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stringlengths 6
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A0A7V1BTS1 | MTAMDERRTSNRAVIALDAMGGDQAPEVVVAGAVSAAGPDIKVILTGRTEEIERCLTGVDEEKRRHLEVVDAPDVIGFDEEPAKAVRGKPRSSLVAAVETVAQGRAGGIVSAGSTGATMAASLIKLRRLKGLKRPGLCVVIPTPGKPTVFIDVGANSEVRPAHLLEFANMASIFASEVLDISDPSVGLVSIGEESIKGNELVLEAHQLLAASPTLNFYGNIEGHDIVNNLVDVVVTDGFTGNVCLKLMEGTSLVVIEEIKKAARKGIASKLGGLLLKRNLGELKESIDPEVYSGAYLLGVRGLVVVCHGNSSSKAIANAVRITARAVEHEVVGRIGDRIASLARTSP | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
EC: 2.3.1.274
Subcellular Location: Cytoplasm
Sequence Length: 347
Sequence Mass (Da): 36347
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A0A938FEK1 | MQREDEHERQERWPMTDVIEGPVTDTGGERPSGNIFSRFGVFLRQVGAELRRVIWPTRKQVVNYSIVLLVFVVIMGLYIAGLDFIFTEGVLFVFGR | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 96
Sequence Mass (Da): 11090
Location Topology: Single-pass membrane protein
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A0A965BM58 | MIATKSIALFGGSFDPIHNGHLFVIEELLSSARFEKFIVIPAGNPWQKSVAASAAQRLAMVEIALKDCMSKYRELEISRFEIDDSKPSYAFQSINYFTMQNPGDNLVWIIGSDAFAKINQVWRIAYFLHSPR | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 132
Sequence Mass (Da): 14946
|
A0A972PVV6 | MPQGEPNTGNDRPAVVFAGSGEFSADLLRELARIGFLPAMALTRRDRPAGRGRRLRPTPLKAAAAELGVEVVEADGPSDPAFMETLEALRPEVLLVADYGFILPKAVLSYPSRGCVNVHPSLLPRHRGAAPIRRALMEGDSESGVSLMLMDEGLDTGPIIAASAVAIEDRDNELSLRMRLAATGADLVARFIPLWVAGDVEPCPQGEEGASYAPPISPEELLIDWALPSREIHNRVRALAPRPGAHTFMRGKRLKVLRSEPCRVEWRLAPGEVSLAESGALVVGTGEGALRLLELKPEGKRSMLAEEFLRGYRPSEGEILGPKAP | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Length: 325
Sequence Mass (Da): 34989
|
A0A2G4F6W9 | MPGIVGGSYFYPKIRRLFPIYSVPRVSPDLQPRHGPPGQPAASPMNPIVALHGFTGQGADFDPLRATLPPGTSLSAPDLPGHGSKSLLRDLPAYSLPAHLDIISQAATAPQITLIGYSMGGRLALHWAIAHPERIRRLILIGASPGLATPEERDERRLGDATLAEFIRTRGLEAFFKYWHNQTFFQPMLHLPKEHLDPILARRAHNDPEGLALSLENIGTGTLPSLWHRLKEIRFPVDLVSGEHDVKFTRLAHEMGAHLPKARHSLIEGAGHAVHLEKPSDLAMLLQ | Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 3/7.
Function: Catalyzes a proton abstraction reaction that results in 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC).
EC: 4.2.99.20
Catalytic Activity: 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate = (1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate + pyruvate
Sequence Length: 287
Sequence Mass (Da): 31537
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A0A7Z9SKK3 | MFDSVLIFSALSLILGLILGYAAYKFKVKGNPLVDQIDVILPQLQCGQCNYPGCRPYAEAIASEEAKINQCPPGGQEVVDDLAELLNIETMPLNAEEFGETQPKRVALIDEPICIGCTLCIQICPVDAIVGATKTMTTIIADECTGCDLCPPVCPVDCISMVEIKPSLGAYVPNVAEIAHA | Cofactor: Binds 3 [4Fe-4S] clusters.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell inner membrane
Sequence Length: 181
Sequence Mass (Da): 19317
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A0A3D2HGZ8 | MDLSLLVVGLGNPGKVYDRTRHNVGFYLVDTYVSHQGGTWIQEPRHSGWLSVIYTPHAKVLCLKPTTFMNYSGTAVRSVCDYYRIDLQNVLVVCDDISIALGHFKVSIKPGSAGHNGIKHILECCGSGFARYRVGVGGKPQGMRLDDYVLAKFSPEEQAKLPEVAAAFEKNLEVFIDKGILKGLNFIERL | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
EC: 3.1.1.29
Subcellular Location: Cytoplasm
Sequence Length: 190
Sequence Mass (Da): 21045
|
U4LRU4 | MSRLALRTSQLLTLCRQCVPHARRLPQSRLRYLSTATVDSVADSAPIFADLQKSQKRALKDRHKGAHPSSSFSEGDWEVTCGLEVHTQLNTKTKLFSYAKTSITAAPNTCISFIDAALPGTQPTLNPAILLPALRAVFALECTPAKVSRFDRKHYFYWDQPAGYQITQFYEPLAKNGRLVLTPDADGVDKRLELKIRQIQIEQDTGKTIAAPPNSLVDLNRVGSPLIEIITDPFPLDSAETAGKVLAKIQAVLRAVDACVVGMEWGGLRADVNVSVRRRGDPNTLLGQRCEIKNLSSFKAVTDAITSEAARQIEILEAGGTIEGETRGWDNEKSTTRRLRGKEGEVDYRYMPEPDLPPICLTSEALEAVKKDMPLLPDQIITQLTDVFGLSPKDARTLLLWDEGRSGHPDSVISYYKNVVGLIQSAPGVGKIVGNWVIHELGGLITTHGLSWQKNPVGKKRLADLVSLIVNGKITNPTAKALLPRLFTDKRIPAEIVEAENLGIKEMSRNELETIIKEALDTDRGRDVLKQLVEMKGDDSKAAEKKKKGLRGFVLGGVMRSQGGKVKADQVESALDSLLEKL | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
EC: 6.3.5.-
Subcellular Location: Mitochondrion
Sequence Length: 582
Sequence Mass (Da): 63949
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A0A3D2HHD0 | MSLPSSGLAQYLSPERIPLAVRQYIAAHEGPLCVACSGGADSRATLVLVRLLWPDRPCILLHFNHRIRPESEAEEQALTAWARQWSIPMIVGYRKDYESTTEADLRAARFAFFEAQLQAHGSQILLLGHHQDDALETVWMRLMRGVSLEGLIAPRAVHCVAFRNPRGSWTHYAQLRPLLGFSKLEIKRACQACELPFFEDKTNAQDGCLRNRIRHQLMSQMDTVFHSSDWRKGFTRSCQILSEERDYLADHLQAKFLTYDFSHTTFDRASIQALPLVEVRYFLQTWFSYHAISPICFQQSDWLFQALQTCEQSTLMINARYRLILSPKQLCLAPKPIDFAPFQCRFHQGVIFLPNGAQCVCQIQPCTPDLYASVGDKRGSNQHGVLLDASCFMGPYQVRNRLPGDRYQPLGVRREKKVKELLSKRKMSNKSSLPVFCDCNGRIAWVPGLPPADCFKLSDKTKYCVFLIYEKDNFI | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 475
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Sequence Mass (Da): 54361
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R4VKS6 | MIESLLSLSVIDLTAIAVKAAGYLAFLLAAGSALVLMALAGLPGSEVRFLRRLVPAMALLAAVLAAARLGVEVVILAGDDWGAIFDFELMMLILQGSTGLALGVQGLGLLLLMGVMLPGVIGLIAGFLGALAVATGFGLTGHTASVDGWWLNALIIVHLLGLSFWVGIFIPLYRVARYDLGHAGQVAAAFGRIAIWVVPILVAAGVLTFQQLTGGVGTAIKTSYGQLFAIKIALFSGVLLLAAINKLSLTPALARGERLAPAKMRRSLMLESLLIVGILVATASFTTLTGPQG | Function: Involved in copper resistance.
