ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
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stringlengths 117
4.4k
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A0A399RKT8 | MSGSEWTDPRPMSPHLQIWKWHWTMAASIFHRVTGVGNYLGAFLISVWVISIAAGPEAYGVVEGIMLSPVGQILLFFWLTSLLFHFANGIRHMIWDGPKAGFNPKTASAWSVFNFAFAIVAAATIWSLATNLF | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Membrane
Sequence Length: 133
Sequence Mass (Da): 14770
Location Topology: Multi-pass membrane protein
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A9A3V3 | MNAQVISSEAKEINLSITETDIGILYLIQHELLKESNIDFAGVIVKHPLTNECWMRINSSSKPLGEIKKATDSAIKMADEFKQLFNSKLKVN | 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: 92
Sequence Mass (Da): 10334
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A0A960HUF5 | MSVLEAIVLGIVQGLTEFLPISSSAHLRIVPELFGWDDPGASFTAVIQLGTMAAVVIYFWGDLWRIAGAWLASLR | Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Membrane
Sequence Length: 75
Sequence Mass (Da): 8146
Location Topology: Multi-pass membrane protein
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A9A2X3 | MRLVIKYGGTSISSAKDIRAVANHLNSLSKKNQIVVVCSATSGTTDDLIEISQSIKKENKSKAEQLASKITNRHKQLAKQTIKKADLRKKLLKNFDDDFAELVALIDGMVLLGEVTPRTMDYLFSFGERLSIKLVSMAVNDSGKKSVPLTGKEVGIVTDSNFGESKPLIDTTRLRVSKNVENLFSKKTVPVVGGFVGADQHGHVTTFGRGGSDYSATIIGTCIKADEIWLMSDVDGLMTADPKIVKNAKLLKEVSYIEAIEMALFGAKQIHPRTFEPLLSKKIPMKIRSSFNLKNEGTLVTASPSPSVKNTVKCVSNVRNNGLIDIQGGSMVGTPGTAAKIFATLAKAGINVMMISQNPSESSITIVVKNADLDKAVSSLEMELLGKIIKKLEVTTNVAIIALIGSGMRGTVGVASKVFGAAEKNKVNVSMITQGSSELNLAFVVKNSDTNAAVRALHNAFALDKIN | 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: 467
Sequence Mass (Da): 50068
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A0A961G3R3 | MIEKLPAWLRDRFPPDKPHLVGVSGGLDSLVLLDVLRTIGYRELIVCHLNHGLRGRESGGDAAHVRRAAGALGLPCEVEKVPVSDLAAISGLSIETCAREERWLFFGRMSQKWGCRTVFLAHHRDDQAETVLARLCRGTGVRGLGGMRFCHEIRTAQGIDLELVRPFLEIPREALREWAVGKGLKWREDKTNAEPIATRNRIRNEALPLLEDIFGRDPRPALARLATLAAAESSWMESLAREALEQARDESGALRVLNVAPLPEAVQRQVLRLWLEDTGLPGVDQADVEAVRSLLTFSPGSSGRINLPKNKHCRRQAGRLWIE | 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: 323
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): 35976
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A0A0R2V9M3 | MPNLHTVRKGLDLPILGAPDALVDGHLRASVYAVRPSDFRGLVPKLAVKEGDRVLAGDVLFTDKADPRIRITSPVSGEVARVERGDKRKILAVVVLADSQQEYRKFTSGTPANREDAINWLLESGAWSLVESRPYGRIANPDAEPKAVFINGMATEPLAVAPAVALAGREEDFAMGLQVVGLLSKRTVLSIAASETAPALTKASGVELHQFKGPHPAGTTSVHINQVSPLNKGEVVWTLNYQDVIILGHLARTGNFKLERVLALSGTGIAKPRAITAVAGASLEAFLNAELKSGNYRVISGSVLTGTKVSKAGYLTYYASQLTAIPEGEGTDFFGWVLPSFAKWSVSRTLFSWLTPSKKFDLNTKQHGEDRAFVVTGLYEKVFPFDILPMPLLKAMWAKDLEKMEQLGAYEVVPEDFALCEVVCPSKQELQKLAEEALDLLYTEMN | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
EC: 7.2.1.1
Catalytic Activity: a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+)
Sequence Length: 446
Sequence Mass (Da): 48456
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A0A6P6M268 | MLRLALQVRPSGRFTRPSVLPGPAAAASQRSGPVSCHHLRRYQSNGPARIQSLCHGRREYNSILSNGSWGLRSRMASFSQSMRMYSLPPHQKVELPALSPTMQTGTIARWEKKEGDKINEGDLIAEIETDKATVGFEMMDECYLAKILVPGGTRDVPVGGVICITVDNPDLIPAFKDLTLDKLSSSAPPAAASPDPPPPASPAAAPAPLQVPGSSYPPHMKIPLPALSPTMNMGTVHRWEKKVGEKLIEGDLLVEIETDKATVGVEVMEEGYLAKILIAEGTKDIPLGTPLCIIVQKESDISAFADYSETGVDATPVAAPPPAPAAPSPTPPTAPANSAAPEKGRVFASPLAKKLAAEKGIDIAQVTGTGPDGRVTWKDINSFVPLKPTPAPAAAPTPAAPKPGPPAAPAVASVPTETFSDIPISNIRRVIAQRLTQSKQTIPHYYLSIDVNMDQVLELRKELNSELKADNIKLSVNDFIIKASSLACLKVPEANSYWMDTVIRQNHVVDINVAVSTPMGLITPIVFNAHIKGLATISKDVAILAAKAREGKLLLHEFQGGTFTISNLGMNGIKHFSAVINPPQACILAVGGSENRLLPADNDKGFDVASMMSVTLSCDHRVVDGSVGAQWLAEFRKFLEKPYNMLL | Cofactor: Binds 2 lipoyl cofactors covalently.
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
EC: 2.3.1.12
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA
Subcellular Location: Mitochondrion matrix
Sequence Length: 647
Sequence Mass (Da): 69076
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A0A520XY27 | MPCWQRMAGIPAISSTSVTVCSPRLTRPCWSGSWSGSTRTVAKPRIAIVGGGIAGLAAAHHLVGEDVEVHLFEAADRLGGKIDSTMLGAEQLPAAADNFLARVPQMKDLAHELGLGDELISPTATNAYIYRDGSLHPLPPTLLGIPADLDVLAESSLISNAGVERARADLSAPDDRPEGDESVGDLVRRRLGDEVHEYLVDPLLGGINAGDSDRLSITYGVPQIRAARDRDASLIRAAQNMRSGLIVGAPVFLSLRGGLQVLIDALADELEQDEWATVHIDSPVADLQRGESGWQIEGASFDAVIVAVPPVPASALLSSCAPAAAAAFGAIEMSSVVMTVIALAPESLPVASNVSGVLIPRLEGLHVTAVSIATNKWPDLSDRQILRVSVGRRTDTRWRSLDPDELTAIVISDLQTIFGCAIHPQDAIAVEWIDSLPQYDVDHGQRIDAVESTLAADCPGVHLAGASLRGLGLPACVQSGRDAADAALSSIR | 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: 492
Sequence Mass (Da): 51720
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A0A524NDB1 | MSPVTDPITPPTTDAVPDRPAETNDPIRDAHRILQWAHRRFGSQLCVTASFGDAVLAHVANEAIPGVEITLLDTGYLFAETEWFADELRERFGINLRIVRPDAEIATNVWQTDTDACCAARKVEPLNRALLGRTAWVTGLRRSDSPSRRTAPFVHLDLLRGVTKINPLAGWTDAHVVTYVAAYGIPDHPLADRGFPSIGCWPCTRPVADDGDQRSGRWADSDKTECGLHQ | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate.
Function: Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor.
EC: 1.8.4.10
Subcellular Location: Cytoplasm
Catalytic Activity: [thioredoxin]-disulfide + AMP + 2 H(+) + sulfite = [thioredoxin]-dithiol + adenosine 5'-phosphosulfate
Sequence Length: 230
Sequence Mass (Da): 25375
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A0A9D5RX72 | MPFESYLMIFAISLGVTLVAYPVLIPFLHKLKYGQTVSEYMPSQAKKTGTPTMGGIIFIAIPIIIQCILHPTSIQNPSVILVMLAFIGYGIIGFIDDYIIVVTKNNAGLSPRNKFLAQLFLAVVFYILFQSSISTAISIPLTSISIELGPLYVLFVLLMFASCSNAVNLTDGMDGLAGGTSILALTPFVLFAIHDGEYELACFIIAIIASLVGYLRYNFFPAKIFMGDCGALALGGVLAALGLVLKRELIVILIGLVFVVETASVILQVFWVKKFGHRIFKCSPIHYHFEQSGMKEKNVVFMFYGIGALCAVLGYFIGL | 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: 319
Sequence Mass (Da): 34783
Location Topology: Multi-pass membrane protein
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A0A399RJ29 | MAKQPLGSADRLTGLVAKLAETVDSRAGGNPEKSYTAKLLNSGELRCGKKIAEEAAEVALAIAAEGRKETASEAADLIFHLLVGLRAKGVPLDMVADALAERRGVSGLAEKAARQTKA | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
EC: 3.6.1.31
Subcellular Location: Cytoplasm
Sequence Length: 118
Sequence Mass (Da): 12226
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A0A9D5RXF6 | MMVNPRKVVVIGDGNVGSSVAFTLVIKKQVSELVIIDVNKDKAEGDALDMAHAMSINAPVNIKAAGYSEIADARIIIITAGAAQKPGETRIDLLNKNKMIFDSIFDNMRPYLNQESIVLVVTNPVDVLTMYTYDKLSLPANQVIGSGTVLDTGRLKYLLSRDTGIDPRNIHAYIIGEHGDSELAAYSVTSIGGVTMSEYCKECGRCGGRQEERLELIEEEVVKSAYEIIAKKGSTYYGIAAATSRIVDAILHDTRSILTVSSYISNGLGGQIDGVYLSVPTIVSHLGAEKTIWPNYSEEEKQSLIESANKLKSLIG | Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Function: Catalyzes the conversion of lactate to pyruvate.
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
EC: 1.1.1.27
Subcellular Location: Cytoplasm
Sequence Length: 316
Sequence Mass (Da): 34233
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A0A2A3LMS2 | MTIQNLEELEGLKRAGALVANILATMREQALADVTPRDLDAIAADMLRNAGAVSAPVSTYGFPAQTCISVNRVVAHGIPSGVPLRDGDLVNIDVSAELDGFFADTGASFVVGTASAAQQRLLDATREARDTAIAQLRAGELLSGIGRSIETVAARRGFRVIRNLQSHGVGRALHESPGSIPGYYDRRDTRRLHDGMVITVEPFLATHVTRTDELDDGWSLICRKGYGAQFEHTVVVTHGAPIIVT | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
EC: 3.4.11.18
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Length: 245
Sequence Mass (Da): 26196
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A0A0G1CXA8 | MPTLDDLRKTRIEKLQELKKMGIDPYPSRVIRDQTIAEAKTKEGEDVSVVGRITGRRGHGKICFFDLVDESGQIQIVCKADKVSEKTFALMELVDLGDFLSVQGTLGKTEAGEVSVFAANFQLITKTIRPLPDKWNGLKDIEERYRQRYVDLLMNSEVKNVFLIRTKIIKFLRHYFDSHSFIEVETPILQPIYGGAAAKPFITHHNTLDTDLYLRIAVELYLKRLIIGGFEKVYELGKDFRNEGMDRGHNPEFTMLEFYWAYTDYEKLMQFTQNMLIELVQDVCQTIELDYQGIKLNFQAPWKRITYREAILEHTGVDINQADTEEKLRTMIKSKGIKVDLTGAIGYGAVLDTFYKQTTRPHLVGPLFLTDRPTDFVSLAKRLPEDPRKTASFQLLIAGREIINAYNELNDPIDQANRWKESEKLGEIGHSEHEVFDDDYIRALEYGMPPTAGWGMGIDNLVAILTNQHALKDVILFPTLRPITDEKKEQKQEEVSNKQNNHNGHSTKDIGISYPQAKKLLDEYIKDPITKMHCIESEAIMRVLARHFSEVEEEWGIIGLLHDIDWEETRTNTKLHCIRCADILRKNGGTEFLIKTIQSHGYGQGFGDAYYGPPEFKDKTREGRVQHALAAAETLTGLIVATALIQPDKKLASVKPESLIKKYKSKGFAANCKREIIAECEEINIPIDQFLGMGLKALQDIHEGLGL | Cofactor: Binds 3 Mg(2+) ions per subunit.
