcellular Location: Cell membrane
Sequence Length: 338
Sequence Mass (Da): 33108
Location Topology: Single-pass membrane protein
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A0A4U1BJD2 | MPKKSELAYRIFTLGLKKELSVMNRDWEWLKQQFAAISRLEHAFALMEWDQATLLASGGQRARGEAMAELQLVINQRLQSPKLEDALSRAETALSLEQKRMAQLMRRKIEEAAVLEDDFVRRRIELSVACESAWRTARVEGDFTRFERAFAPCLALLKEEAQIRRTDQSQPLYQALLNKFEPDLSVAKLDELFAPLKAQLPDLIRQASEHSAGRSRQPLPHVDAVKQQKLAQLLLKPLGFNTERGRLDISSHPFTAGVASDVRITSRYDETNPLSGLYSLIHELGHGCFEQGIAHRWYNTPMVKVQSAALHESQALTFEM... | Cofactor: Binds 1 zinc ion per subunit.
Function: Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.
EC: 3.4.17.19
Catalytic Activity: Release of a C-terminal amino acid with broad specificity, except for -Pro.
Sequence Le... |
A0A1L8QVA9 | MNLKPITHSFLVLFLTISSLLAFPLDLFAETVTTPDDFSIEAKAALAVDMQTGTILYEQQSEERMPVASITKLLSLYLVQQAIANGELRWDDNVTISSDIATLSQNLALSNVILEAGETYTVEELFETAVILSANAATVALAELVAGSEFAFVDLMKEQLTTWGITDFVLVNSTGLNNEDMTTPLYPSSNPTDENEFTAKDIAIITRHLLQDFPETLDYTNKASAVFESKSGGPATMYSTNWLLAGMPYEKAGVDGLKTGTTDLAGPSFVGTIEKDGRRVITVLLNAETSEARFSETSRLMDYAYNQWAYQTILNAGDEI... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
EC: 3.4.16.4
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanin... |
A0A1I2A9A1 | MNIIAACIDYNSARLEEREIFSFTKSEVESFYKVLGNIDIIQGAALINTCNRTELYLSLKDAVTADPFKLLCDAKGVGYDENQHLNKYFSGDGAVRHLFMLAAGTESQIWGDAQIVSQIRESIVTARENKAADSVLNVLFRSAVSAGKKVKTLIDFKLNDNSTALRAINLIKERSDIKDVLIIGNGMIGRLVGELLVREGKNTCMTLRQYKTGAISIPRGVDTVNYANRYEKMQGCQAVISATLSPHYTLEREKLNEFDSLPCLFIDLAVPRDIDPEIEVLEEVEYYNIDDISKGARDESKEEQLKEIQEIVFEFEEDFY... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tR... |
A0A8T4KYJ0 | MIEFINNLNSDDTKKFGKKACHLAKLCQNDIRIPKGFVISTDINEKNFLYFQDEILDFFERLNSNYVSVRSSMTMEDCKEHSFAGLFDSYIKVTRNRLFKNIINCWKSIKSERVKTYCNFKRIDYDSLRMAVIVQYMIEAEKSSIVFTQNPVNKKNEIVIEAFKGPCKFIVSGKIGPCRYYINKSDFHLETIESKKEISTLDESDINEIKKISLYIENIFNFPQDIELVKERNGKWWVLQSRPITCL | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 247
Sequence Mass (Da): 29062
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A0A7C4DFS0 | HRMKLKNLLPSLREKKRYVLFRVISEEKIEVHQLKEAFFSNMLNMFGETGVAQIKARFLDKLWDPERQIGILRVNHKEKFKVIVALGLILRIGESRVNVKIYKISGTLKSLMEKFKDRKELKN | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
EC: 3.1.26.5