Subcellular Location: Cell inner membrane
Sequence Length: 293
Sequence Mass (Da): 30237
Location Topology: Multi-pass membrane protein
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A0A9D8HPW1 | MNVDLISIIPEMVITATGLLVLLLSVFIGKKFDRAIAPISAAGIIAAIAAVFIFNFYNRAYSFSNSFVVDNFSNFFRIFTLVSTLIFTGLSASYIKDSIHIKRHLGEFYFLVLTVCTGTMLMSASGDLIMLFISLELVSIPTYILAGYEKANERSNEAALKYFILGILASAILAYGFSMIYGATGEVNLKEIARVIINRELLNQNFMLVVGIIMSLIGFGFKIGSAPFHWWAPDTYEGAPTIVTTLITTIAKIAAFAGLIRFLYIGISRFSKSLWIIVFIIILSLMSVIIGNFMALPQKNFKRLMAYSSISHAGFMLVGFAVATVDAQWAVFLYLMAYISMNLGAFAVAMLVERTRKSEEIAAFAGIGYTNPFISICMIIFMISMVGLPPFAGFIGKLFVFKAGVENNLTWLVIVGVLTSVVSLWYYVNIIRHMYFVKYEGAPSTARIETPKLSIFIITILALFTLAMVIVPSVFIMVSTNSVTSF | 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 a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 486
Sequence Mass (Da): 53650
Location Topology: Multi-pass membrane protein
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A0A933UPE0 | MSGPTAPEPGEHPGAAEPDERADADRGVDRVQEHVLRDRTVAALRRRTPSGVLVGLRLGRMRWRRSLRLRVVATTVVFATLVVLAVGSVLLARISEGLQTSSNELARGEAKQLYAEAQRLVKGRSGDPGPFGTELVTRLSNEDNRFVVLRQSLDATAAGPIQDRSSSGMPADVIPTDLRQKVVATKGQLFGRPVALPPRDAGRAAPRTSPGYTWGGTLDLGQGIGYYELYFVFRQDREAATLDLVRRTFFVGGAALVLLVAGVAFVVTRSVVEPVRLAARTAEEIASGHLDRRVRVRGEDELARLGAAFNDMATSLERQIHRLEELSRVQRRFVSDVSHELRTPLTTIRMATEVLHEARDGFDPATARSAELLMTQLDRFESLLADLLEVSRHDAGAAVLDVDPADVRDVVTRVVDGLRPLADGRCDVVVDVPAQPCIAEVDARRLERIVRNLVGNAIEHGEGRPVVVRVAGSADAVAVVVRDHGVGLTPAQARMVFNRFWRADPARARSTGGTGLGLAIALEDAHLHGGWLQVWGDPGRGASFRLTLPRRAGVVLRTSPLPLVPPDAVQQDEIAAGGTHLAGTGLASGPAGVLDVEALIADLDTVLTETEAAAAEAAAEAAAPSAPLDPATAPQGRDGRG | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell membrane
Sequence Length: 641
Sequence Mass (Da): 68448
Location Topology: Multi-pass membrane protein
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A0A3D2KVW6 | MLSPSERALSDQVNQVLSVSDFTLNLKQVLEGHFAEVWIRGEVSNCRQQSSGHVYFTLKDENAQISAVLFKGHALRYANLVKEGQRIVVFGNVSVYAPKGNYQVLVRFVASDGMGKLQLEFNRLKEQLGREGLFDPERKKPLPLLPKKIALVTSPTGAAIHDFISILKRRKWAGTVIVFPSKVQGEGAKEELVTQIQRADGMAVDVIVVCRGGGSLEDLWPFNEAVVVRAIAACSTPVISAVGHEIDFTLADFAADFRAETPSAAAERITSDRIAVLERIDGTKHFLAKEAKHRLAVWKSHLLRLQAGLSPATLKRTFENAILHHDDLTRAFALALQRHLDQKRTHYTHVQHRFAQTHPEHALSQSRNRVQQVEHRLHNLSFAHTLQRGFALIRDPHGHPLARKALFGEKLIVEMADGTTAVRMDSGLND | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular Location: Cytoplasm
Sequence Length: 430
Sequence Mass (Da): 47939
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A0A8J3JDF2 | MARIGVLGPGGIGGLLAARFGAAGHDVTVVATEASAAALTVRGLHLTGPDGATTVTRPLARPWLTDPVDLLVVAVKATDLLPALARVPAAVLGGATLVPFLNGVDHPALLRAAYPGAVVVPASIAVEATRHRAGVIEHLSPFADIVVANGTPAGAAAVDLFASTGLRVTGHPDESAVLWRKLAFLAPLALSTTVADAPIGPARTGHPERLRALVEETVAAAGTAGVDIDADAVAARLDALPATMQSSMLKDRRSGRPMELDAIAGPIVRALGADRAPATAEVTGAILAAT | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 290
Sequence Mass (Da): 29060
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A0A2A5X9W9 | MKSNELLYELLKINSIKIQIKKPFTWASGWKSPIYFDNRVSLSYPYIRSEIKEHLSNLINKKYKNVDVIAGVATAGIPQSALVADMLKKPLIYVRSKPKSHGMKNMIEGKLEENKKIILIEDLISTGGSSIKAVDALREKSTDILCVISIFSYGFSISERNFEDAKCKSESLFDYDDLISVALDNKFINNDDADSLREWRIDPEKWGEKFT | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
EC: 2.4.2.10
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Length: 211
Sequence Mass (Da): 24079
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A0A938AGN8 | MSTTAPDPAITAVIGAREVPVHLGAGAIDLVGPLLAARGEGDGAMVVVDDGIAAAGERAAASCRDAGLRVHVEAVPAGEASKSLAEIERLGRACARAGIRRRDAVVAVGGGVVGDLAGFLAASYQRGVRLVQVPTTLLAMVDSSLGGKTGVDLPEGKNYVGAVYQPEAVVMDTTVLGTLPPRELSCGFAEVVKYGLLVGGDLIEIIAAWPELPGPDNELADLIRRCAECKLEVVAEDEFDLGRRAILNLGHTAGHGIEAAAGYGLYHHGEAISLGLLAALRVSEQQLRLDPSWRDRTAATLARHGLPVELDPSVDVDEVIEIMSRDKKSDGRALNMVLLRAPGDVLTHQDPDPAVVRAAVEELLP | Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
EC: 4.2.3.4
Subcellular Location: Cytoplasm
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Length: 365
Sequence Mass (Da): 38010
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A0A194AGB5 | MIYHLLYPLSGDMGVLNVLRYITFRSMLAMLTALVLSIIFGPAFIGWLKKIKCGQYIQEDGPKHQSKAGTPTMGGAFLGLCLLVSVLIWGNLKNPYLWLTIFVFSGFGLVGFVDDYIKEVRKNNQGLTARTKFVGQVIVACGALTILITMPGYSSELMVPFFKSIRPDFGWWYIPFALLVMVGSSNGVNLTDGLDGLAIGPSVVSAGCLGIFLYLAGHVELARYLQVAYIPGVGEVAVFCGAMVGAGLGFLWFNAYPAQVFMGDVGSLSIGGTLGFMAVLCKQELLLVIIGGLFVIETLSVVLQVGYFKMSGGKRIFRMAPLHHHFELKGIPESKIIIRFWILSILLCFMALATLKLR | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP
EC: 2.7.8.13
Subcellular Location: Cell membrane
Sequence Length: 358
Sequence Mass (Da): 39077
Location Topology: Multi-pass membrane protein
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A0A2M7A192 | MKLRQNKKILYQIKLLLCFTILASLISCAAHHKSKQAAQYSTTGIASWYGPGFAGEKTANGERYKPSGLTAAHKTLPFGTCVKVTNLANNESVIVRINDRGPYVRGRLIDLSQGAAKKISMLHHGTTKVKIETIIPSENKIAKTVTPAPKSKNKKNQLALQTKKLENTSKDLPEEF | Function: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 176
Sequence Mass (Da): 19360
Location Topology: Lipid-anchor
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A0A7V1CK46 | MKDTQTRIHLKTKSIANSNYYRTKETIREQRLHTVCEEAGCPNKFECFGVKTATFLILGNSCTRNCSFCLIDKADDFQLDSQEPYRVAEAINKLGLKYAVITSVSRDDLPDKGASFFAETMNWIRKMNPPCLIEVLTPDFGGDEKALKKVFEAEPDVFNHNIETVKRLYPDIRAQADYECSLDVLHKAKQYGLVVKSGLMVGMGETRQEIIDVMQDIRATGCDILTIGQYLQPTKDHQEVKRYYRIPEFSFLKQLGLSMNFKVVQSMPLVRSSYRAYDSFLKAESSEQKTA | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
EC: 2.8.1.8
Subcellular Location: Cytoplasm
Catalytic Activity: [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Length: 291
Sequence Mass (Da): 33237
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A0A9E2Q817 | MDEKELLELLESSGALRNGHFKLSSGRHSDTYVQCALLLRDPDDAVRVGNALAEKVEGEVGLVLCPALGAVVIGFTVALALGVELVFAERHNGKMELRRGFEIPAGSRVLLVEDVITTGGSIMELARMVEEAGASVTALCCMVDRGKLDAGEYRLCSLLRLQVASYPPDECPLCARGVPIDAPGSRYTG | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
EC: 2.4.2.10
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Length: 189
Sequence Mass (Da): 20158
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A0A9C8C3R9 | MILITCRARKHLKKKKKRQLKPIHIIISIVVLLIFIGCRGYIGLKNLKPVASKEDNTVKTSVSVEITPGLGIAEIGKILVDKNVISNAFYFDLYAKSSGLGSRFKPGNYIFSENMKYGEVVKILAEGPRKKKIYKIVIPEGFTVEQIAERLDKNTPINGGEFKRLALDIRGLGALNYYFLKDNQAGSLEGYLFPKTYSFLEEKTAEEVLRIMLDQFDEEIGKFDFGYAKEKGMSIHEIITIASLIEKEVSIPAEREVVAAVIYNRLKKGMSLQMCATVQYVLPERKQHLSNEDLKIDSPYNTYIYRGLPPGPICNPGLTSIRAALNPASVDYLYYVLTGSDGSHTFTNSYDEFIKAKKDAKNGQ | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 364
Sequence Mass (Da): 40900
Location Topology: Single-pass membrane protein
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A0A947SYS5 | MPELPEVETTRRFLVPALEGRTITAVSIRRLRMVRRQARPGDFADRVIGCRIEQIDRHGKFLLAKLSTDVTWVTHLGMSGSVRLAVAGDPEDPHTNVVIRLDDATECRMVDPRTFGFVAAFLPDEMAAGSLAGLGPDALDDLPTTAVLRARMEGRAVPIKPLLLDQAFLAGLGNIYADEVLFRSGIAPSRRAGSLERDEVKRLRGAIRPILEAGLRHGGTSLDDLAYLLPDGRAGDYLSRLMVYGREDRPCRRCGTPIRRAVLRQRSTFWCPECQA | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
EC: 3.2.2.23
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Length: 276
Sequence Mass (Da): 30525
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A0A8J3JFK6 | MTIPGLPTPVHSGKVRELYDAGDGLLVMVASDRMSAFDVVLPTAIPDKGRVLTALSLWWFDQLSDLVPNHVVSADVDEYPGVFRGRDELRGRSVLVRRLAMVPVECVARAYLSGSGTKQYRVDGAVCGVPLPAGLTEGSELPDTIFTPTTKATPPDHDAPMTYAEVEAAVGPEQAAELRKLTIEILDRGRRVCGPRGIILADTKVEWGVDAAGTLVLADEVLTPDSSRFWPAEEWQPGRAQPSYDKQPLRDWLESSGWDKKAPGPELPPEIVAATRERYVAAYERITGERFA | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Length: 292
Sequence Mass (Da): 31860
|
A0A8J7QXZ6 | TDVNGVYTTDPRMCKDAHKIDRISYDEMLELASMGAKVLQIRSVEFAEKYNVPVRVRSTFTDDPGTLVTKEDHMMESVLVSGIAFDKDQARVTLCDVQDRPGSAASIFSPLGKAGIVVDMIIQTASRNGVTDIAFTVSRKDLGRALDVLQKAGPECSHIENASNMAKVSVVGVGMRNHSGAASRVFDALYKAGVNLIMISTSEVKISCLVAESDLEMAVNVLHKEFEL | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
EC: 2.7.2.4
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP
Sequence Length: 228
Sequence Mass (Da): 24742
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A0A4Q7JE93 | MKPPQADRPGEDDPGPGRRLGVDVGAVRVGIALSDPSPVLATPLVTLSRDATQDSDLDQLAALVTEHEVVEVIVGLPRTLADRHGPAAAIAVEYAEALAGRVAPVPVRLADERLTTVSAARMLSGRGVKGRKQRAVVDQAAAVEILQGWLDGRAALRARKGES | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 163
Sequence Mass (Da): 17044
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R4V336 | MDLPDSAVRHLQARRLRSGDGLVLFDGTGGEYTATLVDLQRRRAQARIDAHTPREAEAPVAVTVLQGISKGERMDYAMQKATELGVARIIPVISERCVVRLDSERWAKKQRHWQAVAIAACEQCGRNRIPSIDSPCSLEAGLAEVDSLPGVIFDTEGDRAARDLKPTEQLATLIGPEGGLAPEEIQRVADLGWQRIRLGPRILRSDTAPVAALAVIQTVIGDLG | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
Subcellular Location: Cytoplasm
Sequence Length: 224
Sequence Mass (Da): 24329
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R4V8U7 | MNDSKETPDFEGALKTLEGLVEQMERGELSLEQSLQCFEQGIRLTRECQKALDEAEQRVDILLGKDADAEPEPFGEAGDESAD | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular Location: Cytoplasm
Sequence Length: 83
Sequence Mass (Da): 9202
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A0A2D4NHH2 | DASQPAAMPDAPRPLPAEAARKPGSGSPDRLGAAYFDQPCIRLAKALLGQILVRKLTDGRELRGRIVETEAYLGGEDTASHSRGGRRTARNTAMFMQPGTLYVYQIYGIYFCMNVSSQGEGAAVLLRSLEPLQGLEAMRELRLARQQKAPARPLKDWQLCNGPSKLCQALAIDRSFDQQDLGCN | Function: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.