Catalytic Activity: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys)
EC: 6.1.1.6
Subcellular Location: Cytoplasm
Sequence Length: 707
Sequence Mass (Da): 80614
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A0A960FUH6 | AGADLFVVHVEATDEAGHAGDHEEKVRALENWDRRILADLVDGLDALGDWRLLLLPDHATPIELKTHTPDPVPYLLVDSRTDGPGGVYTEEGVADADALPGHQLLPRLLGR | Pathway: Carbohydrate degradation.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 111
Sequence Mass (Da): 12029
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A0A950Z753 | MLAPTPAERRAILEETFHFHPLAIEDCLTRLELPKVEVYENYLFLTFHEVDFNRETESFEVHEMDMFIGKNFLVTFHEAPLRSIQAAIDRCVKNPTQITRGPDRVAHSILDALVDNYLPVLNSFADQVNEFERLLVDDLRSESLQRIMKLKREINKVGQIIRPQREIVHRFVRSEFPLIRAKLIPYYRDVYDHLTRYQDLADNYRDSLNSTLEVLLSFSANQTSEVVKVLTLITVISTPATIIASWYGMNFHDMPEVNSPHGYWVAILVTILSTMAFVWWFKKRRWL | Function: Mediates influx of magnesium ions.
Subcellular Location: Membrane
Sequence Length: 287
Sequence Mass (Da): 33716
Location Topology: Multi-pass membrane protein
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Q65RZ0 | MSVVKRKTTQKKIKLAEPKTRVFLQVKPLLVLCCVGLLYFAYINWQTLLDKLDSKPISSFALVGTPQYTTNADVRDMILKMGELKGFFGQDVDVIREQIESMPWIKGAVVRKIWPDRLSIWVAEYAPVAFWNSEDFVSLDGVVFKLPKDRLKNDNLPRLYGPDYQSLAVLDAWKQIFNELKSKGITLKAVSIDERGSWEIVVENDITLKLGRGEWKSKIDRFMTIYPQVEIPENKKIAYIDLRYKVGAAVSFADIN | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Subcellular Location: Cell inner membrane
Sequence Length: 256
Sequence Mass (Da): 29382
Location Topology: Single-pass type II membrane protein
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A0A1Q9NVD3 | MTRNEEEDLANRILYHKRKYYDGEPEISDAEYDKLEEKLTNLNSSHPVLHIVGTPIGGKFNHDPPMLSSDKATTLEEVVKWANKVGDHSLSAGYKVDGLSLSLIYENGKLLQAATRGNGTSGDDVTLAVMLIDDIPKTIPIEDRINIRGEVFMKISEFTKVNSKLPKEQRFSSPRNLAVGTLRQKNVSGIENRRLSFKAFEVLGISENKTIQEQNELLEKWQFSRADFEFIEHNNSEEIDRIFLKIENERKSIDFEIDGVIFKYNEYLDRNEAGSTEHHPKWQIAWKFKSEGSETIINDIIWQVGRSGALTPVALVDQVELKGALISRATLHNADFIENLNIAPGDRISIIRAGDVIPKIMAVVDKGNNDFEFPINCPSCGNSILRDGVNLICTSLICREKDIQSIMHWMRMTDVEHLGQKTIEKLYVLGFVQHYSDLYKDDLSEEILNRHFGKNGSKMKTSIEKSRNLSFKQFLAGLGIPTLGKKLGKELAKHFPSLKALQSTTTTELATLDGISDVTANHILGGINDKSRAARLLLNNVTIFYGTEKRIQQTKIEKSTTPSLGDFWDDEALQPHAEYNIKPDKPQKIGNDEKIYITGSIEGYNKKKLQEFIESMGFEWSTSISKNLDFLVFGINAGGAKLDKAKTIGITILSWEEFVKKFGI | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
EC: 6.5.1.2
Catalytic Activity: NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.
Sequence Length: 664
Sequence Mass (Da): 74890
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A0A961AT07 | MYGSFQSLLTETLDSIRDAGLYKGERIITTPQSPHIAVSSGAEVLNLCANNYLGLADHPEVEAAAREAIERWGYGLSSVRFICGTQQIHKDLEKALSEFLGTEDTILYSSCFDANGGLFETLLGPEDAIISDELNHASIIDGIRLCKAQRFRYRNNDMADLEEKLKAAAESSRFRLIATDGVFSMDGSIADLKSICDLAEKYDALVMIDDSHAVGVLGERGRGTHEHHGVMDRIDIITGTLGKALGGASGGYTSGRKEIVELLRQRSRPYLFSNSVAPAIVAASLKSLELLTRSSELLDRLRENTAFFRGEIAKTGLTVLPGEHPIVPVMLGDAKLASGMAERLLERGIYVIGFSFPVVPEGKARIRTQVSAAHTREDLEFAARAFGEVASEIG | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Pathway: Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 2/2.
Function: Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.
EC: 2.3.1.29
Catalytic Activity: acetyl-CoA + glycine = (2S)-2-amino-3-oxobutanoate + CoA
Sequence Length: 394
Sequence Mass (Da): 42780
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A0A963HDK6 | MSENKKAAGGEHDTAPVSDHKRPYRGRFAPSPSGPLHFGSLVAAVGSYLDARANDGEWLLRIEDVDQPRTVPGAADAILRTLAAFGFEWDGEVLVQSRRLDFYHAALVRLQLDGEVYPCACSRSEIAAHAPPRSVDGGLVYPGTCRAGLAGGRAARAWRLRLPDRTVAFDDRVQGRHQQNLAQAVGDIVLLRADWQYAYQLAVVADDAAQGITAVVRGVDLLDSTPRQIWLQQRLGLPTPSYAHLPVVTNAAGEKLSKQTRAAAVDASASNALLSAALDFLGQTVPAKVRAGSLSDLWRWAIAAWSVERVPALRGVFPGQRLPP | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon.
EC: 6.1.1.-
Sequence Length: 324
Sequence Mass (Da): 34905
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A0A960N838 | MRYPPVFLMPALLACALLMLFGQVPVLAGKKKTQPPLPERDRNTVLVRKPIIVDNAVFDMKGKTYSGRDRDSQREDGEPLFILKNNAILKNGRIIRSAEGVWFRGINSRVENVEFPNVYEDAVSTRSAKCRKAVGKKRNRIIRCTFSRFKDKAVQLNAGELEVRGCTFTNGVTSIRQNGRSSEPLVLHVYDCTFRNTHSMAKADGKNPRSRVYRAGNEGQNVNDPDWEISGKTKLIDRRKY | Function: Catalyzes the depolymerization of both polygalacturonate and pectins of methyl esterification degree from 22 to 89%, with an endo mode of action. In contrast to the majority of pectate lyases, displays high activity on highly methylated pectins.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
EC: 4.2.2.2
Subcellular Location: Secreted
Sequence Length: 241
Sequence Mass (Da): 27345
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R5CEE7 | MNNTLRFVMALVVTILLMLTFRALVFTVYTVSGTTLEPCFADGDRVLVNRWSYGLRTGGGGMFRYARWIGSPIERGDLAVFNNPADTARRISAKKALAYYCTGVPGDTIRIGGARVVVPGKDTPCRVTPANARLLCFLYNRFEGRKASVSGGRLYVDGKETKCATLANDYYWFSSGRAGDRSDSRSFGLVPETHVIGKVAMLLYSTDKSKPFTHRLRKDRFLLIIRK | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 227
Sequence Mass (Da): 25270
Location Topology: Single-pass type II membrane protein
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A0A960NDV3 | MLNWIPTKLFSSKAARDSRSLRRFVADVTEREKRFANFTTEDCQHQTSVWQSEVQALDPDRLDVIDRHLKLIAPDAFALVRQASRLLAERDPEWKLIPFDVQIAGGNVLFQGNISEMATGEGKTLTAVAPAYLRALAGRGVHMITVNDYLAARDAEWMGKLFATLGLTTGCLQNDQSPDQRRAMYAFDITYGTSSEFGFDYLRDNGLARSAGTQVQRGHYFAIVDEVDSVLIDEARTPMIITTIGNTRSSFLPIYVSSVARLVKEQASHCNKMIQEARDLYGDGSHRDTDAAVGMLLYKCRLAQPLHPGLRRMKQDPALLRLLENATLYFHVDSRRSELFVMKDELLFWIDERSHDAELTDKGCRFMSPDCPELFQVGDLMSALARIDNLDETKEIKQQRRERLEADADEHGRRIHEVRQLLKAFCLYERDRNYLIKDGEVVILDEAQGREMPGRRWSDGLHQAVEAKEGVTIQPESETMASITVQNYFRLYDHLAGMTGTAMSDAGELKDIYGLDVILVPTHRPCQRVDLQDQVFKTRKEKYQAAVREIKAAHSRNQPVLVGTASVEASETFSRLLKRESIPHQVLNARHHDQEAAIIARAGEPGAVTISTNMAGRGTDIQLSDGVADLGGLFVIGTERHESQRVDRQLRGRCARQGDPGTSVFFLSLEDHLMRRIDNGGKMAVILDKVGHVEGEPLASPMLTRTISSAQKRVEKTDYEQRRRTLRYDEVVNGQRSWIYDWRNELLHAAHPQDWLFEALPDCLSSAVHIEPLDDGSGSHTLTFAPEVDYFALPLLDELEALAQERDLLPVHARLEDAIVTRVREAVTAIDHDLVSPGEFLRQAALTKIDRAWQMHLVELEALRERIGFQALAQKDPLVEFTREASFVFRDRLDSIRLGIIAAAREGLEAASRAEARILSERLRPAESEIRLNFDVRPRDLQSSGRNASCPCGSGRKFKKCCGVRA | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
EC: 7.4.2.8
Subcellular Location: Cell membrane
Sequence Length: 966
Sequence Mass (Da): 108932
Location Topology: Peripheral membrane protein
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Q4JVE2 | MSNPETLSAKETEAVEAVESTELSAAEANPVDAPDSEAQGFFEKLYNGNGGFRIVQNRGRLYGILVAVVVACLLSILVRGFTLGIDFEGGTRMTMPPAGGATESSVSEIFENATGIAPQSTQTVGSGDAESIEITSERLSEEQIREARSALFNEYHPKNNVGEVTQDAISDSTVSESWGSSITKKMLIALGVFLLTVFLYIAFRMERDMAAAAIICLLIDLTVVSGIYALVGFEVSPATVIGLLTILAYSLYDTVVVFDKVHENTAGLFGSTRATYAEETNLAINQTIMRSINTSIFSLVPIASLLVVAVGIMGVGTLKDLALVQFIGVIAGTFSSIFFAAPLLVTFKMRQQKYKQHEARVERARSLAASQEGTSSNDAAVETSDGDSEKVTVPADNGDEEENTGRAKRNVSSPNAHVAADSTEDFKRETHNEDAGRSWRPGM | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Location: Cell membrane
Sequence Length: 443
Sequence Mass (Da): 47439
Location Topology: Multi-pass membrane protein
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A0A0D6JFF0 | MTATPKAAQASINVTHTSVLAIALPIIASNVSTPLIGLVDTAVVGQLPAPHYIGAVALSSTIFTFLYWAFGFLRMGTTGLTAQADGAGDSVEVGAALGRALLIAAVAGSALILLQAPLSWFAFLMVEGSKAVEGEAHNYFAIRIWSAPAALANYALLGWFIGLGRARIALLLQVLLNGLNAILDAWFVLGLGWNVAGVALGTVIAEIAAAVVGLVIATRVLARIGGFPDFTAVLAPEHLRRAIAVNTDIMIRTLCLLTAFTWFVFQSAASGDVVLAANAVLMQFVSFMAYFLDGFAFAAESLVGRAIGARNRSQFDAAVRLSSLWAGLISLALGTALMLLGGTLIDLLTISPDVRAAARVYLHWAALVPVVGVVCFQLDGIFIGATRSVDMRNMALISLVVFMAAWAILHPAFGNDGLWLALIILNVTRAITLAARYRSLVDDAFPVERAARQAIPS | Function: Multidrug efflux pump.