Subcellular Location: Cytoplasm
Sequence Length: 123
Sequence Mass (Da): 14580
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A0A2A5CHC2 | MDRIIAATNINWFSVSIATFSKFFIDRTWYRLMLGKSRLLALSLVGLLLMGCQAMNPAQSIAPMHHPLDPLTADEYSQATSILRTAGYINDASRFATLDLQDPPKQSVRSWQPGEDFNRSAFAIVKQGSQTFEALVDLSNSSVLSWVEIEGVQPSLIVEDFIDSFRALAEDEGFIAALARRGLAPDEVACSPMTVGNYNNPVYAGRRVIKLPCYALEGEGSRFTRPIEGLWAAVDVNTQQVIELVDEGIIPLSETPASTSVAATNRQALKETVLYQPDGANFTVNGHVIEWDNWRLHYRMEKRSGLVVSDVTYRDGDRDR... | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
Catalytic Activity: an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+)
EC: 1.4.3.-
Sequence Length: 690
Sequence Mass (Da): 76587
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A0A485D6D4 | MVTRTWVGTSKPISTPGDYGMGTLTSPIVRGKDAPANSVLLDETIADYTGAPTTIPHAIAIFERYAGPEYKHQEMGQPNVSTERRELVVRWISTVGNYDYIFDWVFHENGTIGIDAGATGIEAVKGVMAKTMHDPSAKEDTRYGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPEVKPNTAGGPRTSTMQINQYTIRQRTKSGAEVRPGHHSPAE | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 221
Sequence Mass (Da): 24267
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A0A0T7E9F4 | MENKITNTGGCPLHNKRVVEDSMVTDLDTINSYGDFLHLDRLLNLQNSFSESHEGMLFVIVHQVSELWLKLVKHELAVVIDYVKNDEVAKAQKGLARILCIQKQLSTSFKVMGTMTPVDYDTLRNLLGEASGFQSYGYRAVEFMLGNKDRNMVELHRHNKEAYEMLDQLMNAPSLYDEVNRLLVRNGIEIDKSHLNRKLAAPYEANQSVVDAWMHVYKNAEEYWDLYQVGELLMDVEDNFQNWRFTHMRTVQRIIGFKVGTGGSTGVGFLKKALDIQFFPELYTIRYEFN | Cofactor: Binds 1 heme group per subunit.
Pathway: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
Function: Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-... |
A0A7C0UW69 | MKIKILKKSDDEIEFEVTGRTPAFANALRRTMMVKVPVLAIEDVIFTANDSPLFDEVIAHRLGLIPLKFVPKTFNRRDECSCGGEGCINCQVVFVLDKTGPCTVYSGDLKSTNPEVKPLYDNIPITKLGENQKLKLEAVAIMGTGKEHAKWKAANAFYQYEGDKFKFTVETVSGLSPKDIVIQATEILESEAKELKKAL | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
EC: 2.7.7.6
Subcellular Location: Cytoplasm
Sequence Length: 199
Sequence Mass (Da):... |
A0A8T4K911 | LSPSARKIGTTGRGIGPTYMTHAARVGLFVSDFYRPASYVISRLKDLDEEFSVSERLERSGERPIDARKVCEDYAAMFGVLRPHVKDTVYYLNRELDKGTRMLFEGAQGTFLDVDLGTRPFVTSSRPISGGVAAGLGVPPSAVTEVVGVMKAGYLTRVGSGPLLAELGTEQSIKSEKRLKQASEEFMDLKRKVAHGTANDFETGKYHRNEGDEYGASTGRPRRVAWPDIPLIEYAAMVNGIDWLALTKIDVSDFVTEIPFITAYDLDGRQTREFRGVNYENYKPVLGRRVRGWMQSTRGTQNYGDLPEGAREVVEIWNSI... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