EC: 3.2.2.21
Catalytic Activity: Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine.
Sequence Length: 184
Sequence Mass (Da): 20105
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A0A942QL44 | MSDEIVSRFPYATIGTILGAHGGTGEVIVFPTSHSAELRCGMTVWVVPPGEDFGPLTIESVRPGPKGLLIKLSLIECRNHSSALKGARLIAAASDLLDVSDDDAALNPIGYKVMDEKLGELGVINEVIHTGANDVWVVEGGRWNQVLIPVIDYVVRSTDPDSGTVNVRLLDGLISEDLIDEN | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Subcellular Location: Cytoplasm
Sequence Length: 182
Domain: The PRC barrel domain binds ribosomal protein uS19.
Sequence Mass (Da): 19458
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A0A946KW38 | MTKTSFRPLEELFNPGEFVPRHVGPSLSDRQHMLETIGMSSLQELIDQTVPTSIRSTEPLNLPGPVSEAETLRRLRALADKNSVFTSCLGAGWHDTFTPSVIVRNVLESPGWYTAYTPYQPEISQGRLEVLLAFQSMVADLAGMEI | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
EC: 1.4.4.2
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Length: 146
Sequence Mass (Da): 16219
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A0A938EFT2 | MPHPYIPNSAPEVRREMLDAIGVDSVEDLYRPIPSELRFQGRLPLEEGIPEEGRLRRHVEGILRRNTPATDVLSFLGAGCYQHEVPAVCDEINRRGEFVTSYAGDVYGDHGRLQALWEFQDVMAELIEMDVVTTPNYDWSTAAAMCLRSSVMLTGRKRVLVPAALLLDRRLVFQDYLAHDVQVDEIPFDEATGLLDLAALQAAIGDDVAAVYVEYPNALGVIEHQAGEAVEIAHEHGAMAVVGADPSGLGVLASPGSLGADFAVGDLQPLGMHMSYGGGLSGYIGCRNDAEVIGSLPVFIFAKTATLEPGQHGFGYLNFDRTHYVKRGEGSQNGGTTTALWAITAAAYLGLHGPEGMRELGEGLLQRTRYAADRIGALPGVTAPRFTGASLKEFVVTYDAHDVASVDAALRERGIFGGKDLSVDFPSLGRSSLWAVTEVHTKDDIDRLVATLGEVLA | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
EC: 1.4.4.2
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Length: 457
Sequence Mass (Da): 49257
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A0A3D2KP70 | MSTLAVDKDFDLPYIGAFNVENTLAAIECVRGLVELKSDAFLDYAGIRRRQECLLRAGDLTVYQDYAHHPREIQAFLSYAADRSNARKIIIFQPHRYSRTRQFTKEFADVLKGADQLILLPVYAASESRDLGVDTDAIYDQLKGSMDVTYTTLESFSLQYSFDTPTDVLFVGAGDIEVIARDYAKNAIDFLKRQLSVNIGQTRLTCHEPLGPKTSLKIGGNALFFAEPDSESSLIQLLQNACKLPVFTLGRGSNLLVPDEGFAGLVISMNVPWLQTASVENDVIVVGAGLRLKELCGFATKNGIGGYTFMDGIPGSVGGALRMNAGAMGAAIGEKVLSVEALDRQDNKHVLDARQLHFEYRACRTLDDKIVLRARMAVLRESRETLEAQRAQFLEKRKQSQPVGASAGSTFKNPPGDYAGRLIEQAGLKGTCVGGAEVSQKHANFILNQNRASSRDVVSLVKHIKKTIVSTSNIALEPEILFLGHSWKDVL | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 491
Sequence Mass (Da): 53899
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A0A1V4MGV3 | MKYELRQEGNTMKTVEESLELILDFVAPRGVEKIPLTECLNRVLAEDAYSNRNIPPRDNSAMDGYAVKCRDLGNASPEQPAVLRSVEEIPAGTSPEKRIGEGEASRIMTGAPIPDGADAVIKIEDVAVEDDIVRCFTPVEEGENIRKRGEDVIEGEAVIAAGTHIQPAHMGMLAATGHALVPVYRRPLVAIIATGDEIIDLDGDLSSEKIISSNSYSLYGQIIEAGGIPLPLGIARDTKQDLLSHFTMAKDRAQVVISSGGVSMGDYDLVQEVLTELGARVEFETVAQRPGKPFTFATMGTIPFFGLPGNPVSTMISFEQYVRPALRKMTGQKKLFRRTARAVLDENITKKNNLTYFIRGKATWRDGNFTVVTTGEQGSGILKSMVLANVIIVLPRGITHARRGDEVTIQLIDTSILSAATPGYLDALSWKDPSS | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 435
Sequence Mass (Da): 47240
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A0A0G0JB19 | MKLILEINNKTPQKVVKKTFLSVFGRTLDLVSMDCLKDKTIELSVALVGEEEMHSLNLQYRKKDKATDVLSFSEYETTALLCKQASTSDSEIFLGEIILCPNYIANNAHEDGEAFEYALNYIISHGILHLLGFPHGKKMFSLQRKVADMLK | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 151
Sequence Mass (Da): 17086
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A0A938DHX0 | MTSTSRRARLVVAYDGSSFHGFAPNPDVPTVASALTEALEKITQSEVQLVAAGRTDAGVHARGQVVSVDLPSRTKIESLARKLNALCGPQIAVRDVQWAPASFHARFSAIWRHYRYTILNSKMPDPFLATTAWHIHVPLELRAMQLASDAIMGERDFSAFCRKPDAADEPDSPPSTKSGAAKKPATMTRFVTQAAWKREGEVVTFEVRANAFCHQMVRSLVGTFVDIGLGKRPPSDMMNLIRSGRRHDASQLAPPHGLCLWEVGYPSSLE | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
EC: 5.4.99.12
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Length: 270
Sequence Mass (Da): 29621
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A0A7C5H0H1 | MFRAIADLAADDSPLDVITLSEWLERRGELADAGGFAYLATLAKDTPSAANIKAYAAIVRERSLLRQMIGVGTEIADKAFNPQGRDSNELLEQAEQAVFRIAEQGSKQQQAFKPIKGLLKETLEHIRTLQHSDSSITGLSTGYAELDEMTSGFQKGDLVIVAGRPSMGKTTFSMNIAEYAALSIKKPVAIFSMEMPAEQLTMRMLSSMGRIDQSRLRTGKLTPEDWPRVSQAVQMFSEASLFIDDSPALSPLEVSARARRLAKEHGQLGLIVLDYLQLMKSANGRAENRATEVSEISRSLKAMAKELNVPVIALSQLNRSLEQRPNKRPVMSDLRECVTGDTRVILADGRRPCVRDLVGTTPEVLALNTKNQLETANSDCVWSVGKKPTVKITLASGRTIQCSENHRLRTLWDWTEAQKLAVDDRIAIAHRLPEPAKPVVWQREALILLAQKKHFPDEIFQLSNTQLALFLQHLWATDGCIYLGQNNTSHRIYFTTVSERLIHDVSAALLRFGIVTRIRKVTVKDKPTMLNDSPNSENNDENDENKEGGYWFTADISGTTQQQLFLQYIGGFGKQADTAKQLSDYLATKQPNTNIDTLPIAIFDYIREKMKAQGISHRQMAQLRGTTYGGTAHFSFAPSKKVVRDYAELLNDAQLYDLANDDLFWDRIVAIEPAGEAEVFDLTVPDQACWLADGIVSHNSGAIEQDADIIIFIYRDEVYNPESNDKGSAEIIIGKQRNGPIGTVRLTFLGKYTRFENFAADVYTPNAFEH | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 770
Sequence Mass (Da): 85790
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A0A963SEF3 | MHDYLIALGSNMPSAEHGAPAANIRAAFAMLRDIGPVIASPIVASAPLGPSRRRYANAAALLESDLSPPELLALLKHIERGFGRRAGGRRWGA | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
EC: 2.7.6.3
Sequence Length: 93
Sequence Mass (Da): 9825
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A0A7C1AGP4 | MLKVYAAQLLLAVEVGEEAEASGTDLLLPAQSELIAGIIAFIIVFVVVWKFAVPALNETLEKRQSAIKGEQEAAAAERAEAASLREQYQKDIANAEAKASEIVEAGRKDGMAAKADIIAKAETEASAIKERAQAEAAGERERAEGALRREVASLSLDIAEKVVGSGLDRGASQALVDEFIADLDGAQA | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 188
Sequence Mass (Da): 19791
Location Topology: Single-pass membrane protein
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E7RZ99 | MTDARSHALPSIRLRLLGTVPYTDALTRMREWTAARQAARKAALAGGAPPAATPAIVPGTGEASLRRDWPDLAEAATAGDEIWLMQHPPVFTLGMNSQPEHLLNAGDIPVVPTERGGQITYHGPGQIMAYLMLDLRARRLGIRTLVERIEDALIDCLSQYGITAFRQEGAPGIYVLPGQNGPVQPADGAAQWPAGTVTPPVSGPHHVHARHARPAAGVAKIASIGLKTSHGFSYHGLALNGQMDLSPFHRINPCGFRNLQMTDIHRQAALSQDLDLDALALALGKALAAAIEG | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
EC: 2.3.1.181
Subcellular Location: Cytoplasm
Sequence Length: 293
Sequence Mass (Da): 31150
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A0A0R3WFQ3 | LVKTTLELTECVAKSVSENDMTLILGGDHSIGTGAIAGHLKIFPNSFVVWVDAHADINTPMSSVSRHTHGMPLSFLLKETSKLIPQTHGFENIKPVLEANQLLYIGLRDVDAPELKFIKDLNIPYFNMEDVRSIGIEGVMETTLRTIMRFSPNCQIHLSFDIDGLDPKYAASTGTPVPGGLSLEEGKYICKTLGQTGLLKSMVVAEVNTSLGSPEDAQTTLNSALEIIKSALLLD | Cofactor: Binds 2 manganese ions per subunit.
Pathway: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
EC: 3.5.3.1
Catalytic Activity: H2O + L-arginine = L-ornithine + urea
Sequence Length: 235
Sequence Mass (Da): 25494
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A0A0R0LRF0 | NSICTIKGGTHVQYVLDQIIEPVIEKLKKKEKGLNIKPQFVKNNIFLFLNCLIENPSFDSQTKETLTLRSNAFGSSIGEIKPKIFLNILELIGENIINIAQQKNLQQLKKTGGNKKTKIQHKKLDDANKAGTKDSKKCSLFLTEGDSAKTFAMCGIESIKEGRNIFGAFPLKGKLINVRDASHEKIMKNEELNNLKKIIGLQHGKKYETVETLRYGTVIIMTDQDYDGSHIKGLLINFFEHYFPSLLKIEGFLKEFITPIIKATKIKRSRAGNNNGG | Function: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.