Subcellular Location: Membrane
Sequence Length: 457
Sequence Mass (Da): 48027
Location Topology: Multi-pass membrane protein
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A0A960IZI0 | MATRRARPDPDHREDPTVTDTVYTLPDLPYDPGALEPHISARIMALHHDKHHAAYVKGANTALDKLSDIREKGDFSTIAMLEKTLAFHVSGHVLHSLFWTNLSPDGGGVPEGPLADVLDETFGGLPAFRQQMTEAAATIQGAGWALASWEPVAGRLVVQQVHDHQGNHGQGTIPLLAIDAWEHAYYLQYENRKTEFFDAVWNVVNWVDVARRLADARGTATT | Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 222
Sequence Mass (Da): 24489
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A0A2E6X8N3 | MNLKSLDLPEVKLLTPKRYFDDRGWFSETYNSKTFSKLGLRYTFVQDNQSLTNNIGTIRGLHFQNPPYAQVKLLRVLQGRIFDAVVDIRVGSPRFGKFVAIELSAEDGSAILVPEGFAHGFMSLEEKTEVLYKVSKFHVPSAEFGINPMDPDLKIPWPVEDIGHHGNVYSSERDSTFPMLKEAHSAFIYPERIKEK | 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: 196
Sequence Mass (Da): 22353
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A0A832JKV4 | MGSELFRSFEGNYHLMGVGGAGVSALALLLKGWGFEVSGCDVDVEDGYADAVRRRGVRVYRGHSPEHLVLERCDRVVFSKAVDRSNEELVAAIRMGLSVESRSSFLGRVFNAMRSIGVSGTHGKTTTTSMVAFALKGLGFDLTALVGGEVPSWGANVLLGDSDLLVCEVDESDRQMAEYSPYISVLTNLELDHADVYRDVGQIYEVFLSYVMNSKRGGALVYWGDDPLLSRLAGEVSRARSDLALLDYALGSRARLGAVGIRQEGRSALFTLLADGSPVGEVRLGVPGEHNVLNALAAMAVVAAMGLPLSSALGSLEGFRGAKRRLTVVGEAGGVVFVDDYAHHPTEIRRTLATARSVWPGRRLVVLFQPHRFSRFARFAAEFAEVLAEGADLLFVLPVFSASEARPEDFGSKTELFLDVLYGRKGAGDIILLDGVDCDTGGVTGLLMPGDLVVSLGAGDVNVLLRRVFEDWCRLKEV | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
EC: 6.3.2.8
Subcellular Location: Cytoplasm
Sequence Length: 478
Sequence Mass (Da): 51440
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A0A1Y1SFL1 | MPQNIAKVSYLSVGEDETGQRLDNWLLARLKGVPKSRIYRIIRSGEVRVNKGRAKPSSRLAAGDSVRVPPVRRDTEDHAGPVPDGMTQTLSDAVLYRDDDVLVVNKPAGMAVHAGSGVRFGLIDAARALWGERWQLVHRLDRETSGCLLLVARRELQHEFQRAHDAGSIRKQYQSLVHGRWSEQQCQLESRLGKYRDGSGERRVASGDDAPNKRALTYIDKVQWLRATSLLEIRIETGRMHQIRVQTADAGHPVVGDAKYGRRALDAALELPMRPGLCLHACALQLELGGRSLDVSAPLPESFEAVITAQS | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 311
Sequence Mass (Da): 34458
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B8CYQ7 | MADKGGGVKSFIGIVIMMVLIAAGTSYGFMTYFDRTNSQHVLESKDIGPTYSLGDFIVNLSGTGGYQYIKASIVVEVSQDSVIRELDKRSPQIRDIIISILRDQKMADIEEPGARTIKNRVRAELNQVLTTGKITSVWFTQLVVQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 145
Sequence Mass (Da): 16033
Location Topology: Single-pass membrane protein
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A0A284VKW4 | MESTNKEYGAEQIQVLEGLEPVRKRPGMYIGSTDARGLHHLVYEVVDNSIDEALAGYCTGIEVYLRSDSSVRVVDNGRGIPVEILPKYNKSALEVVMTKLHAGGKFDNNAYKVSGGLHGVGVSVVNALSEWLEVEVKRDGKLYKQRYEQGGPTRDVVLIGDAQGTGTTVTFKPDKTIFETLQFDIDVIAGRLRELAFLNKGLKIAIKDEFSQKEQVFQYEGGIISFVEFLNKNKNVLHEKPIYFQKQKDTTIVEISMQYNDSYIENIYAFANNINTHEGGTHLIGFKAALTRVTNDYAKSKAMLKGDDKLSGEDVREGLTAIINIKLTNPQFEGQTKTKLGNSDIKGIVETLVSEGLSEFLEENPTAAKNILSKALEAAEAREAARKARELTRRKNALEVSSLPGKLADCSEKDPKLSEIYIVEGDSAGGCFSGDTRVALADGRALSFKEIVAEYEMGKENFCYTIRSDGTIGLERIINPRMTRAKAEVIRVTLDTGEHIICTPDHNFMLQDGCFKQAVDLTQDDSLMPLYRKFSDMSEPGITIKGYEMVWDPRSESWLFTHLLADWYNRWHGIYAQDNGEHCHHEALACEAIANFNHRIIAIERLEECMDVYDFEVPHTHNFALANGVFVHNSAKQGRDRKFQAILPLRGKILNVEKARLTKILKNEEIRALITAIGAGIGEGEEFDINKARYHKIIIMTDADVDGSHIRTLLLTLFYRYMRQLIDTGYVYIAQPPLFKVKKGKVEFYVYNEEELTRKLAEMGRDGIALQRYKGLGEMNPQQLWETTMSPETRTMLKVTLEDAIKADEIFTILMGDKVEPRREFIERHAKDVKNLDV | Cofactor: Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).
Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
EC: 5.6.2.2
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Subcellular Location: Cytoplasm
Sequence Length: 838
Sequence Mass (Da): 94466
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A0A0L7R5I7 | MPKCNTKARYLPATLAWTVLLSTTALFFCFPCQYYVFRWGTWVPVLQGVIIFFVLANFTLATFMDPGFIPKALPDEDQEKSYPAPIYTSVQINGITVRMKWCGTCKFYRPPRCSHCSICNHCIETFDHHCPWVNNCIGRRNYRFFFFFLLSLSFHMLSVFGLCLYFVLERKQQLGEVDTIVALVLMGVVAILIIPIFGLTCFHIVLISRGRTTNEQVTAKFPDGVNPFSHGCLHNCCYTQFAPQYPSLIKPEKYSGKRRGMSTSEISTIGSENQVKTYMDSSNGVRNASSNAYNKLSPGRDGSDTDMEPTASQSADCEPTPPLQRHGSKNNFFLPPVENSESPRHPPPSQHCHPMHYTRGSPHPRPRGMNGSRSHTPDPLSPEASGSPATASQRGQGQGGASPTTQRIKAIGVPTPLAISSPIRRYTMLIYRI | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 433
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 48409
Location Topology: Multi-pass membrane protein
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A0A6A4URQ4 | MELSLMDLHQIKEIAIRAGALLMEIYDSSYEVKTKEDQSPVTKADLTSNAFIIKELKKLYPNILILSEETKDDLNRLRHELLFIIDPLDGTKEFIKHNGNFTVNIAFVHRQRSILGVVHAPALKKTYYALKGLGAYEDNEDALNRCISVTDKLTDLNLVGSASHRSLEDEKLVEENALQIKTYKQLGSALKGCMVASGEADVYYRFGKTGEWDTAAMQIIVEEAGGIFREINGKPMIYNRFNPFNEKGFFAVNRKENIWTVPSVKI | 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: 266
Sequence Mass (Da): 30107
Location Topology: Peripheral membrane protein
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A0A1Y1SAP0 | MTDSRQVVLKALSLLNTGRNLPDALSQAGISKLSPRDRAFARRLAVHAVRHRRRLEQQIQAYLQRPTKDRGVLDLLWLGAAQIDLADVATHAAVNSTVEVAPKRLRGLVNAILRRRLREAPAAPQGLAEQHSFPGWMVARITRDWGDRAGEILDQLNQDPALCLRINRQKSSRAQWLTALSDDSAQSLGSDVVQSDGVVLAQSRELAELPGYADGGLSVQGPSAQAAAHLMQLQSGQRVLDACAAPGGKTAHMLELCPDIVCTALDIEPARVARIEDNLKRLGLQARCMSGDMLEPGDWAGEYDRVLLDVPCSGTGVIARHPDIKWLRREQDVAQLAARQLKMLQRAWSWLAPGGVLLYCTCSILSEENDAVVAGFLNEQPEARLQALSLPFGQASEYGWRVAPQAPYEGFYFARLIKDP | Function: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Catalytic Activity: cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.176
Subcellular Location: Cytoplasm
Sequence Length: 420
Sequence Mass (Da): 46058
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A0A7W2H3C4 | MPPWGFWPLAFIAFAMLDQILKETHGATSRFFTGFGFAVGWLFPGTFWMIALTVPGYFIQGFLFSGLFALSTSLIPTSIHRLVALPAAFTLIEAVRYRWPFGGVPLATIAMSQSDSPFGQTARVLGPLFLTAFVIICGMAFAMIWERKWRHTGLIVSVLLIIWGFSTIAPKGSVTSTIDVAIVQGGGEQGTRAINTNEREVFERHVEATGLIQGNPDIVLWPEDVVNVRQLLIDSPEFSELQQLSRNLNSWLIAGIFERTSITSNANASIVFGPDGRVYDRYDKVRLVPFGEYVPLRSLIEPFAPEYLPVRDTQPGSGKPNLQVALNGNDLNAGISISWEIFFEDRAREAIRNGGQILLNPTNGSSYWLRILQSQQVASSQLRAIENGRWVLQAAPTGFSAIINSDGKIIERTSISETRILQGNVELRDGKTLATRAGPLPLIILAGLTVISSNFLARRRP | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