EC: 6.3.4.4
Subcellular ... |
A0A8T3Z985 | MKIILFGPPASGRGKIGREVAKSLGLRLISSGYTLMKKAASDPTLSDYMRKGEVFPDKFVNEVMSKEIPMDGGFVLVGYPYSPEQARFFDASNKIDAIVEFQMGEDVIMKRVAYRVVCSDCFVSFNMSTDKPKTHGVCDLCGGVLVKREDDTPENLKMRMYYYEKMSKVMNDHYRTAGVPIVVYRVDPSATPSENASMVLAELRRVGITGEKSS | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
EC... |
A0A8T3ZGX4 | MIRDIRAIFRRRREREISSIVDMYHQDEGNAKIYLPDGHLYKGRGEKIGAGEEIWKYTKLPYGTLNHANYEDIGLKIGDALFLDPEELKALGYSTDDMSQLLIIIRRPQQIPRSVRDEGMGITGKDWSADMLDIPLINGNGKNEDEYEKWYVAELNERGIETPGSLKYRPSHLVLAFPRHYGIKTYEDAKMQVELLSRNLRVASEFETLARSVMRKRLGLGDRQYDLTVTHGKTETFAISGDSDCIIDVAESGNGLMDNRLRAINPPVMQTSTPYFLINRSTREKFPDFTKELTERLYEGRDEVKKKHPSLFEDKLDKRI... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
EC: 2.4.2.17
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
Sequence Length: 352
Sequence Mass (Da): 40666
|
A0A8T4DZ78 | MRMFIEKSVLSKIRTELLVLPFSEEDVKKISKKAHKYREITDSVKSGDFTGESGKSVLLRNIDGKKRILLAGMGKEKEIDQEGIRKACAHSLKVAKSLKLKSLSVLCEGFGKISGPKAAKSIVEGIILGNYEFDKYKQEDRKKKKDVEEFTVYYNEPDMSEVRKVAKETRTVCENTNWVRDMVNEGGDVIHPDRIARIAEGLAGKSRLKIKILDEKQLRKMGMELLLAVGDGSRYDTKMIVLEWNGSKAKEKVALVGKGITFDTGGLYVKPSPYMDDMRCDKAGALTVLGIMKTVSELNLKRNVVGIMPLAENMIGPKSF... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
EC: 3.4.11.1
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xa... |
A0A4R6FZ57 | MISRRNFLASATTILGAGFVSKAGAAGIPEAQIIQHAQTLPPKAPSTGRPFNPVVTLNGWSAPWRMKNGWKEFHLIAEPVIRELAPGMKATLWGYNGSSPGPTIEVVEGDKVRIFVTNKLPEHTTIHWHGQRLPNGMDGVGGLTQPQIPVGKTFVYEFEAKRPGTFMYHPHAKHKFSIMDIQTQHDLVWTYRFYG | Catalytic Activity: Fe(III)-[cytochrome c] + H2O + nitric oxide = Fe(II)-[cytochrome c] + 2 H(+) + nitrite
EC: 1.7.2.1
Subcellular Location: Periplasm
Sequence Length: 195
Sequence Mass (Da): 21683
|
A0A8B6ZLF5 | MVRSRLLLCLLSTAALSLLAGSSAFLSPHRLKGRFQRDRRNIRPNIILVLTDDQDVELGSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSPSWQAQHESRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPPGWKEWVGLLKNSRFYNYTLCRNGVKEKHGSDYSKDYLTDLITNDSVSFFRTSKKMYPHRPVLMVISHAAPHGPEDSAPQYSRLFPNASQHITPSYNYAPNPDKHWIMRYTGPMKPIHMEFTNMLQRKRLQTLMSVDDSMETIYNLLVETGELDNTYIVYTADHGY... | PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity.
Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Exhibits arylsulfatase activity and highly specific endoglucosamine-6... |
A0A1I4X5X8 | MVFRSVSLNYTRNPSRRFEIDVGIGVNEDLLLAQEIGCAELAGVDGVMAEPPPRALIVALGDSNVQMRFHGWVDQRAHDFGQVRSEAIRRVKLALEAAGMDMPEPIYRVQLRDESARIPGPPLHHTAVAATAEADTRINTDLSTQIDREQEESANHDLLDPAAPREL | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
A0A7Y8HN19 | FDTAGLIAMANIGPNTNTSQFFITTVPTSWLNGNHTIFGKVIDGYDIVKKIENTKVGAMDKPVEEQKIIKAYVKEKKD | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 78
Sequence Mass (Da): 8645
|
A0A257GTT3 | MAKAIFDLEASGRVIKAPRPRARRNQYQLGVAELLGAAVRNTLNKSVGLARSLPMIARSAKSALIPDKGSNGKRDWSLPKDFKLFAPRTSLNVAITNQRTFAGRTVPLAEVKQIAKLLGVSLNDVVMATTAGGLRAYLKENNDLPTKPLCAAVPVSLRQEGDTTSNNQVSMVTMNLATDIKDPLERLMKIHADSANTKEMMGRFKAAIPTDFPLPAAPWLMSA | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 223
Sequence Mass (Da): 24136
|
A0A4U1BRN8 | MKRLFLGVAIASVLAGCTTPLERRQASGEFDYIEQPEPVELKVPADLTPPSVSEEFAIPAKTESAQALGQRIDVRPPLQVLPLGESIRLQEGTDSITVLIEDQAGDRNLKQELMTNLKEFIEHKKIGVESIDEVNGEIVTQWVETVEEFGGSWWGKDEYRMRQKYKFDVAVKDNGRTGSLSIELLGHEEFIEDVDQDINLTDSDKRRYAIDMLNSSISYMNFKRQQEAKIAQVKDASGLSITLGKDANGNVTYDTPADFERVWSRMEKLLPVIGFTVKDLDKSQGTYYVDYDPNDGFWASLWGDNDLLALKSGAYQVSVQ... | Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 361
Sequence Mass (Da): 40540
Location Topology: Lipid-anchor
|
A0A845GS92 | MLYLVLKALHVASVITWIGGMLTVAIILACNRLQHSQVIYWLSGLRAWDRRVTTPAMLLAWVLGLGLASLGHWFPQAWLMAKLGLVLILSGFHGMLVGRLRSLSSRPLAVALPGGFATAIGIILAAAIITVVVITKPHVY | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Function: Catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX.
EC: 1.3.99.-
Subcellular Lo... |
A0A8T4KRZ4 | MIVSITGVAGTGKTVVSKLLAKELKWKFIKLDNLAKRKKLFLFYDKERRTHVVDMKRLKKEFNKESRKYDNVVTESLYSHLFPSDILIVLRCNPKILEKRLKRKYSWSTKIKENLEAEMINLITEEAMEIKKRVYEIETTHKTPKQTVKSIREVINGKTAKYKAGRINWL | Function: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates.