EC: 5.6.2.2
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Length: 277
Sequence Mass (Da): 31153
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A0A3D4HJB5 | RIQTSYDAGDHVVVVVSARSGVTNDLINRASRLTSKPDCRELDMLLSIGEQETIALVTIALHALGVPAVSRTGAQAGIITTDQHTQARILHITGGDIKEQLDAGRVVVVAGFQGVSDKGEITTLGRGSSDLTAVAIASFLEADRCEIYTDVEGVHTGDPSLIADATLLKQMDYGMMQELSSSGFKVVQARAVQLAERYKMPMVVSSSKKSSAGTSIQDELSSFEGPRVYGVALDKQQAKILIEGIAHEPRSLAQLFAALKAASVEVGMVLQSDSRDIKKGLSITVPHAQLHAASAALEVVFDRLGEGRIIDMGPVAKLSVVGAGMRSDVSIMATLLAALAEAQVQVLMVSTSEVRITVVIPVQKAEEALRFIHSALGLGSKKTEEALTMQVG | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
EC: 2.7.2.4
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP
Sequence Length: 392
Sequence Mass (Da): 41438
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A0A933PB56 | HLDGVLRNRRLNRLVDDLELTLHVDDLPVQAWDREEVHQVFDGLEFRVLRERLFSTLATPEPEADGGFDMATERLDGAGVKEWLEAHGAGTVGVAVVGHWAQGRGDARGVALAASDGTAGYVDLVEADEQAQSALAAWLADPVAPKAFHDVKGPLVALASRGLPLRGVVSDTALAEYLCRPDQRLFDLSDLVLRHLGRELRAEAGAPAEEPAQLTLDMEEAPGGPDEAETAMVRARAVLELSEKLGAELLDKGGLALLDGVELPLVDVLARMEQAGIAVDTQGLADLEAYFAGEVAAAAKEAFTHIDGEINLGSPKQLQVVLFEQLGMPKTKKTKTGWTTDAEALADLYAKTEHPFLLHLLRHRDASKLRVTVEGLIRSVADDGRIHTTYQQNIAATGRLSSTDPNLQNIPIRTDEGRRIRETFVVGAGYECLLTADYSQIEMRIMAHLSKDEGLIEAFLTGEDLHRFVGSRVFSVEPAEVTPAMRSKIKAMSYGLAYGLSAFGLSRQLAIPPAEARTLMEDYFDRFGGVRDYLQSIVAEARRTGYTETILGRRRYLPDLTSDNRQRREAAERMALNAPIQGSAADIIKVAMLRVDAALREAGLTTRLLLQVHDELVLEVAAGEREEVERLVRAAMGGAAELSVPLEVSVGVGRSWHEAGH | Function: In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 661
Sequence Mass (Da): 71960
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A0A2M7DRM8 | MRIIFYGTEKCSTDFLELLVNKENVVAVTTQPDRPSDRGLNIQPSPVKTFARKKNLLVFTPEKLSDRTFQTSITNLKPDLGIIVSYGKILPKEILNLPAYKTVNVHFSLLPKYRGAAPIQWALINGEEVTGVTVFFIDEGMDTGDIILQKEVTIKPQDDAISLEDKLVQCGLQLLEETLILMKNKKIEPKPQTGEPGYAPMLKKNDGEINWSKKSTEIYNLIRGTKSWPSAWTRYHSGKLLKILQAKPTSFDFAESGISFTPGQIVGIEKKVGFMVGCGEGLLIVEQVQPEGRKPMSAWDFLQGARLKVCDKIGTHPI | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Length: 318
Sequence Mass (Da): 35505
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A0A972HBV4 | MSRTSSGASDRQDRDDGSRGRPDRVAFVTYPDEGAARTLAETLAREASGRFGFEGLYVPVQSRLDNVDAVISVGGDGTVLHAAAAAREADVPILGINLGRVGYLAEVEMDAVDHVLMRLGAGDLATVDHPTVAVEFEDGSTATAINDMVVEKVVSQRIVDLEVMIDGELLTTYRADGIIVATPLGSTAYSLSAGGPIIQPTVGCMVMTPIAPHSLLSRSFVLRSESVISIRATSERPAQVNVDGRGTRQLQRGETVRVTTSDRPVRFLLTGATPFPRAVRDQFGLDHA | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Location: Cytoplasm
Sequence Length: 288
Sequence Mass (Da): 30631
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A0A364NCF5 | MSLPEFKQNFLKDCVSAGALKFGTFTLKSKRISPYFFNAGLFHRADLLRSISSAYAHTLKAHGDADPSFQWDILFGPAYKGIPLAAASVDKLADLDLAKYGQKSYSFNRKEAKDHGEGGNIVGASLKGKKIVIVDDVITAGTAIREAIEIIKKEAWTKRHWRGQEAVRHPSSPHLDPG | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
EC: 2.4.2.10
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Length: 178
Sequence Mass (Da): 19569
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A0A9D8DTX0 | MPCGGGRCVVARGGGRSRSARRARRERSPRPVAHGGPDEERDVSRARAIVDVGAIRHNVGVIDAHVRGLADAVRSAAVCAVVKADGYGHGAVASARAALDGGARWLAVAHAFEGAELRAAGIDAPVLLLTEPLSHELDAVVEHDLRVAVYSVEGLDRLTAVAARSAQAIRVHLKVNTGMNRAGARPEDVSDLAVRVARTPGLELEGLWTHFASGEVVGSSATAVQLERFAEVRAGLGAAGIEPPLVHASNSGATILRPDAHFDMVRPGLAVYGVAPAHELAGHLHLLPALSLESEVTHVQRGLAGEGVSYGWHHRLARDTVLATVPIGYADGIPRRSGMVGATVLVGGRAVPIVGAVTMDQLVVDVGPTGEVGVGDAVVLVGAQGGERVAVEDWAGRLGLLTYEVLTGIGGRVERVYRGGGR | 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: 422
Sequence Mass (Da): 43676
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A0A4Q7DI19 | MFSLLSDSLSKLFQKLKSKGVLTEKDIDDAMREIRLALLEADVALPVVKELIANVKTKAIGQEIVKSVAPAQMVVKIVNDELVNILKSDDQSINVGGQAPVVIMLVGLQGAGKTTTAVKLGAFLRKKLKKKVLLASLDVYRPAAIEQLQILGKQVEIDTFESDKNLPALEIAKSVLLESKQKGYEVLILDTAGKLHTDPVAINELQQIKKMAAPLETFLVVDALTGQDAANIGKVFNEQLGITGIILTRVDGDAKGGAALSLKMITGAPIKLLGVGEKISELEEFHPERAVSRILGMGDIVSLVEKASSLVNEEDALTMTQKMRQGRFDLNDLKRHLKNMKKMGGIASLLSMLPKLPGMSLPTEGAVGDDAFKRIEAIIDSMTELERQEPKILNASRKIRVAKGSGTSVQDINRLLKQHLAMSDMMKRFSKMDPRRLKDMLK | 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 receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components.
Subcellular Location: Cell inner membrane
Sequence Length: 442
Domain: Composed of three domains: the N-terminal N domain, which is responsible for interactions with the ribosome, the central G domain, which binds GTP, and the C-terminal M domain, which binds the RNA and the signal sequence of the RNC.
Sequence Mass (Da): 48230
Location Topology: Peripheral membrane protein
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A0A2D7V6H3 | MGVDLSKVDFSLFPGMERRQSLLFESEQRMIMEDYAHHPSEVRAFLAQRRFAAPNDLLRVVFQPHRFSRTRAHAKGFAEELSVADELHLIQTYGAFEDFDAEGTVEALSGHLPPRLREDAKVYEDFPELRTALRGKPRGKLKRDQVLFVGAGNLDSWAHAFASYEKSKDDRDKAFADYLANRLSPACDLRFKESMSSKTTMRVGGEALWYAEPGTLEDLLNLVEASHLFELPRAMIGRGSNLIIPDDGYAGLALRLKGSFWSEVSLRSEALVVGAGASLREICRIACAGGLKGFEFLEGIPGTLGGALRMNAGAMGWETFDLVDWVLFLLPDGSMRRIDGSELNVGYRYCREAVEGIALRAKLRSEGRSDHRAIRKAIDNMAKRRRKSQPREASAGCIFRNPGEESAGALIDEVGLKGEREGNAVVSDVHANFIVNEGGASAEEVIELIRRVRKRVKESNGMELEPEIGVLGKNWDEYLS | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 480
Sequence Mass (Da): 53399
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A0A938ES79 | MWKSNRQSASSSLSTCNPLHALQTERGASLIPTSHWRIILSVALAVYSLDLLTKIWAVETLEGKPTQYVIGKFLRWEFARNSGAAFSSFTGATFALTLISVAVLLYLALRAAQVSVKAWSYPWGGLIGGVLGNLTDRIFRDPAPFQGHVVDWIGLPNWALFNIADSAIVLSVITMAILSLRGSTFRGVAP | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
EC: 3.4.23.36
Subcellular Location: Cell membrane
Sequence Length: 190
Sequence Mass (Da): 20664
Location Topology: Multi-pass membrane protein
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A0A0P7BA35 | MVPKQQEMDGIVQSLFESMVSKAHLKSTLLVLCGDHGMNDAGNHGASSPGETSPALVFVSPKLKTISSKLPAPAQPKGEFEYYSMVEQSDIAPTIAALLGFPVSKNNLGAFIPDFLPFWPKTSDQIQILIRNARQILNIVTAAFGGGLFDTESATDPCALESSEINDLACQWQKIDKQARFSANAKELDQEWLIDMSEWLRRAQDLMSSMASNYDMPRLFLGQGVALASAVTSGIAVLQLGSHRGGLLAPLVLITVTYGIMMFASSYVEEEQHFWYWSSTIWIAYLGVRHVRRSTELPSMTWFILALAALRVTRGWNQTGQKFAGEPDIVKTYVVPNPQLLWITITVAYIMLSFRILSRLDSLPYFAATSLASLLLTSAFSFKMDFTSEDAPELVIGFAHTFNQMFQGQSLLWKARTVFGLLATLWGKPIPSSLHPDILFHALQVANLSIPEITTASILLQHASFFAFGGSNAISSVDLSSAYNGVSGFNIVAVGLLTLVSNWAGSIFWVSATNLMLLRKYHEGHRRVFRQHLAVMTFFFAASVVFVMAACTVLRTHLFIWTVFSPKYLYSMAWSLGQHLLINTGFGGLLFWLTAR | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 596
Sequence Mass (Da): 65904
Location Topology: Multi-pass membrane protein
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A0A972PVR8 | MPNYMMVLEYDGTAYHGFQKQPGLPTIQGALEGALSRVAGMESPLYAAGRTDAGVHARGQVVSFHGRLKIPCARLAQALNALLPPDIAVKECAEVDDGFNARRSALAREYAYHVQCGGQPSPFDRRYVFRCRGGLDVEAMREALGAAVGVHDFAAFCRREEGKSTVRDVYEAELEAVGEKLRIRVKANAFAWMMMRMLCGALLEVGRGKWTPDRFRDILESGESSHGAQTLPPHGLFLERVYYP | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
EC: 5.4.99.12
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Length: 244
Sequence Mass (Da): 26937
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A0A972KC66 | MIVEEIPPSLDGERLDRVAALITGWSRTAVKTLLADGRVLLNGSLPTERVVRVAVGDEITIDLPPKAAPSGPEPVDSIEVPVVFEDHHIIIVNKPAGLVVHPGPGHVDDTLVNGLLVRYPEIASVGQIERPGIVHRLDRDTTGLLVVARTNTAYEALVGALSTHEVTRRYVALCWGGPENERGVVDAPIGRSRRTRTKMAVAHDGKPARTHYEVRTRYTDPAVATLMDCQLETGRTHQIRVHLAAVGAPVIGDEVYGRPDRLGVGRVLLHAAELGFEHPSTGELVRFESPWPDDFTTAVDRFK | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 303
Sequence Mass (Da): 32986
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A0A077M1C1 | MNALAARRRHPAVLTVLLLVALVATGCAYAAFAPKPAQAATADADQVAQGKKLFQANCATCHGLNGEGTKTGTGDQIAGPPLAGVGAAAVDFQVGTGRMPMAAPGVQAAQGVKGAQFTQTQIDQLAAYVASLGPGPAIPAAADYDYSNADAAKGGELFRVNCAMCHNFAGSGGALTRGKYAPSLATVSPKHIYEILNTGSQAMPVFNDTNLSPDSKREIIAYIKTIHTEPSPGGLKLGSMGPVSEGLFAWVFGLALLIGFAVWLGNKSA | PTM: Binds 2 heme c groups covalently per subunit.