EC: 2.3.1.269
Subcellular Location: Cell membrane
Sequence Length: 461
Sequence Mass (Da): 50839
Location Topology: Multi-pass membrane protein
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A0A9E3YCU8 | MQSTGALGAVLMLVAPTDNVLEHVAGAGPMNDAPSIADLDINSSNDWFTQTFRSGQALFVDDTAGWEPKSAVTERALERGVTACWTTPLVTVEGDIIGTFSVGWPDAVEPGDDQLWLFQEFALLAQAVVDRQQSHWQRMALIAHERERIAGELHDDSVQAMTAVSLRLQRLQARLAEHELRQSVVELRHQVDEAIERLRHMLFSLSSPTLEQDGLVITLEIYLETYVEKAGLAWELHGDEALRLPHDVEALAFRLARGALINAIKHARATKVSVSVDRSDDGGLAVVIADDGIGFETGEITAKDKPGHVGLTYAQSLARAVGGAYAIDSMPGKGTTVSFSIPGF | 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 transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cytoplasm
Sequence Length: 344
Sequence Mass (Da): 37313
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A0A9E6F4L1 | MENRFKVINVTPRGFCKGVYNAIELAKQTRMDYPNEKITILGELVHNKDVVLALKSLNIHTIESKGKQRIDLLDDVLEGIVIFSAHGISPLVQIKAKNKGLKTINASCEDVLKTQDLINAYLEKDYDIFYIGQLGHPEAEASLDLDLNKVHLIQIGNELPKIDSKKIFVTNQTTMSILDIKNTIESIQTIYPYAIVSDEICSATRLRQEAILKLPESVDAIIIIGDKSSNNTKMLAKISRNRSIPTIIKIQNLGELDPKLLDQCHELAITAGASTPKFIIDEIVHFVNAYAIDPQIDKKDYSIHPFI | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
EC: 1.17.7.4
Catalytic Activity: H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Length: 307
Sequence Mass (Da): 34387
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A0A960NBT9 | MSIVINILMVLLVALCLLMLLIILMQRPKQEGLGAAFGGGMMDGMLGSGTTNFLQKATVYLTVGYFVLTMALDVIQARTSEARSLQGVNLEVSAAAASPADDSEPATTPDPATTPAPDTDNVPAGGEIEPPAPAPSSIDTEENPGDDDNVDAAPEDEPTAETSDDDAATEEEAEGDAAPAAEDDTPAANTDTEAPN | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 196
Sequence Mass (Da): 20074
Location Topology: Multi-pass membrane protein
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A0A2E3P2G5 | MAPRSVHPLPPGSTIGIMGGGQLGRMTALAAARLGYKSHIFSPEDDSPGIQVSAAATIADYQDRTALQSFAEAVDVVTFEFENVPADSAAFLADHALVRPGPQCLAIAQDRLLEKEFINKTAPTTPYRRVTSAEDLAKAADEIGRPAVLKTSRMGYYGKGQVLIAPDCDYAAAWAEMGAEIGILEAFVDLDCEISVITARSPHGGWATYPAVENRHVNHILDTTMAPARLPDGLADQAVAIAHDLAEALDLVGLLAVEMFVTRDQRILVNEMAPRPHNSGHWTMDACATSQFEQLVRAVCGLPLGSVDCHHDAVMKNLIGDAVNGWPDLLADPGARLHLYGKAEARPGRKMGHVNRLYPKGKLPNG | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
Function: Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
EC: 6.3.4.18
Catalytic Activity: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP + hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + 2 H(+) + phosphate
Sequence Length: 366
Sequence Mass (Da): 39210
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A0A2M7JD99 | MSNLITFDSSTIPEIQTDTLIIGMGIAGLSAGIQAAKYGKVLIVAKTSFHESNTEHAQGGVAVVLADEDTMESHVADTLITGCGLCNNKNVKILVEEGPQRIRELIDWGVKFDKNQGKLSFGQEGGHSLKRVIHANGDATGKEILRGLLAKAKANPNITLMRDVFVIDLLVKERVCVGAIIHAPLEALRVILAKNTILATGGTGQIYRETTNSKIATGDGIALAFRAGAVLSDMEFIQFHPTTLYVAGASRFLISEAVRGEGGILRNKNGGRFSFKYHPSGELAPRDIVSRGIWAELKETNSVFVWLDVTHLDFEYLKKRFPNIVGTCLEFGLDIKTKWIPVRPTAHYMVGGVKTDEYGQTNIGGLYACGEVACTGVHGANRLASNSLLEGLVFGYRAGEHAGHTERLSKKQRFSNDVNDNIHQKINIADVKNSLASLMLRNMGIERDEKGLLEAKKSIDFWMSYVLNKEFSSPAGWELQNMLIVAGLMQRAALTRQESRGVHFRKDYPYQDDERWKKHVDLSEENCDFGS | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1.
Function: Catalyzes the oxidation of L-aspartate to iminoaspartate.
Catalytic Activity: L-aspartate + O2 = H2O2 + iminosuccinate
EC: 1.4.3.16
Subcellular Location: Cytoplasm
Sequence Length: 531
Sequence Mass (Da): 58407
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A0A663F862 | MANDSPAKSLVDIDLSSLRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKKSPPGHDDQLWLVMEFCGAGSITDLVKNTKGNTLKEDWIAYISREILRGLAHLHAHHVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDLWSCGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKKWSKKFFSFIEGCLVKNYMQRPSTEQLLKHPFIRDQPNERQVRIQLKDHIDRTRKKRGEKDETEYEYSGSEEEEEEALTSSCCSSIVNVPGESTLRRDFLRLQQENKERSEALRRQQLLQEQQLREQEEYKRQLLAERQKRIEQQKEQRRRLEEVETGGAFLTGWIGRRPPYSQCHVLNYSRVLSKEYRWREMEEHRQAERLQRQLQQEQAYLLSLQHDHRRQQQQQQQQQQQQQQQERNKQSYHTPEPKSHYEPAERAREVSPACGQESATCSSAPACWHHRDCSSAIGQLEHLRDITCTLLFSFSVGFSSEAMRSEAIRQDPTRKGSVVNVNPTNTRPQSDTPEIRKYKKRFNSEILCAALWGVNLLVGTESGLMLLDRSGQGKVYPLINRRRFQQMDVLEGLNVLVTISGKKNKLRVYYLSWLRNKILHNDPEVEKKQGWTTVGDLEGCVHYKVVKYERIKFLVIALKSSVEVYAWAPKPYHKFMAFKSFGELVHKPLLVDLTVEEGQRLKVIYGSCAGFHAVDVDSGSVYDIYLPTHIQSSIQPHAIIILPNTDGMELLVCYEDEGVYVNTYGRITKDVVLQWGEMPTSVAYIRSNQIMGWGEKAIEIRSVETGHLDGVFMHKRAQRLKFLCERNDKHCDCAVNIGDSEGKLEPLLSYLFSLPPYGRVEAVKSIS | Function: May play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway.
EC: 2.7.11.1
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Length: 935
Sequence Mass (Da): 107708
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A0A395JTC5 | MEEQFWHQRWQDRNIGFHEGKPNTLLVRQLERLNLTTGDRIFLPLCGKTQDIAYLLSLGFHVVGIEFSAIAVDELFLELDIKPTITQHADLSLYQVAKLDIYVGDFFALQKNMLGHVDAVYDRAALVALPLDMRKQYTAQLVQISSAAPQLLIVFAYDQTAMNGPPFSLVEDEIMQHYAEHYTLELLEHCDASALFNKRVQVSENAWLLQALGQ | Catalytic Activity: S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether.
EC: 2.1.1.67
Subcellular Location: Cytoplasm
Sequence Length: 214
Sequence Mass (Da): 24406
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A0A9D5RXY3 | MKKLVVSENEIQEVCKYLGRKISKDLAHESKPPLLLVVLKGAVNFAIDLSKNITIPVFMDYIQISSYSGRKSTGDIKLIHNLRFDIKDRVVLVVEDVIDTGVSMDYLIHHLYANYQPKKVLVCAMFDKINARKTTVRVDYAGKILTENDFLVGYGLDYNEFERNIPYVYIPTEEEIAHFDELSKK | Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.
Catalytic Activity: diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
EC: 2.4.2.8
Subcellular Location: Cytoplasm
Sequence Length: 185
Sequence Mass (Da): 21263
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A0A924M1J9 | MTLEQLNALEHAEFVQTLSGIFENSSWVAQAVFKERPFPHVSGVFLAMDYVVESSSEIQKLALIREHPDLGSRLKMSSESVLEQSSLGLHNLPPELFERFSQANQKYQAKFGFPFIICVRNQSGVQEVLEAFETRLKNGLEREKGAALYEISQIALHRLTDLLES | Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 3/3.