EC: 2.7.4.3
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Length: 170
Sequence Mass (Da): 20088
|
A0A846NIK0 | MPATVVVCTQWGDSGKGKFVDYLAEDADLIVRYSGGNNAGHTVVVGDEKFALHLIPCGVIRGKRVAIGNGVVVNPHVLKDEIDYLESRGINVDLTVSERAHVITEKHIEKERGESRIDTTKRGIGPCYEDKIGRRGTRMIDYAKEHKEFQEMIGDVSLLVNEALDRNEHVLFEGAQGTLLDIDHGTYPYVTSSNPIAGGICTGVGISPKRIDRIIGVAKAYVTRVGKGPFPTELGTYEKTKAEGRWEEIEPNFEEQLEDALKRANGGNKYYQGKYMRLQGREYGTTTGRARRCGWFDSVAARHSCMINKPDEIALTKLDV... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
EC: 6.3.4.4
Subcellular ... |
A0A842QBV6 | MKDEVIWFTELGKDKDSMGGKAFNLMKMSDMGLPVPEGFVITQNNLSNGIDLILKEYKKLLEKYGSVSVRSSANVEDSEKASFAGIFETTLNVRNKNELLISIKKCFDSIREPHVKNYSKRKGIDPGTVKMNVIIQGMIKANKSGVIFTSDPSGTRNIIIEASDGFGENVVGGKKIPSRYLVDKFTGEIVESKENSTILNDNEISELIKYAKILEEKCGRPQDVEWALDEGKIYLLQTRPLTV | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 243
Sequence Mass (Da): 27105
|
A0A0F6NRF0 | TLYFIFGTWSGMVGTSLSMLIRTELGNPGSLIGNDQIYNTIVTAHAXIMIFYMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALTLLLMSSISDKGAGTGWTVYPPLSSNLAHEGTSVDLAIFSLHMAGVSSILGAMNFISTVINMRPTGMNPXRMTLFIW | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A8T4DXI6 | MAGKSRICNVIEILFKYTEKYSLPVAELSKEWRADPFRILITVMISSRTKDEITAAAARRLFSRAPQPDEIERMGLPEIEALITPVNFYKTKAKRVKEISARVRMDFKGKVPDTIEGLVTLPGIGRKTANIVVNAAFGKKSIGVDTHVHRIMNRLGAVQTKIPLETEMALRKLIPESHWDLINVPFVLFGQNVCTPLSPFCSRCPVEKYCSRAGVKKSR | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the ph... |
A0A0A0N9C0 | MHDETLQELVAVQIVLSTVAGGGEPAAMKEAINQARGLVANQITSLRHLIVEMRPFALDQLGLAPALETLCRRTGETFGLEAELRVGAEWSRLGDELSPEAQAHIYRIVQEAVNNAVKHAQASRLLVELHSDDHAIKVAVRDNGRGMAHQPSTPVGRSALGTVVSTGTGLSAMRERGHLLDGHLTVDSTPGEGTRVSLLIPRHAKRRSRPKDSASA | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
A0A7J2MZB3 | MFGRVGEAIRESLRKLISRGYIDEKTLDSFLDELKKDLLQADVEITTVKEFIKEVREKVLKEKDKGFSIREVVIPIVYEELVKLVGEGEKIEVREKPFKILLVGLFGSGKTTTAGKLALFFSKRGYKVCLVCLDVFRPAAYEQLEQLAKKVKVGFLGDPNEKDPVKLVRRFEGEFEKYDVVIFDSSGRDALDESMIKEITSIERELRPQEVILVMSADIGQQAKEEANAFHEALKITGVIVTKLDGTAKGGGAIVACKETKAKIKFVGTGEHLEDLEEFEPKRFISRLIGLGDLETLLKKAKEVIKEEKAEELKEKMTSG... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP recept... |
A0A8B7AN60 | MAQGLIEVERKFIPGPATEERLQELGSTLEHQITFRDSYYDTPELRLMRADHWLRQREGSGWELKCPGAAGVSGPHTEYMELTAEPAIVAKLCEVLGAEVLGAGGMAAVLGPLGLQEVASFVTKRSAWKLVLLGAEELPLRVDLDTADFGYAVGEVEALVHEEAEVPTALEKIHSLSSLLGVPAQEKPPAKLIVYLQRFQPQDYELLLEVNRSRETTGSQTSRQ | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Hydrolase highly specific for thiamine triphosphate (ThTP).