Catalytic Activity: a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out)
EC: 7.1.1.8
Subcellular Location: Cell membrane
Sequence Length: 269
Sequence Mass (Da): 27398
Location Topology: Multi-pass membrane protein
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A0A9C8EXP8 | MGANNSYPSVPRGLRDIMPIEAEERRQIEKKLRRVFESWGYREIITPTFELFENLASEAGKMMEDEMFKFFDRDGVLLALRPEMTTPIARAVSQRIENSCFSRLYYSASVFREEPPQRGQQREFQQIGLELIGGRSPAADAEVLAVLLESLQAVGLKDFQVGVGQIDFLQGFLETTGISSELIKEIQLLLVKKDLVGLERTIEDNSLSPEDKSKILEIISLRGRKDILEEAKKYTTNAKSCEALKNLSDLYEFLKLFDLEKFVIFDFGIIQNFDYYTGVIFEVYAPNMGFLLGSGGRYDLLLSEFGDNRPACGFALGLERLHICLNEQGALKKENCKKILVYSDVDIKKALMTAKTLRDMDFCVETVLEPSTLDACGSLVKEGRFKWVINADEAPEQIEIFDIEKNLKKISSLSVIEGELI | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Subcellular Location: Cytoplasm
Sequence Length: 421
Sequence Mass (Da): 47706
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A0A920CW67 | MFFYILTLVVVLIDQGSKWWVRTFMEVGEHRSVLAPYLHFEYYQNSGAAFSSFQGYGKWFAYLALIVVGGLIYYRIKGKISGKLMELAAGLLAGGALGNAFDRLFYGKVTDFIVWGSGSGIMNIADLAINAGVLLFIIGMLLRNWRDKRSSYSFK | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
EC: 3.4.23.36
Subcellular Location: Cell membrane
Sequence Length: 155
Sequence Mass (Da): 17407
Location Topology: Multi-pass membrane protein
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A0A942RX58 | MSELIHSLGIEWKILIAQIANFAILFYVLKRFVFGPIMKILERREARLEADRRSSRELSVKLDEAALKEKEVLDTARKESERIISEAHAVATRLKGEIEANASREAERIIASGRAELAHDRTKAEAVLKKEIGSLIALSVEKAVGSALDRKAHEKLVEEARAIVMSNQRSL | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
Subcellular Location: Cell membrane
Sequence Length: 171
Sequence Mass (Da): 19182
Location Topology: Single-pass membrane protein
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A0A960AKB0 | MSTKKRRQELARAKAQRQAQRRAEAAKRGRRNRLIGIVAAGAVVAGAIVWAAWPSSTEQAGAEAEPETTTEPTTSPDETAAATPGPVATPAGVTCDEPGEPRQDTRTWNKPTDQKLSGDATWVLNTNCGRITVALDAEAAPKNVNALAFLTDEGYYTGNFCHRLTTSGIFVLQCGSPGSDGTGDVGFTVPDENLPTDGQDNYPAGTVAMANRGADTASSQFFLVYKDTTLPAAYTSVGKITDGLDVVKYVAAAGVQPGSSDASDGPPAQPIVIKTAAIEN | 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: 280
Sequence Mass (Da): 29169
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A0A0M2VBL5 | MKISKLALPGAVLLELEAHTDQRGYFAETYHQQQLDNALGYRVRFVQDNEALSQFGVLRGLHYQKPPCAQAKLVRVVQGSVLDIIVDIRFGSPTFGQHVTTELSANSARQLFVPRGFAHGYITLSEQALVQYKVDNYYSPVDDCGLHYADPALAINWLLAPAQLRLSAKDLSQPMLSELAAHFQYIADLNV | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
EC: 5.1.3.13
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence Length: 191
Sequence Mass (Da): 21301
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A0A3D4H823 | MVPDGSRKSRVDRFLAEANSEISRADFQRALDAGLVQVNGESVTKKDLVRAGDIVQFKLVATESLPMGPIDLGLLPVYEDDDLIVVNKPAGLVTHPGAGKPEPTVAHGLHYLCKGKLSLLGGADRPGIVHRLDRETSGLIVAAKTDVAYQALGELFRSREIVKEYLALASGVPELMSGSIRKNIERNPSQRHKMRVCQGDHGREARTDWTAEMLFRQGFSLLRCRIHTGRTHQIRVHLMSIGHSLLGDRVYGYRPLTNLPTEPDRVMLHAARLAFDHPISKEKLDITAPLPGDFIPFVEAERLD | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 304
Sequence Mass (Da): 33627
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A0A9E2U844 | MPSPDRHATLASRNAHKARELERLLPGWAIEPLVADDWPAETGDTYEANARIKAVFGREVLGPDATVIGEDSGLEVDALGGRPGIHSARYAPEGAPAIAKLLGELDGVDARDARYVSELVCLTPEGELRGSGTLTGRIAREARGHEGFGYDPVFVPDGERETVAELGDAWKERNSHRARAARALLAALAMTLLVAGCGGTDKTGIRVLRRFFAAGPVARKLGTRFPHKPGTLPCTVDDSGTTVQATCATDISLVKPDKAVVTLTEAWNHGAKAHTWFFFIRRDGSVQSVVQEGSPSPVTTTTSH | 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 a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
EC: 3.6.1.66
Catalytic Activity: H2O + ITP = diphosphate + H(+) + IMP
Sequence Length: 304
Sequence Mass (Da): 32418
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A0A949EYT6 | MMLLERIHKLINLNDRDKFNLSGESDIKKSNIELISQSGKIYFLLGGTRSGKSEYAEQFATSCSEKVAYLATAAITDEEMEKRVQQHKKRRSLSWRTFEIESENIDLPLMGEIVEKINASGCEVLLVDCITNLLFRLAYKYDLENLELIDNKLEKIIENEIASFFDNFLKLLKSARFDSIVVSNEVGLGIVPSYPFGRIFRDLMGVVNKKMAAAADEVYFFVAGLKQKLK | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = adenosylcob(III)inamide phosphate + ADP + H(+)
Sequence Length: 230
Sequence Mass (Da): 26209
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A0A9E3GS73 | HAALMLVLNLVAIAALYLALQSSFLAIIQIIVYAGAIMVLFLFVIMLLGVARDDLLFETRRWHRVVAALGGLLIAGLLVFGVAGELLGDASRCGGQADAETVAASTTTPCEGLDDALAGNDQGSVGIIAERLFTRWTFAFEISALLLVVATIGALVLGRRNDPVVATDRLVGTPEDDVPAGEDGLLPGSAHGPEVG | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 196
Sequence Mass (Da): 20347
Location Topology: Multi-pass membrane protein
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A0A9D8H858 | MERRAGPDLHGGHRVARDRWRDRRACAPGRDHAPPTDPRRALRRRDPQRHRPDRLVPRVRAAGPAHGPDPPPLRGRGLAGDDRHRAALAVRRRVRGPRARPLLRRLHPHPRGHRVTAGAPVRLVVVGLGVTGDAVLRWAAAAGHHAVVVDDRPDSVAPARRAVADALGVAVTAVPTGADAAALLAGTDLVVPSPGVPAHHPFLRAAATAGVPRRSEVDLAAELLAASGRTLVAITGTNGKTTVTELAVAVCRAGGVAAVAAGNIGAPLLDEAVAGTDPVVVAEVSSFQLAGTTAAFRPRVAGFLNLAADHLDWHGTFTAYGEAKARIFAHQGPGDVLVASADDPEVAALAATTPGRLVTFSVAPTADTGYRIGARADGAVLLTDDDREIVPVAAVRDPAPHDLANALAASALAAAAGVDPVQGGAALRDFVKGDHRMRVVAEIDGVPMIDDSKATNVHAALAAIRSFPRVVLIAGGRNKGLDLSTLRGGADHLAAVVAIGDAATEIAAAFRGVVPVSEAGSMDAAVRAAVDHAAVGDVVLLSPACASFDWYGSYAERGRDFARAVAALVEVRS | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
EC: 6.3.2.9
Subcellular Location: Cytoplasm
Sequence Length: 573
Sequence Mass (Da): 58969
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A0A2K9LL04 | MFLSEKWGALSGIGKAAFIVACFSALLLPLIGFYGFYSSDMAPIYQGLSEEDASKVVTNLSENKIEYQLKNGGRDIYVASDKLDAARLQLAGDGVRLGSGIGFEIFDEMEYGVSEFAQKINYQRALQGELSRTIASLDGIKYARVHLVLPEERLFEKKDRAPKASVNLMLEEDALVSATRIQGIQRIVANSVEGLSPERVIVSDNDGEVLSVLTEDGSFQVSATNQRKESLERALTRKCSDLMEKMFGYDRTVVNVDVSLTGAEIKRRTESVVGADDGLSGVLVSKRISTSNNRQNSKKTTAEAMDSSSQTEEMSYRTGTKIEEAVVSAGQIAKLSVSAVVPVSVTDRQLEDLSDLLKTTVGFDSERGDSIAVRRMAFVDINATNEKIVKSVAEPKNANDVGLVRKSSAPIDALGNYSVLIGVGGVLVGFVLFLLSFFVRRPRSLSDSEREILLENIQSWIASDEAAIEGERIR | Function: The M ring may be actively involved in energy transduction.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 474
Sequence Mass (Da): 51688
Location Topology: Multi-pass membrane protein
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A0A951NCA7 | MGFRAKPRAMSPSMLRSARLAAVLLPVGLLSSGCSLREAYEDTFSLGFPKPVTEEALSIYNLWLGSVAAAAVVGVFVTFLILYAMVRFRKKGDTLPRQVRYNLPIEVLYTAVPFVIIAVLFYYTTVSQNFVLDERDGGADVNIGVVGFQWNWTFRHDDAGVQVTGETRKPAQLVLPTNTRIRFTETSPDVIHSFFVPAFLFKQDVVPGRANTFEITITKEGEYIGRCAELCGEKHSAMNFSVKAVSPEAYADYITVLQADPANSIGTTAGDGSVRSAEQAKELIEGRPS | Cofactor: Binds a copper A center.