EC: 4.1.1.97
Catalytic Activity: 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+) = (S)-allantoin + CO2
Sequence Length: 165
Sequence Mass (Da): 18683
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A0A1Q7BDN7 | MLAAAKANNVSEFSITEHVSQFREPRESIGFGSIHPSGRIFESLKEYNAEFRKADRLAYSGMKIERGLEVDFSPRFETRLGDFVNQEAWDILLCSVHEFEDGKDIEKSVRGIVDPASAHERWREYLRLERMALESDFVPFKVLSHPVRITRASKAAPPELDDLLLDLARVARRRNKALELNGRDIDYAPELVRRLATACSRAGCRVSLGSDAHHASEVFRNMNTAMALVKEFNLESAE | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 238
Sequence Mass (Da): 27009
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A0A1I4JIX1 | MQRYFVKPEQMTENDVVITGEDVKHISKVVRLEPGSHIECLNNQGRRTHCRIRSVDKESVAADILEDIESSPELPVYAAVAQALIKGDNLDLVVQKGTELGARSFLLFAAGRSVVKWDSSKVEKKLQRLRKIAKEAAEQSGRQYIPDISYYASTRDMMEEASTYEASLYLDEETAKSGEHHAAADIFSSRPASILALIGPEGGISRDEAQALDQSGCRPVSLGPRILRSESASLYFLSALSYHYEILR | 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: 248
Sequence Mass (Da): 27533
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A0A931ECY5 | MARGKLRLYLGAAPGVGKTYAMLNEGWRRKERGTDVVVGWVQEHGRPQTDAQVRDLEVFPRRVAEYRGQTLEEMDVDGLLTRKPELVLVDELAHSNAPGSKHAKRWQDVEELLDAGINVISTVNLQHLESLNDVVEQITGVTQQETVPDPVVRAADQIELVDMAPEALRRRLAHGNVYPPERIDAALGNYFRTGNLTALRELALLWVADRVDEELNDYRERHNISGPWQTKERVVVSLTGSRGSAILIRRAARMAMRTKAELVGVHVRTDDSLTGRGSQGLVDNRALLDALGGRYVEVVGSDVAPSLVQVARAENATQLVMGATHRSRFNEFARGSIINSVIRAAGGALDVHVIATEAELQPESEQDPQPASDGSAGHTRDKVGRPAASRYRRRLLSPLSSRRRWAALVIGAVGFPLLTLVLTAARSHVDLSTALSSYLVLVVVVAATGGVWVAALAAIAGFLLSNFYFAPPIHTFTIADARDILALVMFLVTAGVVSVLVDLSARQTAGALQARTDARMLARVAGRMVAPEGNPLPALLEELMVAFRLDAAAVLRSDTRLPPVGGPPGTAEAAAATWSAVASAGQDPPQRPVEATVVLPLTDRELLALKGPDLTAEDREILAAFAAQLATVLESAKLHAEAAEADSLARANQLRSALLAAVSHDLRTPLASIKAASSSLLSDQLAFGPDETRILLQTIDDESDRLNSLVENLLDMNRLQTGSMDVLDQSTDVQELITAAVESLGPRGDDVVVDVEAPLPRIHTDPVLLERAVANLIENALTHAGGKGLRIEAGAVAGRVDIRVMDRGPGIRRQDRDAVFQPFQRLGDSDNLVGVGLGLAVARGFVEAVGGDLDIEDTPGGGCTMVVRIPERPAGAGEHPGNAGNGRSEPIENQDATGTPEPRASSAS | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 908
Sequence Mass (Da): 97008
Location Topology: Multi-pass membrane protein
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A0A963MJ68 | MPSNHLPPDDPASTGSSDASAAPRPSSFASNRAARLVADIGGTRARFALLDEQGAPQQVQILAVADFAGPVEAIEAYLDEVGCNGLQAAAIALAAPVDEQEIRLTNAAWTFARSEMKSRLGLARLLLLNDFTALALALPHLAASELRQVGGGKGVALAARAVLGPGTGLGVSGVVFDRGRWLALAGEGGHCSLAPADGRESAILALAWRELQHVSAERLLSGSGLPLLHRLVAEVDGRACVALTPAEIVAQALANDDVQCRAVIDTFCAMLGSMAGNLALTLGARGGVYIGGGIIPRLGELFDRSPFRARFETKGRFAAYLAAIPTYVMLAPTPALLGAAHALAESEDGP | Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
EC: 2.7.1.2
Subcellular Location: Cytoplasm
Sequence Length: 350
Sequence Mass (Da): 36063
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A0A059ECJ2 | MIDFTAMILTVGPELWLVAIALIGVLVGATLKDRFNSVSIKFGALALFAAAAFSLMNYEGGEAFNGLVRTNTFVNFAKFVSYVLAGFALLTSEGFLKRHGTIRYEYSLLILLASFGMGMILSAADLMTLYMGVETLSLSSYVLAAFHRDSAKASEAGLKYFVLGALASGMLLYGASLVYGFSGSTEYAVIAAADPSIGMMFGMVLMIVGLAFKVSAAPMHIWTPDVYEGAPTPVVAFFASAPKMASMVVFANVMFTMFGDVIDQWQLIICIIAGLSMIVGSLGALTQTNIKRLLGYSSIANMGYALVAVAAGPELGAGPLLVFLTLYVIASLGLFMGVLAMRRKGGMVEGINELGGLMRKRPVLAIALSILIFSMAGLPPFGGFFGKWEVLSAGVEAGLMPVVIILVLASVVSLGYYLRLIKIMWFDEPTERFEAVDGPVTITVLLAALIAGILFLFFISALSGWAGTAALGLAG | 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 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: 475
Sequence Mass (Da): 50216
Location Topology: Multi-pass membrane protein
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A0A059E3Z4 | MSTDSPDQSAQEPTLVESRNRTSRRPGKWRISNIIDGRALRVKLTAAALDNIGDAQAMRKAALDHLHGAMFRGRMIAQERLQQGAEGLDTARLLSAVQDEVIHALYDFTTTHVHRARNPTEAERLAIVATGGYGRGVMAPSSDTDLLFLRAYKASPHTESVIEYMLYALWDMGLKVGNAFRTPAECVKSAAEDVTIKTSLLDARFMCGDQALFDEMQAKFKKDAVEGKDAEFIADKLAERDARHARQGDARYVVEPNIKEGKGGLRDLQTLYWIVKHIYGGRTLEDVMKGGPFTRSEYGSFIRSAKFLWTVRCHLHFVTGRAEERLSFDLQPEIAARMGYRDRTGQLGVERFMKRYFLVAKDVGALTRIIAAKLEAEQKKRPEGFRRLLPQKTPQALDDPGFVIDSGRVGITSEDVMKRDPLNMLRLFIIARRENKDIHPDALSAITRNLRGLNEQVRSTEEARTLILDAVIGSKDPALILRRMNEAGVLGKAIPEFGGIVAQTQFNMYHHYTVDEHTIRAVEAIAEMEQVNAERVPLATEIFPLIENRRALYLAMLLHDTGKGRGDQQIEGMKTSTRACQRLGIPADETELVAWLVGNHLELSETAQKRDISDPRTVTQFANLVGSLERLRLLYILTAADIRAVGPGVWNAWKGQLMADLYHNTAAALRGGRADEAGVQAHLEARAESRREALVEDLGSIPPVLLEMETAYWTGFDVPELTWHATALKGSGNVVCYRFPPEGGALTLLVSGQDRAGLFADLAGTLANLGANVVSAQVFTNRSGRIVDIFMVQDAAQKPFGQKDETRLRRLETALAETLDGGSVKDLATSRTGRRQAAFLVQPSAQIRNDVSTEYTVVDIAGRDRPGLLYDVASVLADSGLSIHSAHVGSYGERMFDAFYVQTSDGKKLTGSAQIETLKDRLLDALGQHEPDAPETPARKLRRSRAVDSF | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism.
Catalytic Activity: [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
Sequence Length: 950
Domain: Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
Sequence Mass (Da): 105167
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A0A0G0ARU8 | MGNIKLENSNPKNLLKTNNIKLENAGSIHKFTVKPEEENLRIDTFITNQFKSYSRSFFEKLIELELVKINNKIINKKSWPIKENDIIELQFPEEKNRDQELNKLKDLEINIVYQNQHFAILNKPANLAAHPSNNNTETITLVDWIIANIEQISNVGFDSRPGIVHRLDKDTTGLMIIPKNNCSHAYFADLFKKRKIEKSYLAIVHGHPEKTGEIDIEIARHPREKTKMTHVTSSNIAKIKGKSRNAKTMYEVLEYYDGYALVLAKPLTGRTHQIRVHFCSIGHPLLGDAVYGKSSKIMARHALHAFQLEFEFEDKKMKFEQEPPKDFINAISFLKQKKS | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 339
Sequence Mass (Da): 39135
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A0A0G0B4Z6 | MASNCFKKPVVLVVLDGFGHSNEHSYNAVYAANKPNIDKWLRQYPNTLLHASGQYVGLLPGCIGNSEVGHFTIGCGRVIKQPLVVISEAINDGCFFENKVLLEGLEKVKNATGSLHIIGLLSDGCVHSDIEHLYAFLLEAKEQGIKNVYIHAFLDGRDVGPKTAGKYLTDLNNFMKKNNIGVLASIHGRFYAMDRDKNWDRTEKTYKVLVGDAENSFNSVFNDKNIDLNWESILNSSYAKNVTDEFIFPVNILPEGQGVIKNGDGVIFFNFRPDRVKQITKCLLGQKNDVFEVRNIGLSCFVTPVEYGKDLETDVMFKHSDVHNTLKSILASNGKTIFSIAETEKYAHVTYFFDGGVNIVHEGEEKVLIKSKIMQSYAFCPKMSADKITEAVINSLNNDPKDFYLINYANADMVGHSGDFVATVKAIEYLDKELKKLYDLVIEKLDGVMYITADHGKAEKMFDVSTGQPCTAHTNNLVPFIFIKRGLENSDLKLDLTELADIAPFILQNMAIVVPKEMKK | Cofactor: Binds 2 manganese ions per subunit.
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
EC: 5.4.2.12
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 520
Sequence Mass (Da): 58084
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A0A2D7A673 | MKAPEFWKSGSSSMLPSVLAPLSLLYQLGANLYRSNTIPGLKTSAPVICIGNITAGGTGKTPVAIDLGKRIKKIGAKPHFLTRGYGGKTIGPLRVEKCHKAAEMGDEPLLLSRLADTWCSRNRAEAAKMAVKRGAEVLIMDDGLQHTSLHKDFSFLVVDGGFGLGNGRLLPAGPLRETLQAALPRINAVICLGEDVTNILREIPAHIPTLTAVIEAGTAADGLVPQVEPHKVTKVSYLAFTGIGRPEKFYETLIKAGANLADTVSFPDHHPYTTNEILNLKQKAKQLNARLITTEKDIVRLDSKERDDIVSLAMRLRWDDETALDDVLFKIVKGVDDADSAAGP | 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: 344
Sequence Mass (Da): 37102
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A0A927X0Z8 | MKDLKLIETKLNEIDNKYVDLTNINKKNIIEFINELKALLFPKVLKRNLSVKRLYIELYEILNGIDVEEVESITNHFFDNIIDIKSILIKDVLTFVEKDPACKNSSEVVFSYNSFHAIFIYRVAHLLNELNVEILPRFLTEYAHSITGIDIHPGCNIGENFFIDHGTGIVIGETTIIGDNVSLYQGVTLGAKSLKDAPLLRGKKRHPTISNNVVIYANTTILGGDTIIKENSVIPGNSFITKSN | Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 1/2.
EC: 2.3.1.30
Catalytic Activity: acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
Sequence Length: 244
Sequence Mass (Da): 27476
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A0A1H7PD35 | MLLESGPKLLHPWQDEPIDYRCAAMRFSREPGQAAPGIVLPDRIARAAPRRRAEWLAGRRCASEALRLLTGQGACPGMASDRSPLWPVGIVGSISHSGDVAIAIAARAGACRGIGVDIERLMDGQGASEVASEALTPRERRRLGNDPFSVTLAFSAKESLFKALHPLLRRPISFQLSELVAWNGQGTARLRLVEGLSSEFPAGREIEARFARFGDLLLTRVLIPA | Pathway: Siderophore biosynthesis; enterobactin biosynthesis.
Function: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3-dihydroxybenzoate (DHB) and L-serine, respectively.