EC: 3.6.1.28
Catalytic Activity: H2O + thiamine triphosphate = H(+) + phosphate + thiamine diphosphate
Subcellular Location: Cytoplasm
Sequence Length: 224
Sequence Mass (Da): 24620
|
E1SK09 | MPQKIYWIDNLRAVACLMVIVIHTTTWYITGPMAVTGTTWDVANLLNSASRVCVPLFFMISGYLFFGERSAQPRHMLRLVLCLLFYSAVSLAYITWLTPISEGRSILKMLQKPVFYHLWFFFALIGLYLMSPLIQVKTVQARYVALLVLVLAVLANPNTASQSLGPFHFLPVNLYVSGDSIYYLLYALLGRAIGTMDTTRRGLTPLAAGLFIACVIGITLGTKKALIVNGAFNDTWYLYCGPLVFIAAISLLIVFKNSLNQRTLPGFTVIARYSLPIYGFHALFIHYLRTHHYDDMSRPWLDLPWVFGLTLGGSLLLGMA... | Pathway: Bacterial outer membrane biogenesis; enterobacterial common antigen biosynthesis.
Function: Responsible for the incorporation of O-acetyl groups into the enterobacterial common antigen (ECA) trisaccharide repeat units.
EC: 2.3.1.-
Subcellular Location: Cell inner membrane
Sequence Length: 331
Sequence Mass (Da... |
F4KL57 | MSKQTKSQRLSVIADLLRTHEVTDQAMLLELLRGRNISITQGTLSTYLSELGATKGVRPGSFKSCYQLPLMPQADAVTTQPTGLISPTVGFRSYAISGQMLVIRTEPGFAQSIATILDSSLSSLSLGSVAGYDTIIVALAEEATDGEVIDWLHQIIPESILAIGR | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 165
Sequence Mass (Da): 17679
|
A0A6P8WGM7 | MWFEIIPGAAIITVALSVPIYAMYGLQKLTMGNAYRRNMDERFSRVMYQRDFRLTNNPYIMNGLDEVPDEDQNEQKNNQGANN | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
U3AW27 | MEKCHLFGWGCLTLAASVALLSILSNQEPDHRSASLQSPSQLDTELDVSSVKDFFEYQLSTQGEQTLNKIIHNFDSDSSVAVFEGSVEQDLFHRYIEYKQALLDLNPLPSSQLSLQHLIEIEGVITTLQDKFFTHSEKDRLFGQQNLLRRFTIQKQEIIATTHDPLLQQQLLDDLLSQQPNYIQQVNKNKQLIMQLASTSQLNLQDKYIQHVSLVGEKGAKRLQDLENQQRDFQAALNGYLQQRDDILEYDGLSTEQKNTEIALLRTQSFAEQQQRRVQALERIYDNQR | Function: May be involved in the folding of the extracellular lipase during its passage through the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 289
Sequence Mass (Da): 33322
Location Topology: Single-pass membrane protein
|
A0A2S6GMJ1 | MLVSGSAQRWLVTGACGQLGAHVTDRLARTGARVLGVARRPCRAAHGATVTLDLRRHHDLAALLRRYRPTHIAHLAAVSAPGAVARDPGLGWALNAETAERLAEYAHRERAWLLYPSSDFVWDGTARRRYRESDRPNGDTAYAWTKVGGERAVLQRDAGVVARFSLLHGDPLCPRETTWTRLAAALKRGDEIPVCVDEFRTPLTLTDAADTVIGLGRRRARGVVHVAGPEVLTAKDVVARMAERLGVEPNLRTVGRHELPGGHDRPRNMAMATEVLARRWPDLLPGPLRARAPFGVVIPVYRGADVLARSIRSLAAQTFD... | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 557
Sequence Mass (Da): 60159
|
A0A4U8V7D2 | MSALEWRAGGSLASIFALRMLGLFLILPVFAEYARTLPDGHDAQRVGLAMGIYGLMQAFLHIPLGALSDRIGRKPVMLFGLVCFIVGGIVAAMSDTLLGITIGRAIQGTGAISAAITACLADLTREQHRTKVMAMVGGSIGLTFALSLVIASPLYRLMGMSGMFWLMAVLGAIAIVVVLFGVPTPPALSPADRTPFRVVLANPDLLRLNVGVLALHAAQVAMFMVVPSMLTDAGIALTAHWKVYLPVVLVSFVLMVPPMIWAERHGKVRQVLLAAVAMLTLAQLLFAQVHAMWPIVGALLLFFFAFNILEAMQPSLVTRF... | Function: Resistance to tetracycline by an active tetracycline efflux. This is an energy-dependent process that decreases the accumulation of the antibiotic in whole cells. This protein functions as a metal-tetracycline/H(+) antiporter.