Function: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
EC: 7.1.1.9
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Subcellular Location: Cell membrane
Sequence Length: 289
Sequence Mass (Da): 31719
Location Topology: Multi-pass membrane protein
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A0A942NQU3 | DVPGLPRFNGGLVGYFGYETIGYIEPRLRAGAKPDPIGTPDILLMVSQDLLVFDNLSGKMLLLTHADPAQDNAYHNAKARLDRLVAKLREPHAHPQPHASVKHVHENDFVSGFTQQGFEDAVRKAKQYITDGDCMQVVLSQRMSIPFGASPLDLYRALRCLNPSPYMYYLNLEDFHIVGSSPEILVRLEDNEVTVRPIAGTRRRGETHEQDLELEKELLADPKEIAEHLMLIDLGRNDAGRVAKIGSVKLTDKMIIERYSHVMHIVSNVTGQLQEGKNAFDVLAATFPAGTVSGAPKIRAMEIIAELEPVKRGIYSGAVGYISWSGNLDTAIAIRTAVIKDQTLHIQAGAGIVYDSVPRSEWEETMNKGRAVFRAVSMAEAGLGGKA | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.
EC: 4.1.3.27
Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Length: 387
Sequence Mass (Da): 42560
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A0A9E5ERI4 | MVTADSRTLVIGANGQVGSSLLLQLGAAGIGISRNDADFSSRSDLFRALDAAGPARDVVNAAAYNAVDRAESERSEAFLINADLPRWLAEWSAARGVPFVHYSTEYVFPDGNGAAWREDDAPSPLNVYGESKLVGERAVQQVHGDSVVIRTSWLYSAGKNNFVRRVLELAAGGNPLTMVRDQVGSPTDAVDLARTTLALLQRDDREAVFGNQLLHVAGSGSVNRAEFCRAIIEAGARVGVIPHIVSVIETTTSEYAAAARRPTNCVLDCSKARALGIELAPWHESLTRVVQEMVV | 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: 295
Sequence Mass (Da): 31601
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A0A8J3IV80 | MAVLTWARADTMRVLVVNCGSSSVKLRMLDGTDTVTGHADLAAVAGEFSLASLRQALTGLGPADAVGHRIVHGGREFRGPVRLDPDVVAGIAELRDLAPLHQSFGLAGIRAVGELLPDVPAVACFDTAFHTDLPYAAATYPVPAEWRERYAIRRYGFHGLSHAYAARRAAELAGLDASTARVVTCHLGSGASLAAVRGGRSVDTTMGFTPLEGIVMGTRSGTVDPGLVLWLQTTAGLSAAEVSRALEAHSGLLALAGTQDMATILSRYRAGDRAARRTLDVYQHRLRAGIGAMTAALGGLDALVFTGGIGEHAPEVRAGAVAGLAFLGLAVDPDRNAAPVPDADVTADPAPVRTLVVEAREDLEIAAQVRTVLTG | Cofactor: Mg(2+). Can also accept Mn(2+).
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
EC: 2.7.2.1
Subcellular Location: Cytoplasm
Catalytic Activity: acetate + ATP = acetyl phosphate + ADP
Sequence Length: 375
Sequence Mass (Da): 38944
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A0A847DD56 | MSVFKIKKVLIISVTISILAVAGIITGTGFYLTAPMAHHGDNRVFIIQSGMNLRNISDLLEKEGLIRSSLAFMIRVRLKGMGRMIKAGEYSLNPSMTPERIMEMITRGEVVAYNVTIPEGFTIAQIADVLSSYSLITKEEFLQYVNQHDIEKMYGFIGPGLEGYLYPDTYRFARGLSAKAIVDAMIMRFRTITAPLEGRILESGINLHEVITLASIVEKETGNPDERPLIASVFLNRLKKNMRLDSDPTVIYGMKDYSGNIRKKDLAAYSPYNTYVIKGLPPGPIANPGYHSIKAVLFPADTEFLYFVSKNDGSHHFSKGLAEHNRAVRIYQKNALKTKN | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 340
Sequence Mass (Da): 38007
Location Topology: Single-pass membrane protein
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A0A9D8H813 | MTLIVAIDGPSGSGKSTVARGVARELGLDVLDTGAMYRAVTLAVLKSGVDPADAAECARIANDADLQVGAHVMLGGEDVTEAIRGPEVTSTVSQVSAHPEVRHELVDRQRAWIDERGGGVVEGRDIGTMVFPDATIKVFVTASDEERARRRQRDEVAAERAVDVDSVKEDLARRDRADSSREASPLRAADDAVIMDTTDRDVDDTVQDIVERVRAVSD | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 218
Sequence Mass (Da): 23377
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A0A2A5XAI0 | MRVGLFFGTFNPLHNAHIGICNKLLEKKLIDEVWLVPTPHSPDKNPEKLIDISIRLDMINLVIDKIRNVKVSEIELGMKKPNFTYLTLKELKKKFPHNEFVVIMGEDNFLNFDTWKNNKFINSNFQIIPYPRSKRSTNDIFDDYFDISSSAIRDLVKRNSDISDLVPEVIGNYIKRKALYR | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 181
Sequence Mass (Da): 21200
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A0A938F981 | MAPLIVGCSPIGNPGDASTRLRDAIESAELIAAEDSRKFSRLATDLGVRYQGEVISFFDGNESSRTDQLLKAIESGRSVLLISDAGSPTVSDPGYRLISEVIKRRLPVEVLPGPSAVITALIYSGMPTESFTFDGFIPRSDLARRAYFSRLLEERRSCIAFESPKRLIDSLRVASEIIPKERGVAICRELTKEYQEIFRGSVELALKWAEEREKGEGIKGEITIVFSPATEISQASDSEILELVDQMLEDGLSARDAVIESSKRLSIPKRYVYDLVIKREE | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.198
Subcellular Location: Cytoplasm
Sequence Length: 281
Sequence Mass (Da): 31134
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A0A194AFF7 | MTSQKLIVALDFPSREQALAMARTLSGHVRWVKVGLELFCRTGPEIVSTLDNLGFKVFLDLKFMDIPHTVQGAVTSACAAGADMLTIHVTGGQAMVQAALRGARMAGKKPPLLIGVTVLTSMSSNDLALVAGRSRNLEDTVSSMAHQARTWGLDGIVCSGQEVQRIRQQCPEPFTIVTPGIRLKKDLDSEDDQKRVTTPKAALRAGSSYLVVGRPITRATDPVGTIQRYLDTIEEQS | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
EC: 4.1.1.23
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 237
Sequence Mass (Da): 25616
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A0A2M7DTZ0 | MFYPDLNKFKQLAKRYNIIPVYKEILSDYDTPVSTFHKLAGDSDYAYLLESVEGTERWGRYSFISSSPRIVFIVNKGQLTVHYLDSGSKKEVKKIKTDNPMDELKRLIGKYKSPQIPGLPRFWGGAVGYIGYEMVCAFENRIARFNSAQKDYLNIPESIFMFTDSLVIFDHFTHKTKLVSCVDLSAGLSNLSAGLSYLSNEGDGRNIELKYRNACSKIDKIHIQLKKPLSEHSYHKDKSYRVNSNMTKKKFLDRVKDIKKYIRAGDVIQTVMSQQFSRKTSVRPFDIYRTLRTVNPSPYMYYLNMKNFQLIGSSPEILVRKEGDMAETRPIAGTRPRGRTPEEENRMEKELVGSPKECAEHIMLVDLGRNDLGRVCEKGSVKTNQLMTIEKYSHVMHLVSSVAGKLSPKIDAFELLRACFPAGTVTGAPKIRAMEIIGELEPTVRGPYAGAIGYFSYSGNMDMAITIRTILMKDSIAYVQAGAGIVADSLPEHEYQETENKAKALFSAIDLAERVI | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.