Catalytic Activity: apo-[aryl-carrier protein] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[aryl-carrier protein]
Sequence Length: 225
Sequence Mass (Da): 24369
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A0A927X9A0 | MRYPAIDELSTKADSKYKLVIAVAERAREIKATGKSFLAQTRNYKAIGIALEEISADKVTII | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 62
Sequence Mass (Da): 6871
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A0A960R8R9 | MKLAGALVAGGRSTRMGSDKAFLDWNGRPLYVTQLEKLHSIATPGRLLLSARRGQAFPDYLTDVTLVWDTSDDLGPIGALRDCLKRLAPDENLLFLAVDLPRMSESFLDRLRHLADETGSGIVPKVEDQWEPLAAIYPHAILPLVDDQIERGELSLQRLCDRAEAEGWIAACPVPANEIANFANVNTREEFDLIQQGQFDHPTLLNRFSLEKGFVETHDRLAAEEPLEIRVEEKSVAVVMRTPGHDDELAAGFLLTEGVIRSSADLFEIRRCRDIAEPHLSGNVIAVQLAPNHEADLEKLTRHVFTSSSCGVCGKATIESVFQDFPAVGSNLQVSPETLLSLPVRLGDAQKTFQKTGGLHASALFDREGTLTLLREDVGRHNALDKVIGRSLLDDRLPLTDSILLVSGRISFELIQKALAAGIPILAGISAPSSLAVEFAKQSGQTLIGFLRETSFNVYSGHQRVLQPDP | Function: Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Subcellular Location: Cytoplasm
Sequence Length: 470
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence Mass (Da): 51484
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A0A927X4M4 | MAKVFALAGNPNSGKTTLFNSLTGATAKTGNWPGVTVEKKTGKYREDTIVDLPGIYSLSPYSPEEIVSRNFVLKENVDCVINIVDGTNLERNLYLTLQLLETDVPVVVALNMADILNKKGVEIDVDKLSMKLGVPVMAISALKKNGLDDLIALATKAANDGRAGKTVLRSKELADVAAMLDKHKYFNAAKLIENDELICSEYESLKESVNSIRAKDATSYAEDFANERYSYISNEIIKNVVVKAKDVSNRTEKVDKVLTHRIWGLPIFLLIMFSVFHLTFSEDFLFLSALGIIPEGAFDIPIIGDSAIASPGIILFNIMDWIVGLIGDGLANLFANAPEWCSSLIVDGVWGGVGAILSFVPNILVLFFFIAILEDCGYMSRIAYLMDKIFKGIGLSGKAFIPLLSCFGCAVPGIMATKTLKSDKERRMTIMLTPFFSCGAKLPIWTAFALLLFDGAFAELIVFGVYIFGIIVAIITAAILNKIIKGKQEPFIMEMPDYHMPQGKNIGILIWDKCKHYVVKAGTLIAASTVVLWFLTSFAWNFSMVEDVNDSIIGSISNFIAPIFWPLGWGGGEFKGVFVIGAFAGLIAKEEVPAIFESLGLLEAAVASVAPAAIFSYMAFNLLVVPCMAAVATARGELNNKKHFWLTILFWVATAYISAMLVYLIASLISVAWWVSIILVLGLIAAVVVCAVLSIRRDRMMYGVN | Function: Probable transporter of a GTP-driven Fe(2+) uptake system.
Subcellular Location: Cell membrane
Sequence Length: 705
Sequence Mass (Da): 76971
Location Topology: Multi-pass membrane protein
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A0A920Q2H9 | MNDLAQGSPPSPGSVTHVRVGLLGCGHVGAALAVLVAERRAEVGRRRGLDLEVTRIAVRNTAIDRDVPVADGAFTTDAAAVVCDPDVDVVVEVMGGVEPARELVSAALSAGKPVVTANKELLANHGAELYALAAASGVDLLFEAAVAGAIPIMRPLRESLAGEPIQRVMGIVNGTTNFILTRMADDGASYADALAEAQSLGYAERDPTADVEGYDAGAKAAIMATIAFGARVVAGDVYHEGISGISVADIEFAADLKHCIKLLAVAEQTVADDGEAQIGVRVHPTLVPLDHPLASVNGSFNAVFLEGGAAGDLMLYGRGAGGRPTASAVLGDLIDAATNLRQGTASGIGVLERARIAPIDDVISAYYLNIEVDDRPGVRALRWQRCSAHTRCRSGRWNRRAWAVRLDWCSSPTGHANEICGPRWPTSARWTPSGP | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 435
Sequence Mass (Da): 45356
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A0A927X266 | MSNVSCEKVLLKISGASLGNDKNGFDLSVFKEVAKQIKELVHSGIKVAIVVGGGNVWRGSLGASYHLDPVKADYLGMTSTLYNGYLLEGLLKQIGVKSVVYSAVRVKNLTKKYSKIFARQDLQAGKVVILVGGTGKPFCTTDTAASLRASELGIDTILMGKNGVDGVYSDDPRVNKKARKFDHLTYDEILEKKLRVVDDTSIEICKKNNIKMLVFNINDMDNINRVIKEESIGTLIEGE | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
EC: 2.7.4.22
Subcellular Location: Cytoplasm
Sequence Length: 239
Sequence Mass (Da): 26132
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A0A4S2FE11 | MNLIIGLIAFLFMLSVIVIIHELGHFAMAKKFGVFCKEFSIGMGPALWQKEGKETTFSIRAIPFGGYVMMAGEQDGSQDESEDDWLKDVPAARRLNNIAPWKQIVIMLAGVTMNIVLAYALFTGLAMARGYVVEDAKPVVYEVVENSPAAKAGLQKDDEIIRVTNGSESIEPQRQFDVIEFIQYNPTESTYTIARGNETLDVKITPRYNKDTQTYEIGSIATSYARPIAWYEAFKVGWDDMVDSGSSIFRSLGQLVKGKGYENLSGPVGILNLTKKTTEMGWMSYLSLFALISLNIGIFNLLPIPALDGGRVLILLIERITRRKINEKLVENIILASFVLLIGIFLFATYNDIAKMF | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 357
Sequence Mass (Da): 39799
Location Topology: Multi-pass membrane protein
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A0A9E3YAG9 | MKNLLAEFREFVDKGNIVDAAVGLILALAFKPVVDSLVNDVIMQVVAAIFGQPDFSALSIHWGDPVSVDEFGRTIYDGGQIFYGSFINTVISFLIIAFIVFLMVKAYNNFKRSKEEEAAEEAGPSEIDLLTEIRVSLKK | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Subcellular Location: Cell membrane
Sequence Length: 139
Sequence Mass (Da): 15379
Location Topology: Multi-pass membrane protein
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A0A920U9K6 | MLSRLWYYVRETFVSLWRNLSLTVAAILTVAISLSLVGASLLIREGADRATAQFQEGVEFIVFMRADASADQDGAIRDVLDNSPAILGYSYVDKAAAYAEFQELFSDKPELVESVTAEVMPPSYRIVPANPDAGNVAEMARQFGEQPGVKEVATATDAIRQIEDFSNRVSQALLVAAVVLVGVSALLILNTVFTAIGARRQEIEVMKLVGATNWFIRIPFMLEGTIHGLIGAALAVPALFVVDDRVLAYFQESDAVPLFRGFAVPEGFVWDTSIWLLVIGGVVGMIGSAVAVTRYMDV | Function: Part of the ABC transporter FtsEX involved in cellular division.
Subcellular Location: Membrane
Sequence Length: 298
Sequence Mass (Da): 32342
Location Topology: Multi-pass membrane protein
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A0A1W9P6A9 | MPDTIAAISTPLGEGGIGIVRISGKNALSIADKVFRSPQEKKPSKFESHKLHYGHIIDSEGRIIDEVLLSVMFADRSYTREDSVEINCHSGIVVLRKILDLVIENGARLAEPGEFTKRAFLNGRIDLSQAEAVLGIIEAKTEAGLRAAIGQLEGHLAVKIKEIREALLDIRTQIEAEIDFPEEDIPFVAPEEVLKKAERAKTEIEKVLEKAGQGIILRKGILTAICGKPNVGKSSLFNALLKKDRAIVTPVPGTTRDTVEEVIDLKGIPFYLVDTAGIRESENLVEKEGIIRSQNSLKRADIVLFIIDGSRDIEKEDKQIAREVKNKKLLLIINKIDLPQKVSLQKLCQDLDLEAEVVSISATEERNLPLLEKAITDSVWQGDVYSSAGDLLISNLRQKESLIKARQALINFKQGIEKEVSEEFLAIDLKEAIDSLGEISGETASDDILERIFSKFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
EC: 3.6.-.-
Subcellular Location: Cytoplasm
Sequence Length: 460
Sequence Mass (Da): 50800
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F0SBY0 | MATIKASVPKGTRDFGPIETQKRNYIYNTIKSVFRKYGYQEIQTPTMENLDTLTGKYGEEGDKLIFKILNSGDFYEKASAKKTAEGDFSSKSILPLISEKALRYDLTVPFARFVVMHQNEITFPFKRFQIQPVWRADRPQKGRYREFYQCDVDVVGSDSLLNEAEFICIYDEALSKLGLKDFSIKINNRKILTGIAELIGKPNQIVDMTVAIDKLDKIGLDGVEKELLSKGFTGADLEILKPVILLNGSNNEKLAQLKMVLKDSLNGLKGIEEIETVFSYLAGFDIKTAKVELDLTLARGLNYYTGCIFEVKTNEVAMGSIGGGGRYDDLTGMFGLKNLTGAGVSFGADRIYDVLEELNLFPKTAEESTKVLICVFGKEEEQYAIPLLAKLRSVAINAELYPFGAKLKKQMQYANDKHIPYTIVIGSDEMQSGKLTFKDMNSGEQKQATIDEIVRSLSC | Catalytic Activity: ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)
EC: 6.1.1.21
Subcellular Location: Cytoplasm
Sequence Length: 459
Sequence Mass (Da): 51311
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A0A0G1WIW2 | MEELIKTFHIDWKLIIAQLVNFAIVLFVLKRYAYGPVLKMMTERSDKIEKGIKDAEHAHKKLAEIADKEKEVLVEARKQASEIIIAAEAIALKNKEVIIAESKQQAEKMLSDAARKMEAEKNQMMQEIRTQIADLIVIATEKIIDEKMTTDKDKVIINNAING | 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: 163
Sequence Mass (Da): 18560
Location Topology: Single-pass membrane protein
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A0A927X0A5 | MEDFMKIETKNIVASKYEVNVVMEGTEWTTEVDKAFNKLAKNVSVPGFRNGKAPKEMIKKHLSQQKVYSEAIDSAMQIAYQKALEESKLQPIIRPSVEVKDFAEDHFEVTFVVTIAPTVTLGQYKDITVQKEEVSVSEEELSRALKNVQERNAELTMVTDRAVEKNDIVNIDFTGYVDGKEFEGGKAKGYSLTIGSNTFIAGFEDQIIGMRTGEEKDIFVVFPENYVPDLAGKNATFKIKLNDIRVKVLPELDDSLALDADIENVSTLEELKNHLTADIKKSKQQQQDSKQFQDLLNKIVEGATVEVADTLVNAQIDYKVDGLKKQIEQNGITFDQYLKMTNSNEEKLRESLVNDATKSVKTTFVVEEIIKVENLNVTGEEVEAEVTKLANQYNIPVDEFKGKVKDQLDYLYYNLRDKKLYDFLKTNNNF | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 430
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Sequence Mass (Da): 48784
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C7YN79 | MSAVRQFTRTASRVSAQLRVPAQRRFASTVENEFIKERQHIKDHAKGTTELWKKISIFGVIPALALSAANAYWLWNEHWDHWNHMPPLEERTEYPYQNIRSKNYQWGDGDKTLFWNESVNYHNKDKVA | Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Membrane
Sequence Length: 128
Sequence Mass (Da): 15187
Location Topology: Single-pass membrane protein
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A0A329MDI3 | MSEEKKDSELKPEEAAKTNEIPSADEKKEADSSAAISRDDAQKQSPDKPSSTAPSEASTGASEAENVQSPASGDEAPAAAAKPANSDSAKPDGDAAPAASSADAEKEAKIKAAAEAREARARERAAKAAEAGEGGAEAAAPAASGGDADAEKEAKIKAAAEAREARARERAARAAEAGEGGAEAAPPAASGGDADAEKEAKVKAAAEARAARARERAAKTGEGADAAPAAPKEPSPKQPVLDRLVQLLKDHVAEDAVEEASINERGGHRPTIVVKGDHWPAAAELLKSSPELDLNYLRNLSGVDMETHLEVVYHLISLNSKEEYTVKVKTNRDEPTVPSVTPIWSTANWNEREVYDLFGIDFPGHPDLRRIMMSDEWVGHPLRKDYEPLDPEV | 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: 393
Sequence Mass (Da): 41232
Location Topology: Peripheral membrane protein
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A0A930Z2B7 | MNTTPDPQPDDRPLDYPVVLRVAGRRCLVVGGGPVAARRASALVEAGARVTVVAPQVVDTIERLSRRRPGIDRRTQDQPDPSASLEIERRPYEAGEAGRYGLVVTATGRAEIDGQVVADAVAAGVLVNSADGHSPGSLQLPAVHRDGPITVAVSTGGASPALARWIRDRIVASIPAGAATMATLLDEARLAMRQGGRPTGSVDWDTVLDRQVAPLIAEGKVDEARSALFQACLLPAPESPPAPE | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 244
Sequence Mass (Da): 25503
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A0A832F1J6 | ERVRRALPEAAPVRFACELKIDGAAVNCVYRGGTLEVGATRGTGEVGEAITQQLLAIAKVPYRLSDEDPPALVEVRGEVYYPLAAFEQMNAERIERGEATFANPRNAASGTLRQKDPTRVAGRPLALFVHSLGRVEGRSFVSHESFLDWALVAGLPVASSTVFVDDIDDVWRAIERFTIERHSYGFEVDGVVVKVDDLAQRSVLGATPRAPRWAIAYKMPPVEQQTKLRAIEVNVGRTGKVTPFAVLEPVAVAGVTITRATLHNEAQIHLKDVRIGDTVVVRRAGDVIPEIVGAVVSERPPGAVPWTMPARCPFCGEPLVRPDGEAHHYCENVDCPNRLLESLTHLASRAALDVEGLGEKTVVLLHDAGLLADLADVFRLVDHRDELVALEGWGEKRTDNLLARIADATARPLERLLVALNIRHVGPTVAKELARQLRTLEGVASAGTEELAAIDGIGPTIAVAVRAWFATPRNRQLATDLVALGLRTDTDLAPPDPQASPPLGGTVFVLTGTLDGFTREELKERLELLGAKVAAGVSARTTAVVAGEQPGSKLVKARDLGIPVLDEAGVRLLLGGEPLATVVEASDAARRAAEHVEAQQ | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
EC: 6.5.1.2
Catalytic Activity: NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.