Subcellular Location: Membrane
Sequence Length: 391
Sequence Mass (Da): 41428
Locat... |
A0A564TL75 | MDSFEKNMHKKRNYSKILMVALLLIVTCCPVSVLAKNKNSLSAQKNHRLLFISSYSYNWSTVPLQIEGIQSKLDSNISLDIEFMDTKQINTKMAEQLLYDKLRYKEQHDGEYDAIIVGDDAALVFAMLYKDELFYKTPIVFEGINNIEYAQEVSQDPFVTGVIERSSYKENLEFAKKIEPQAKKIVAIVDNTVTGIGEQQQFYAQEEEYPEFTFDVINGSLLTQQQILDRISAIDKDTILIYLILSEDVNGNIYTNEQVCQIIKEYAKVPVFRFVQAGIGEGILGGNIVSHRKSGEIAAQMVMEIFKGTDPSGISMLDES... | Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporula... |
A0A8B7ADB2 | MLKRELKNLLFSLLLLDKSSLPDDHHIAKMIVTLIMSISDVVNQDLVMGAHLGVFFLENYHVSLAKKDISAVNLSDQISTAFIEASGTGNMKFMLNGALTIGTMDGPNIEMGEEAGEQKLFIFGMWVEDVDKLDQRGYNAQEYCDHIPKLRQVIEQLSSGFFSPKQPDLFKDIVNMLRHHDRYNVLVDYEAYIKCQEKVRALYKNLRKWTRMIIXNTTTSDKFSRDRIIAQYAGEIWNVEPSHQLLPDETV | Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
EC: 2.4.1.1
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + phosphate ... |
A0A066W3S5 | MLWFFSALIALYFFSRRAEALSIKETSTAFELSNGRLSASMAKSSGVITTMTLDGQDLLGTGRGLYLDCSCTPAGFYTPGTSNPIIKSLNGTDSTGIAIPLASYYRTHIPRLANYSSTGQLTIMRRLAPPMTICGWIHHQWYNLRSLACPIHSDLTVDGITYNYMGLTALLALSSTTSTREKTRRYANPEWNTAFYDSIAASVPNYVTTSHRGTFSLSIDTPAGAKKTIAILSENGLDPQDNAQNISAYQYWGDVSDNGLLSIPRVKEGTYRLTVYADGIFGQYAEDGIVIVAGKTTKHQAKWTPETAGKELWRIGTPDK... | Catalytic Activity: Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end... |
W9WY13 | MARARQIIFRIFYSTSFTAVFLILVIIVSVTPADTLYESYKRSRLIDIFLIAGDYVVTALLAALIYASRLYTNRSVLKDIPKTYMPIEKEDLPGRRVHKLIQECLEKSAVIAYQARPRSRRIEHDTVIMGTRMLALTKTQTNTDQNAEPSWGKVAHPGWSSPASKELPGLEYCTVVDELIDLIEAKAVSLAPLDPHTQPDPDGTPRPDPRVIDRLARNGNMGMRAYLQYLIDVGVVPDNSLTVAFLAAYERARFSSAPLSDEDFQSLMRMFAELLRNMNPVDVEFLDLADDSEYPSQSETSSLIRRRMPYRSPHTDAETF... | Function: Required for growth under high-pressure and low-temperature conditions.