EC: 4.1.3.27
Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Length: 516
Sequence Mass (Da): 58408
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A0A2A5X6T0 | MISFFTKVIMFPFSVVYGLFIILRNFLFDIKYYRPQKFNKKVIAVGNLIMGGSGKTPHVEYLVEILLKRKNNISIISRGYKRKTSGMIILSDKDDFRTVGDEPIQYFKKFKNEVKVMVSENRVNALNVNETDKIDVNILDDAYQQRLVKPDMNILLSSIKRPFYNDYIFPVGMLREYRKNANRADFLIFSGCDKEMKETERDEVILKAKQYLNINTPILFSHVRYDEPKKVFGNKFHKDVIAISSIAYPDSFFSFLQSKYKLIKTFKFKDHHIYKDKDLLKVIKECDGDISILTTEKDAVKLCEYKHLLGSYSVYYVPIKVSFLFNNSISNYLGE | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
EC: 2.7.1.130
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Length: 335
Sequence Mass (Da): 39236
|
A0A966XGV5 | MRIVRSWLEEFVDVRKVSDEQLADAITSLGLSVEATEVVGTAIAGVVVAKVLRTERHPEANKVHRVWVDAGDGGERHVWCGAFNMKAGDLVPLATIGTKMPDGREILRRGMFNIDSEGMLCSAAELGVASDASGILILPATAKLGRNVFDALGIARDVVFDLDVTRNRPDCTGHLGVARDVAAKFGKKFTPPKGDGGKKGTPRKVPVKIIADKACARFNVTVMSGIVVGPSPDHLARRLLAAGMRPINNVVDASNLVMLETNQPNHAYDAAKVASGFRVRFATTGERLVTLDGTNRALTTDDLLICDGDDRAIGIAGVMGGANTEISDVTTEIALETAWFDPTTVRLTSQRLALRTEASARFERGVDPQGVDYSVARFAAILRQSCPKLVVHGGASDPKTKHLPKPAVISLRVAQVNRVLGTSLSARDVSAVLTRIGFDCSPKKIAVKKGSLVAAGPGFSVNVPSWRPDCTDEIDLVEEVARHVGYETLGKRVSQSTQPGGLSPLQQRRRALRDLVLSFGASEAMPNPFLAPGDHEKAGVVTSENRSGSALSLENPLVAEESILRTSLRPGMLKAVAFN | Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 579
Sequence Mass (Da): 61747
|
A0A965E4C3 | RGGDVTYHGPGQLVVYPIRSLPGKHGDSSPADITAYVCSVEQLVIDTLAELGVVASRKAGYPGVWLDAETPRARKICAIGVRIARGATARRTMHGFALNIDTDLRYMRDHIVPCGIAEHPVTSLREEGCTASMREVADVVARLASERWGSGVSDRHDVAWQYEPDVVGMHITQRKPEWLRPHVEHGTDVLATKKTLRDLHLVTVCEEAGCPNLSECWKAGTATFMVLGERCTRACGFCLVDTRKPDLPDVDEPRRVAEAVARMGLSHAVLTMVARDDLDDGGFEHVARCVQAIRERTPGTAVETLVSDAKGDDSSLEKLFAVRPEVFNHNIETVARLQRIVRPSAGYARSLSVLARAKRAGLVTKSGFML | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
EC: 2.3.1.181
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Length: 370
Sequence Mass (Da): 40465
|
A0A966K0Y0 | MNDKISLTGISGFGYHGVLESERKSGQEFLVDVVLYCDLSEAGKSDDLSKTINYADVAALIHKRIIGESVNLLERLAQLIAEDIINNFDVNGIQKIKEDFGVQKFDLAVIDGSEFLGDEEFNELPNCDAAVSSPVA | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
Sequence Length: 136
Sequence Mass (Da): 14840
|
A0A3D4HCT3 | MSLLNGSSHPAWKGFNILPMQIELCCPAKINLLLAVTGRRGDGFHDLISLVAPLEFGDTLRLSRSPNNRGIRLRTEGIELSEGADNLAWRAAEGFFDRFGIEEGLDIEIVKRIPIGAGLGGGSSDAAGVLRGLSALFGIDDGKALLELAAGLGSDCPLFLNGKPLIMRGRGEELEPLGGPCRQSLVGTSVALFKPSFGISTVWAYKALAAKRSCYASADDVENVLDRWRNGDLPLPDLLENSFDSVVGAKYPGIPLLLERISDDTGCRGLMSGSGSACFALGSSHEYGRIKEIVRECWGEQAFFQETTITDIGLTEYPSISS | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Length: 322
Sequence Mass (Da): 34451
|
A0A966WET9 | MLTFGTDGVRGEFGKELTERYAASLAEVVAQILQCKVVVVGRDTRESGVLLELAITKALMGRGVEVQLMGVAPTPAIAFAARQHNVVAIAITASHNLYQDNGIKIFGAGGRKLSDDEQQRIEHEMSLRDGATGNVESNMAPSAIVGAASSTTNSLARPELLQEYCDWLVASVRHGALENLHIALDCANGAFSMLAPEVFSKLGATVTTMNATPDGRNINLQCGATHPEPLSEVVKSVGAHFGVAFDGDGDRLIAVDELGRIVDGDHLLAISALQMKQQGTLRNNKVVVTVMTNIGFHQAMKGAGIEVVTTPVGDRSVLVALEENSLSLGGEQSGHIIYRDFATTGDGLFAAIKLAVFVADSKKLLSEIAEQAMTSFPQVLINLRVAKRVDAIDQMFKGEIETAQKSLGDSGRVLVRASGTEPMVRVMVESQQQSTAEKVAATLADAISARLG | PTM: Activated by phosphorylation.
Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
EC: 5.4.2.10
Catalytic Activity: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
Sequence Length: 452
Sequence Mass (Da): 47889
|
A0A928TG86 | MHSDPRTNSQATMSSRFQAPRGTQDVLPAMQPYWSAINDAILAVTRLYGYRRIDTPIFEAAALFEKGSGDTTDIVEKEMYVFTDRGGEALALTPEATPAICRAYLEHGMGSWPQPVRLYTTHPMFRYDRPQKGRYRQHTQFDCEVLGSGDPLVDAELIGLLWDLYRRLGLKGLQVRLSSIDDPGPRRAYVDRLKEYYRPFLGDLSEDSRRRFERNPLRLLDSKDDRDAPYKSDAPKLVDHLSPPAAAHHEAVTAALAALDIPFVIDPLLVRGLDYYNRTVFEIVPVEDERAQSTIGGGGRYDGLMEILGGPPTPGIGFGCGFERVILEMQKNGVEPAEGPQASVFVVHRGAATAAAALRAVAALRAAGLPALPGEGERSFKSQMRSADASGARVAIILGEDEVARGTAIVKDLRGEGGQREVPLGEVAAAAESLLASFG | Catalytic Activity: ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)
EC: 6.1.1.21
Subcellular Location: Cytoplasm
Sequence Length: 439
Sequence Mass (Da): 47922
|
A0A0M2V6W3 | MVNAPRFSWRFLLPQYWLLWLGVGLLWLISWLPYRLLMLMGSGLGALLYRLLGSRRKVAARNIALCFPDMPDAEQHKLLKANFAESGKALFETIIGWWWPTWRVRKLGQVQGYQHIEAAMAEGKGVLLLAGHFLHLEAACRVFGLTHPSVGFYRPHNNPLMDYLQYHGRNKANKYMVGKRDVKGLIQALNEQEVCFYLPDQDYGRNRAEFVPFFAVAETATTTGTLLFAKAANCVVIPVYTYRLPGYQGYQIDVLPAFDHFPSGDNKADVTRVNQWVEQAVLKHPEQYMWLHRRFKTRPSPDAPSLYKAAPDNSGGRH | Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Function: Catalyzes the transfer of an acyl chain from an acyl-[acyl-carrier-protein] (ACP) to a Kdo(2)-lipid IV(A) to form a Kdo(2)-(acyl)-lipid IV(A).
Catalytic Activity: a fatty acyl-[ACP] + an alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA = an alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(acyl)-lipid IVA + holo-[ACP]
EC: 2.3.1.241
Subcellular Location: Cell inner membrane
Sequence Length: 318
Sequence Mass (Da): 36410
Location Topology: Single-pass membrane protein
|
A0A9D7RYV9 | MHSLLERIANLPWASYAAHWALRLSLALLVLLIGLWLTRLATRLLTRVLTRMNVDPMLREFLRNLASGALIVVVVVGALDQAGVPMTSILAALGAAGLAVALALRDSLSNLAAGVVLLLLKPFRAGDLIGIGGQTGKVESLRLMHTVLLTPDNCELILPNTRVANEPIMNYTARASRRIDLIIGIAYRDEVGRAFDIVRGVLAAEPRVLKEPQPALLVDRLAESSVDLAIRPWVATADYLETRAELLRRLKEALAAAGIDVPFPQRELRVVHENAPTPAAQLGAAAD | 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 conductance with a slight preference for anions.
Subcellular Location: Cell inner membrane
Sequence Length: 287
Sequence Mass (Da): 30988
Location Topology: Multi-pass membrane protein
|
A0A965EBQ9 | MSGTLSTLDSIILGIVEGITEYLPVSSTGHLVVVQRWLGLGDSAGRDAADTYAIAIQVGAILAVLLLYRRRVSSMLNGVIGRDAEGRRLLGLLVASFIPAAALGAAFGDAIKDELFSPGPVVIAWIVGGIFLLVWKPRTEGVALTSLTGKSAVVIGVAQALALWPGVSRSLVTIAAAVLVGLSLSAALEYSFLLGLATLTAATVFDLAKNGGELFDAYGIGRPLLGVAIAFVTAAVSVRWLVGYLARRPLSHFGWYRLAVAALTLALWSTL | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Cell membrane
Sequence Length: 271
Sequence Mass (Da): 28213
Location Topology: Multi-pass membrane protein
|
A0A835AIE9 | MDRARREREDRRLLDLAVECGFDRSVAANCLARLLDLYGEDGVVFVTVEKIGDDFLASLADATQPVDDWDDLKGIETEACGNLNDMMMKNVPNSSRAPDGLEAFDFPLDNLDFDMGDEIDNLRNNSSGIQRQLCCLDNVNLANVVIFGNKSFRPLQYEACRAAMDNQDCFILMPTGGGKSLCYQDQIVALTYKFAVPAAFLNSQQTPAQASAVIQELRSGKPSFKLLYVTPERIAANYTFMEILRGLDQRGLLARFVIDEAHCVSQWGHDFRPDYRGLGCLKENFPRVPIMALTATATESVCKDVLGALKIPNAVILKRSFDRLNLNYEVIGKTKTAQEQLGDLLKERFMNKSGIVYCLSKNECADTAKFLREKYKIKCAHYHAGMAARQRTSVQEKWHSGEVKVICATIAFGMGIDKPDVRFVIHNTLSKSIESYYQESGRAGRDDLPAHCIVLYQKKDFSRIVCMLRNGGNFRSAMEQAKKMQAYCELKTECRRQALLEHFGEQYSRQKCRDGPSPCDNCLKT | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 525
Sequence Mass (Da): 59087
|
A0A1X0CUR5 | MSAAARGRGQNKVVHMMAPELLGGRYEVRGVLGRGGMAEVREAIDTRTGYSVAIKLLYAGYDTNPEYLHRFWLEAQAASALHHPNIVNVYDSGQHRGAPYLVMERLPGRSLAEVIAMGPVPPPYVRRMLVEVLAALSAAHAAGILHRDIKPANILFTATGSAKVADFGLAKGPETFHTQTGQIMGTMAYMSPERLTGRPATVSDDLYAVGVVGYEALTGRRAFPQENLVALARAITENPPPPVAVLRPDIDPQLAAIVDRAMTPEEAARFPSAEAMMAELIDVGGDPVTGPLPMLQPAAPVAAPAPVPQPVPAQAHAPVMAPSPPVIMVPQPVLMRRPIWHLVLLVAVVVALVVGAVAFILGASTAPTGGPAVTTVTTTRPIHPGRPGSFG | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 391
Sequence Mass (Da): 41188
Location Topology: Single-pass membrane protein
|
A0A7V0NUS0 | MSADSARFRRLTSTDLMFLRLESTAWPAHFGGLAVLEGAALLDDTGKLRLGEIRDRLDRRVAHVPTMRQRILRPGFLGGRPLWVDDQEFDIRDHVHERVARSPGGDAELLEGAAAVYGGLLDRSRPLWELWFLTGLSEGRVGVLLKLHHAVADGLAAVAVMASLFDFEPDAPDPDPVAPVREPLPGSWSLVVDNVSSKMHAVRRAARAVAHPTQLVKRVRTFTHVARRSFGNQAAPGNSLNQPVRAGRRVQSLRLDLASMKDVAHAHQGKVNDVVLDLWSGGLRRLLTSRAEPVAGVELMTALPVSLRSPTGTTTVDNQVGTMVLPLPISEADPRRRLEMIVATTRKVKEEQRPAAIMGFLAALAATPIGRSFATRQRSTNVLVTNVIGPPVPVYLLGAPVLDVLPIIQLIGNIGLTLCAFSYAGQISLVVTADATAFPDVDELMAGMERDWHELADSPGPAGP | 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: 464
Sequence Mass (Da): 50232
|
A0A7V1H199 | MPTDIISELRKETGKLDIELTSAQEDRLLLYAKILAQENEKSNLTAIPVQKFVTEHFIDSFTVLKTDKIRRNMKIADVGAGAGFPGVPIKILETGISLYLIEPNNKKASFLRKLVEKLGIEGVEIIRARAEAAGREPDLREKMDVVVARAVAGLPVLLEYALPLCKVGGWFLAMKGPSVEEELGPARLAAAELGSKIDSVLKPYGRGHSKQRTIVQVQKDLPTSERYPRRTGIPVKRPLGGHFS | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 244
Sequence Mass (Da): 26875
|
A0A7V1CJP0 | MNTDKTLASQEYREDDREKLKGLLKEAIVFKETTLASGKKSHYYLDARLITLSSVGALLVSRVLLNMLQDYDVDAIGGMTMGADPIVSAVAVLGCLEDMSIDAFIVRKQAKEHGRQKQVEGPSIKGKKVVIVDDVVTSGGSLLQTVDAAQSAGAEVVLTTCLVDRQEGARDLLDKRDLKFEPVFTVKELL | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
EC: 2.4.2.10
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Length: 190
Sequence Mass (Da): 20699
|
A0A966VPZ7 | MCVAGDLVEPLARAARVSDELILSITASGNLVVVKTPPGGAHLLASALDRASQSGEMKAVIGTIAGDDTVLVISRNATGGKALASDLRDFISPKKARRK | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 99
Sequence Mass (Da): 10153
|
A0A944UGX5 | MRTFFDSNSMDSNECISLDEMESHHLSKVLRLNKGAEVEALDGKGNIYYTEIHTLDRNNIILKILNKRFIEEAKPFLSMAIAMPKGNRWEYMIRPLTELGVRRLTPLLTDHSECYNQEKKLDAKRHKWKKIAEDACKQSGNPWLPILDPPQPFSSFLENISLDETVCIGSLAKYAHPFKKLEFKPRDFVSILIGPEGGWSEAEELRAKENGVIPFSLGSNTLRLESAAVAGLAVARERFIL | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
Subcellular Location: Cytoplasm
Sequence Length: 241
Sequence Mass (Da): 27420
|
A0A966J3P4 | MTRHDPRIAVVGGGISGLSAALELALGTEGRADIALLESQERTGGVIRTSEFAGLPVDEGADAFLRRVPDALEVAAAVGMRDLTAPTGASAAVWVDRLRPLPEGLLLGVPTSVRSLVRSQLVSPRGSARALADLVLPSRGLEHDSIGTWVRARLGSEVHDRLIDALVGSIYAADTDRFSLASVPQLDGLARGGRSAILTALRTRRPPTGEPIFAAPPTGMGSLTDAIVSRIVELGVTMRIGRAVDRIQAVDGSVEIDGERFDAVVLATPARVSARLLETSAPTAASALASIEAAGVIMVTLAVPAGSLPPSCSDLSGYLVPKSRQRSVTAVSFASSKWAHLRPADGSQILRVSLGRDGLDMDDLDDDDTQTRVIDEVSLHLGCDVAPTATRITRWPGAFPQYRPHHGALVASIEGSLPQTIVAAGASLHGIGVPSCVASGRRAARTVLERLGLGHPPNGDPVRP | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III.