Sequence Length: 600
Sequence Mass (Da): 64417
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A0A2C5Z5D3 | MAPSKSAFDSKVILQTGSPRGRDLSIKLSRPSQTSSEAWFNKTQPLLDVLSPTPQETDDDYRRVKIAVIDTGISPDHPLINDFIVKNFVETPNGRVRDDPKHGTDSIDLILTMLDTAKIYVARVFQAKEGDQLTPGYMAEVSRLPSGSLLYVDIISISAGFEHSHAKLAEAIRRASAADPEILIFAAAANWANTQSVAYPARLTGQVFCMFSTNGALRNSRDFNPNALDNADNFALLGQDVKLNPLSREGLSGTSIATAVAAGLAGRIIDFTRHADSRGHLTQQHRNKVASKLGLREIFHFMSQDHKDLEYRCVAPWELLPPEEMSAPTQHREDTRSKICGTIERALWKLNIVARQEYHKKLLTKLFGGNSRHACYALAATIFSLGLVRDWLYKQAIQEQPSHALLLTPASRLAGISLLVAGNVLVLSSTWALGITGTFLGDYFGILMDDMVTGFPFNVCGAPMYWGSTMSFLGTALLLGKPAGVFITAWVYIVYCAALRYEDPFTSAIYAKRERERAAMGGAAKKQI | Pathway: Lipid metabolism.
Function: Catalyzes the second two steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylmonomethylethanolamine (PMME) to phosphatidyldimethylethanolamine (PDME) and of PDME to phosphatidylcholine (PC).
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phosphocholine + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.71
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 528
Sequence Mass (Da): 58024
Location Topology: Multi-pass membrane protein
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A0A5C8NRS1 | MQTPDTWRHAPAPHPLVVPIDAFSDNYLWLVRAPDGETAVVVDPGDAAPVRRALAESGLRLVAILLTHHHADHAGGVAELVEQWSCPVYGPAGEDIPDIDRPLAGGDAFEVASLRARFEVLDVPGHTRGHIAYRCGRLGADPRPLLFCGDTLFAAGCGRIFEGTPQQMLDSLDRLAALADDTLVFCAHEYTVSNLRFAAAAEPESGEVAGRLAEAIRMREHGLRTVPTSIGIERATNPFLRSGEPSLRRAAAVRLGREPASRLEAFAALREWKNVYR | Cofactor: Binds 2 Zn(2+) ions per subunit.
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
EC: 3.1.2.6
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Length: 277
Sequence Mass (Da): 30046
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Q65RL0 | MNTMTLVFLHGLLGTKSDWRKIIENLPHFRCVSLDLPFHGEHKFTEANNFEQCADFISHQIKSAVGNQPYFLVGYSLGGRIALYYALQSQCEKGNLQGLILEGANLGLTCDEARKVRWKNDEFWAQRFITESAESVLNDWYQQPVFAHLNAQQRADLIEKRVTNCGKNIGKMLEATSLAKQPYLGDKVRESTLPVYYLAGEKDQKFRQMAVQEKLNLQLIANAGHNAHLENPVEFSQKLTALLRNHKIKKTDNL | 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: 254
Sequence Mass (Da): 28980
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A0A154PDE1 | KKQDIKWAAVLWYIHLHVLGVYAIWLMITSAKWMTVLFTLFITSIGCLGVTAGAHRLWAHRSYEASGLLRLFLTLAHTLAGVVRFLYSHYMGNFQSPKVDYEQAKIDIDMRDIENDGYVWAQKKIPPDSISVFLVRKSKSLAYHYMILKSGEFGTYDSGCSTFFIKMWYELGLVNNLITTTSNDIRDVLHQVARKKITMDGALNKLKEMSEYNMKKNRLV | Subcellular Location: Membrane
Sequence Length: 220
Domain: The histidine box domains are involved in binding the catalytic metal ions.
Sequence Mass (Da): 25371
Location Topology: Multi-pass membrane protein
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A0A154PGP8 | MYFCVNDLQNNECKEYFTEPQIVGTYCFDGNRCYHSDLSQLKYYKEPRNLNNVDFNLDDNLNTIQKLDNINKKIDYLLKWISENFNHLQMERSKNRRWLEPEFVCYRGVLSNLLATPFDSRDGWIICASKFKGTIYLCGFDTDKKKRYEINKNEFHKRCTSWGYKFEQYLVSDSPSENPDLSKPLNQNEEFCCVFKSRLGNNILLYGAEVDAVCSEHPIQDTLIGKKVELVEMKTMHHNALNLYKNSIASYRAHRTLKWWVQSYLVGIDKIICGLRDNNGIVHSIQKFNLNKLVKDSKHDWNPEGCTSFCTGLLERMKAVISQNYDKCLYKFTYIPGKNTITVEELKPTPDLEYVFLHPWYITKANQYFEK | Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA.
EC: 3.6.1.-
Subcellular Location: Nucleus
Sequence Length: 371
Sequence Mass (Da): 43752
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A0A0B8QHJ9 | MGKSLVIVESPAKAKTINKYLGKDFIVKSSVGHVRDLPTAGQSSGAKAKPVSTKGLSAEEKARIKKEKDRKSLIKKMGIDPYHGWEANYQILPGKEKVVSELQKLAKNADHVYLATDLDREGEAIAWHLREIIGGDEERYKRVVFNEITKNAIQQAFESPGELNMDGVNAQQARRFMDRVVGFMVSPLLWKKVARGLSAGRVQSVAVKLVVEREREIKAFIPEEYWDIHADTVTKAASDFRLMVAQRSGEAFKPQNEAETKAAMSILEKAEYEVCKREDRPTKSKPSAPYITSTLQQAASTRLGYGVKKTMMLAQRLYEAGYITYMRTDSTNLSKEAVEAVRGYIGSEFGDAYLPAKPLVYGSKEGAQEAHEAIRPSSVDVKSEDLSGVDADAHKLYALIWNQFVACQMTPAQYDSTTISVKADEFTLKAKGRILKFDGWTRVQRPMGKNEDQILPEVQLGDKLDLKALDPKQHFTKPPARFTEAALVKELEKRGIGRPSTYASIILPFKTVVM | Function: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
EC: 5.6.2.1
Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
Sequence Length: 514
Sequence Mass (Da): 57309
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A0A924M0Y9 | MKRIGITGNIGSGKSAVSSILRTRGFTVLDADEVALRVSSDPLTLLEVSEALGPQYVTERGLNRPLLAELVFKNALALETLNGIIHPRVRAQMSRLEGEATGATVFQDIPLLFENGLEHGFNATILVDAPIKTRLERVRKRSGLTAEQFWARENAQMSPQQKRVRADWIVKNTGTLEQLEREVLRVLEGLDLGG | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Length: 194
Sequence Mass (Da): 21398
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A0A960F6M7 | MSGFSNAYRNNTNVNFPRMWPRAALVIGALLLISVVALLVRGLNLGIEFEGGAAWEVDAHGVSTAEARDALRPLGLADARIQTGDDILRVRAELDQSDQKVDEVSQALSDLTGTPLDEVNQTVVGASWGDEITKKAVRALIVFFIVIAIYITLKLEWAMAVAALFAVANDIVVTVGIYALFQFEVTSATVIAFLTIMGYSLYDTIVVFDKVKDNEGRLAATGKLSYPGLMNMSLNQVLMRGVNTTVTSILPVLSLLLVGSLILGAVTLQEFGIALLIGLLSGALSSFFIAAPVTVWLKERFDSRYAEARERAVARAGGTKEAREAVRSQVSSVEDAKAQLQGPDADFGTGGAPRGRKQGKRR | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Location: Cell membrane
Sequence Length: 362
Sequence Mass (Da): 38863
Location Topology: Multi-pass membrane protein
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A0A7C1UG96 | FEGHTDVVTEGDPSEWTHDPFGAEIVDGRLYGRGSADMKSGLAAMIHATAAVASAGPFPGRIVLGALCDEEEMMIGVKRFVADGRCEGIDGVIVCEPEEGEICAVSKGAIRLRVDAVGKMAHGAMPDKGANPLAALARLAVDLADLQAELQDRFGVHPHLGKVFVTPTVISGGSLIQMNVIPAEATMAVDIRTTPAVDHAEVLARVEALAAEAGKGAGVELSIEVVDDRPSTDTPEDSAVVRALVGAHERVTGRPAVLGGVPGSTDGTILWRDGRLDTVVYGPGGKWIAHQVDEYVEVDAVIEAANVYVAAALEFLGS | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3.