Subcellular Location: Membrane
Sequence Length: 372
Sequence Mass (Da): 41655
Location Topology: Multi-pass membrane protein
|
A0A8C4S3G1 | MMKIRKHLRGSGRVLAFIFFASVLWLLFDMAALRISFSEANSKLNKKEMKLLEKVRQGQKEPASHAPLLRKRPIGLLSRKEDRPRVEAGERVAPPKLDKLQKKKGKVFFAADAAVGGGTPVGNAQLVLNKTGGAEKARTSPHVLDKERQPKVYNKTESEIQRNKPTGFSKDATPGRAQQGNRSSHSPGNPKVALGTAKDSKQATEHVVPATGHDHKKLGQNESLGAEPESEGKASRLVIKAERSAPNKTQGSRDENAAKFGVGPPGISERNITGAPNKVTRLDTGKHKVLPVDLTSNPRNPEAPGQFGRAAVVPMEDELK... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 807
Sequence Mass (Da): 91444
Location Topology: Single-pass type II membrane protein
|
A0A2S0KM89 | MRKCLIASSNVNKAREVQEILKDFNFEVLTTHDVEEELEVIEDADSFTGNALLKAKAYHERYPEYYILADDSGLMIEALDGRPGIYSARYGGDLSYPEKFKLIWSELAETGVDPNEWRAKFVCAIAWCEPGVSLSGEVDARVFQGEMHGIILDEARGENGFGYDPIFYLPEFGKTNAEISAEEKNKISHRGRALSELQKYLKN | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
A0A968KID9 | MKDVPVLLPIELGLAVILERDTPLDALVSKNGLPLAELPPGARVGTGSLRRSSQLLQIRPDLEIVPLRGNINTRLRKMETENLEAVILAGAGLRRMGWDHRITELISPDLLLPAMGQGAIGLETRKNHPELQHLLFELDHEETHLALDAERAFVRTLEGGCQVPIGAYATLDDQGGLILRGLVASLDGKTVYRKEKHGPAIDGPRVGRELAEDILSMGAGRILQEIYNPPDS | Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
EC: 2.5.1.61
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Length: 232
Sequence Mass (Da): 25291
|
A0A1G3L2C7 | MNETLKSGLETLGCPEIYEKLLEYFHEIKLWNTRYGLVNFSEDRELIVKHFLDCLAPLEPFKKWGSLRFADIGSGAGLPGIPLSLALPECRFTLVEKQAKRVRFLENTQLMVGLPNVEILNVNFESLESSYDLVTFRAFTPLDTEVVLKLLKLVAPGGRIAAYKARKQSIDLELKALESLNLPLEVIPLKVPFLDDERHLVVIHKV | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 206
Sequence Mass (Da): 23389
|
A0A1G3LAW7 | MRATRAVINLTALAQNFQEIKEFIGPNKKICVAVKADAYGHGAVQCAKTLSEAGADMFGLATAEEARELLQYGISTPLLLLGLVCPEELPELIDGGVALVAGDRDYLEKIWKIAATLNKPVRIHLKVDLGMGRLGCQPEEVLGLAKAIFCHPFTQLEGFCTHFPSADNHQPQPTLSQLSHFNDLVKSLEDAGLRPPLVHGANSAALVEFPESHGDMVRPGIITYGYLPDEGLISPMKLTPVMSLETRVSFVKDVKKDSTISYSGTYETLQDTKIATLPLGYADGYFRAFSNLAPVRIGDGIYKVSGRVCMDQFMVDLGPE... | Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
EC: 5.1.1.1
Catalytic Activity: L-alanine = D-alanine
Sequence Length: 367
Sequence Mass (Da): 39911
|
A0A0Q7EF09 | MSSCLPSLPLEPIPVRERTIALVGLMGVGKSTVGRRLAKRLDLPFADGDVEIESAAAMTVSDIFAQLGESEFRAGEARVMRRLLEGPRMVLATGGGAILNPETRDVLKNRAVTVWMRADLETIAARVQRRDTRPLLRGRDPLEALRQLAEARYPVYALADVTVDVAGGAHATAVDAIVGALEAYWAREAEVKA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
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