Catalytic Activity: coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2
EC: 1.3.3.15
Subcellular Location: Cytoplasm
Sequence Length: 464
Sequence Mass (Da): 48306
|
A0A2K9LP91 | MILSDSLATQSNILSPRQWLMLLASMLMCIGLVLVASASMDMASLNYGSPFFFVQRHGVYLAAGIVVGCLVYQIPLAVWERSSGALLIVAYLLLALVLLPGIGRTVNGSTRWIQMGPVNIQVSEIVKVCALMYVSGYLVRRVEEVRSTLWGFLKPVMVLSVMVLLLLKQPDFGAVVVIMTSVFAMLFLAGVKVSHFSLVVFGSVGAAYALVASSEYRMKRVIGYIDPWADQYSSGYQLVQSLIAFGRGEWTGVGLGNSIQKLFYLPEAHTDFVFAVMAEEFGLLGNLLVIGLFLVLVVVALRIGREAEKLGKLFNAYLVYGLATLIGLQAMVNVGVASGLLPTKGLTLPFISYGGSSLIVMCVVLALIMRSDRENQMGDSESTRSGKDDTRSSKNSVGKRPAKRSGSNVKKEPVL | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Peptidoglycan polymerase that is essential for cell division.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
EC: 2.4.1.129
Subcellular Location: Cell inner membrane
Sequence Length: 415
Sequence Mass (Da): 44944
Location Topology: Multi-pass membrane protein
|
A0A9D8GZA8 | MPATLPTINATDTSVIDEVLVLGFALDNKSKKYSILSGDLQVDQGPLLRALADLQASGASDEVIKLPGSSSKLILLTALSALPNGSIAHEVLRRAAGAAARALAGTSSATFALPQNSKQDFQAIAEGALLGAYAFDEFRGSSKADRKLALKKITLYSKKAKNKSYVQGIKRAEIIAKYTHLTRDLINTPPSHLTPDSFSQRFKGIASSLGVKVEILNETQLRKGGYGGIVGVGQGSANPPRLLRLSYSGKGAKKRYAYIGKGITFDTGGLALKPAQGMEAMKSDMSGAAAVCAAVLAIAELKLPIHVDAWAALAENMASDKATRPSDIITIYGGKTVEVLNPDAEGRLVLADAMVRAAEVGKKAGGLDGMVDVATLTGAQVVALGTRTSAVMTNNEGFRAQFLALAEITGEAFWPMPLPEELRESLDSPVADMANIGDRMGGMLVAGLFLKEFVDSELPWLHLDIAGPAYNEAKAHGYTPVGGTGVALRTLVALAESSSAK | 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 Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Subcellular Location: Cytoplasm
Sequence Length: 501
Sequence Mass (Da): 52435
|
A0A929L3N0 | MSDVQNSALPVNSGSQQRPDYENQILELISKTISPKALRDELEDYHANDIADAFTRLDDAAREKLFKLLDADRLAEIIPYLDADEQAGYLNSINIKKTLAILAEMEPQDAGRILKRISKTRREVIFELLDAETRRNLKRIYAYSDDEIGSQMSTDFIEIPRYYNIKETMRSLRDQARESDTDNISLVYVIDENGLYYGAIRIQDLFAARANTNLEDIIQVNFPIVYANETIDSLMEDLKDYDEDSIPVLNNDNQIEGIITKSRLLQLFDQEMKEDYAKLAGLSAQEDLKETVFRSIVKRTPWLILLLFLSLLVSAVISMFESVVAKLTVAVVFQSLILDMSGNVGTQSLAVSIRVLADPELTRTQRWKLMLKEVRAGAVNGLIIGTGSALVLTLFIHFFSGYVWLQASAIALCIGLAMVTAMIISSFTGTAIPIALSAWGIDPAAASGPLITTLNDLIGATTYYSMIWVFLIQMLHI | Function: Acts as a magnesium transporter.
Subcellular Location: Cell membrane
Sequence Length: 477
Sequence Mass (Da): 53432
Location Topology: Multi-pass membrane protein
|
A0A365YS74 | MPPDAGAHQGGAGPPRRPRHPNAGPPGRERLRGRRAPGRSGYVRRLTAALWLVALLGGLAASGAPAAAGARAPDAFVDLADVAPGIRQEIRYATRDNFTGRVVDGYREPVCLLTRDAALALRRAHRALGERGFGLLVYDCYRPRRAVESFLRWADDPDATGRREEFYPNVPKDRLFEEGYLAERSGHSRGSTVDVTLVRRSGRQVDMGTGFDFFDPRSAPSSRDVGDEQQEARAVLRAALTAEGFAPVDTEWWHFALEDEPFPRRQFDFPVDKGALSKGR | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
EC: 3.4.13.22
Catalytic Activity: D-alanyl-D-alanine + H2O = 2 D-alanine
Sequence Length: 280
Sequence Mass (Da): 30846
|
A0A2J6SXL0 | MSESASHLIRLRYQTQHNIWGKCGNQSLVRKLAISGSLANPLLAYDQPYAELWMGTHPTLPSHDFNTNRPLLKIIQEKPHLLSETISHRFGTDLPFLFKVLSINKALSIQAHPDKVLAERLHLLDSAVYPDKNHKPEMVIALTTFETLCGFRSVEELSGLLSRIGPFQQLVGDEATQGVHLAARMGNDSDQEAEIAIRNAFVALLAADSERVKACCRELVVLAQSSKERRSQNTGLESPGLAELVIRIYEEHPDDIGLFIMFFMNHVRLDPGEALFIQSGELHAYLKGDVIECMASSNNIIRAGFTHKIKDIEHLIPLLNFSDGLPRRIAPVPNNGVKFSEHQSPSVSTAVLYNPPAEEYKVGRITLGHKGTQANFGPTIGPSILICEQGKGTISVDGNIDNIELGYVFFLADGAFVKLENSSDELFISYGAFCGAGGA | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.
Function: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
EC: 5.3.1.8
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Length: 439
Sequence Mass (Da): 48278
|
R7GK06 | MSKIVVVEGTHDEALIKQVFKGQACIVTNGSEISKETLEMISSLSKDNDIIVFTDPDHPGERIRARVHEVVPKAIDCFIKKSDCISKNKKKVGVEHATSEEIKELLGPYLEGDIKAKGNITRNDIVALGLTGSNSSPLREAVSSKLNIGRPNAKTFLNRVNMLGITVKKLNEIVGEINGKNR | Function: Required for correct processing of both the 5' and 3' ends of 5S rRNA precursor. Cleaves both sides of a double-stranded region yielding mature 5S rRNA in one step.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 21 and 42 nucleotides, respectively, from the 5'- and 3'-termini of a 5S-rRNA precursor.
EC: 3.1.26.8
Subcellular Location: Cytoplasm
Sequence Length: 182
Sequence Mass (Da): 19904
|
A0A965IK24 | MQSPRTPVSWPAPVAAGPVIGRVSVPGSKSITNRALLLAAISDGPSTVTNVLAARDTSLMIGALESLGATFANVGQSRMHVTPISKGRQIGSVAIDCGLAGTVMRFVPAITGLVAGSVTLDGDAAARRRPMTALISALQQAGIAVTSKGECLPITIEATGAIAGGNISIDASTSSQFVSALLLAGATYDSGITLTHTGTTLPSLPHIEMSIAMLREHGVAVIESRTDQWQWGVAPSAIGAINRTIEPDLSNALPFIAASVVTAGSTTVNDWPTQTTQPGQLALPILEAMGCTLALAPADGAHQLTVTGPERIHSVDVDMSAMGELVPTIAAICFFADGPSRLRGISHIRGHETDRIAALIDIAERIGAVCRDVDGDLIIEPLHHTQLRAASDGPTVTIPTYDDHRLATAGAIIGLRRAHVLVENIATTGKTMPDFPAMWESLVSAR | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Catalytic Activity: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate
EC: 2.5.1.19
Subcellular Location: Cytoplasm
Sequence Length: 446
Sequence Mass (Da): 46138
|
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