EC: 3.5.1.18
Catalytic Activity: H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate
Sequence Length: 318
Sequence Mass (Da): 33072
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A0A2C5Z5J7 | MPPRRWARRLERACCTLGTYVPVAFVYGMTTWAVWVVIVIGGAEPVSRWRGTPSSVVGLALYLLLNWSYTTAVFTSPGSTTTDDGYGLLPTAAARPSASSLTVKSSNGQVRFCKKCQARKPDRAHHCSSCRRCILKMDHHCPWLATCIGLRNHKAFLLFLIYTTVFSLYAFALSGSWLWSEVVVESARYVDSLMPVNFIVLAVVSGIIGLVVGGFTAWHVLLACRGQTTIECLEKTRYLSPLRRMHQQQALPPPAQRLVDMHANALPGVTRPEEGESSVAMVASADGGCDDDDAEVDVEAGALFAGRRPVSYADRERQQTRRRYEDYLDEHDSDKLPNAFDLGWRRNLTHLLGPRPALWLVPICNTTGDGWAWEAGPRWLDARERLRRERQRQREREISAGWGAAAEGEDEENRQRRSPSKADRVLGRDPDLYADGTQGGWTGCFNGEVILMVRSTFLRRRVDLTLTLRVRQDRMFNGEVYQMVL | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 485
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 54494
Location Topology: Multi-pass membrane protein
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A0A7X7XQH0 | MTIKDHIKHRFAAIYNTPPVAVYFSPGRVNLIGEHIDYHGGLVLPVALSIGTYGAYSLRDDDEVRLYSTGYSDYPITINLGDLSKDSFTGWANYVRGVFQVLKDEGYHVPHGLNLYLESDMPTSGGLSSSSSLELLIIKMLNDIFNFGIDRTKMAVLGKKVENEYIGVLTGIMDQFVIANGKKNNALLLNTNTLKFDYIPLDLKDYQLVIVNTNKRRGLADSKYNERWNETMGALKTLKNHFKINNLTELKSSDLPQIEKLLDPLLFRRVRHIITEQERTLESAMLLKEGKIEEFAKLLTASHNSLRDDYEVTGLELDTIVLLLLETGAIGARMTGAGFGGCAIAIVPKEKVEKQAPLVIDLYKKVIGYAPSFFASDSSDGTHELK | Pathway: Carbohydrate metabolism; galactose metabolism.
Function: Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P).
Catalytic Activity: alpha-D-galactose + ATP = ADP + alpha-D-galactose 1-phosphate + H(+)
EC: 2.7.1.6
Subcellular Location: Cytoplasm
Sequence Length: 386
Sequence Mass (Da): 43085
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A0A396TV01 | MGPTASGKTALAMALYDALPCDIISVDSALVYRDMDIGTAKPTQAELKQYPHALIDLRDASESYSAADFCRDALDKIAQSRANNRIPVLVGGTMMYFKSLIEGISPLPEANPDIRKAIEEEAVSKGWPAMHEQLATFDSVSAKRIHENDSQRISRAIEVYRITGNTLTQLSQLKGDKLEGNVLQFAISTSERSELHDRIALRFNQMIDLGFEKEVVKLKERGDLHEDLPSIRCVGYRQMWQYLNNECSHDEMVFRGICATRQLAKRQLTWLRSWPDLHWLTTNDERNLSKVLSMVKVTP | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Length: 299
Sequence Mass (Da): 33800
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A0A142JDD1 | MLFLVIMQAQGFKVAKSDGTVLDLAKISAKIKEASTFAVSVKEVHTLVKSVDNLAKDIEKK | Function: The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion.
Subcellular Location: Cell outer membrane
Sequence Length: 61
Sequence Mass (Da): 6634
Location Topology: Lipid-anchor
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A0A7Y2DNZ0 | MSRPIDLTTKPSIHVIGCGGTGMAPITAVLAHLGLSVSGSDQRPSATLDALSDLGVRVTVGAGYDDIDDEAVLVRSTAVPDDHPEVAAALLTGRPVHRRADVLAAITDIHRTVAVAGTHGKTTTSSMVTAALAGAGVDISSIVGGKILGLDQPVPGAVLGEPGGVLVVEADESDATFVELVAEVAVVTNIEPDHLEHYGGEAGLLSAFDTFLTNDGLRAAVVCADDPGVGAALDRTQADRSRLVTYGQVAGCDVGLHFDPPAATVRIDGFERRLEPRLPGLHNALNLTAAFAVAAALDLDLESAAAALDRFEGVGRRFERRGVSGGVQVVDDYAHLHGEIVAAIAAAREVCDGRIHVAFQPHRYSRTEALWHTYADALLTADSVVLTDIYASGEDRRAGITSDLIFDDLVGRHPRTALVRVGTPAEVPAALAELAQSGDLCLLLSAGDLPSIVESLLDALRTTP | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
EC: 6.3.2.8
Subcellular Location: Cytoplasm
Sequence Length: 464
Sequence Mass (Da): 48116
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C7ZPQ9 | MDSFMLGDEGVRDRIRQAEEFLDPNDPQVRSYRSDIILMLQKNERRLTVNLDHVRNHNAELAQGLLEQPFDYTLAFDQALKNIVQALPQARPDQSAKDTVYYCAWAGSFGLNACNPRTLSSHLLNYMVSIEGIVTRCSLIRPKVVKSVHYNETKDRFHFREYQDQTMTNGVTTSSVYPREDDDGNPLITEYGFCTYRDHQTISIQEMPERAPAGQLPRGVDAILDDDLVDRVKPGDRVQLVGIYRTLGNRNTNHNSALFKTMILTNNVVLLSSKSGGGVATATITDTDIRNINKVAKKKNLLELLSQSLAPSIYGHDYVKKAILLMLLGGMEKNLENGTHLRGDINILMVGDPSTAKSQLLRFVLNTAPLAIATTGRGSSGVGLTAAVTSDKETGERRLEAGAMVMADRGVVCIDEFDKMSDVDRVAIHEVMEQQTVTIAKAGIHTSLNARCSVIAAANPIFGQYDPHKDPHKNIALPDSLLSRFDLLFVVTDDIEDTRDRHVSEHVLRMHRYRQPGTEEGAPVREQGGQSLGVSATSQADSQGPTEVYQKYDAMLHSGVTVTSGRGANKKPEILSIPFMKKYIQYAKTRIKPVLTQEASDRIADIYVGLRNDEMEGNQRRTSPLTVRTLETIIRLATAHAKSRLSNRVEERDAVAAERILRFALFKEVVEDASRKKRRKTQAVDFASPSDESSSDDDQDGTQADGTRSNRSTSRATRTSSRLQTTSSRAARNGGDTASSSREPNLDEEEEDALAQPTPRRSGRRTQNTSQSQTSFASSIPASQLPSQTQAESQKDDELADGTAGLAIDDTPISAQRLGTFRTALGQLLSTDLFEDDSAELDAVVEAVNRKVGNRDGGAFTKGEATKALQKMGEANQIMFTEGDLVYKI | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 889
Sequence Mass (Da): 98058
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A0A960T0Y0 | FYLAVILHDTGRAENVREHTDGSAILAARLCNRLQIQGARRRLIMFLVDNHLTFWRTATSRNLDDPEVIAEFAAIVKTPANLDALLLFTYIDSNGTAPDAWNGWKESLMLQLHTATHAFLDSGREQYEKKLNADRLALRKEVTGLMREDYHADVRKHFDRMPAAAFHFRQAAHIVTQVRTVRHFLQRESENKDGIAFNVKWIDHPDRGNTEMVIVTRDRPLLLEKICCALASEQINILSADFFTRSDGVVVNIFRICTTNFEPVSSAETRKRFLQTFDKILHAEKFEPEKYLKRRANFLKARNDHDIPVPVRAYVSNELHPTCTTVEIQALDRIGLLHDLFHTINSHDLETVHARISTEKGVAMDTLYITEANNGKVSDPALLEQLEQEFTELIGRREQPE | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism.
Catalytic Activity: [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
Sequence Length: 401
Domain: Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
Sequence Mass (Da): 46033
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A0A395JRG3 | MHQRSLFTHLLFFLFTLISTSPAFATDAKDFRILLTNDDGINAQGLHALVKTLSPHYDVVVSAPAKKWGGRSHGTLLWEGPMEVSKFNLKNTTSDTPAYHVSAYSVQGLPADAARFGIIQQREKNQAVDLVISGINHGENLGSLSHLSGTIGSAMEGAYYGIPAIAVSIESKAAKENKFEAATQAVLTLVEGIRENGLPKGVVLNVNVPENAKGGMRIAPMDHDNVKVDGFTQTGDKFEPTFSYPKANLSYSDMTVYEQGLIAVTPIQLDWTDHEAIKLMNTWDLDN | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
EC: 3.1.3.5
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 287
Sequence Mass (Da): 31245
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A0A389M4T0 | MIAHIKGTLTTITINSVVVDVHGVGYQIFVSNPYESKQNTEVFFHTYHHIREDINVLYGFKTLEDKDMYIRLLSVKGVGPKVAMTILATTSSSMVIHAIDTEDVAFLKKIPGIGPKAAGQIILDLKGKLATNLETPANQNQNEAIEVLLALGYTKKEIDFALKGVGTVEVEVEVIVKAALKNIMR | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Subcellular Location: Cytoplasm
Sequence Length: 185
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Sequence Mass (Da): 20308
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A0A345DBE8 | MPTAAPSHALDRTRYQAGRSMLFSQFTANNSPTRAVRRLMRELTHLTDLCVLEAWAHCIGTLPDNLRHSSSLIAIGGYGRAELLPNSDIDLLVLIKTDHLPAESKAQLSLAIEQWVSMLWDMGVTLSHSVRTIDECIADALEDLSIQTSILEGRYLAGDKKIHQTFYAAFNRHFDLLTFWREKMAEMRQRHSKFDDTPYSLEPNCKESPGGLRDLHLMLWLAKAANIGQTWQELHHNNWLTASQLRLIQRSENQLLAIRAHLHILSKRMENRVLFDLQTPLAHAFGLFETDGKRAGEHLMQRYYLAARAIYQQCALFVQKFELFLSPPSAPHIAHKIKGFPDFVEVDHVLDVVRNDAFIRKPHLLIDVFYVYGQVTGLTGFSPKLWDAILQARNLITPEFRRTPENRSKFIRLLKLDNGITHAIRLMNQTGVLGRYIPAFRRIIGQMQHDLFHIYTVDQHILTVVRNLRRFTLQEHMQSHFLANQVMAEFGQPWLLYIAGLFHDIAKGRGGDHSDLGAIEVARFAKQHALTKKQTTLVVFLVKHHLTMSTFAQKEDLSDMETIQRFASTVKSVENLQALYLLTVADIRGTSPKVWNAWKDKLLADLYQLTLRELSGQTQAPVSMLKERTMDALELLPNAEIQAQAQALWNDFDTEYFMRHDATTIAWHAEHIVQRPKHTGKTSAVVATKPFNNDHSLHVMVYTADVPDLFARLCSFFQQRYLSIFDAQIYTSGQGIALDTFQVLLPESHQADALFVQRLNQELRETLTTAPALRAPNLGRLTARSRNFPIVPRVSLTPTDKGEYVLKLAATDRHGVLYSIAYILKQMNIRLRSARIVTLGERLEDVFILSSDQLNDPSAAAQLEAELMRVCTIS | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism.
Catalytic Activity: [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
Sequence Length: 874
Domain: Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
Sequence Mass (Da): 99660
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A0A194W409 | MGYKFETLATLPAPWGETSREYIENRENEVVNNKAQYCSVVRTGIGKTVLCLGGEVDAVWDSKPPKAGDPVNWVELKTSIDIRNGRDQENFQRKLLKFWIQSFLLGVPKIIVGFRSRDGILQRLEEIDVASIPTTVAQRGRQWDGNVCINFASAFLEWLRTKIDDDGVWRIRRRARDTHIEVYKTKETTGHGRILTDEFINHRIKLSLPPAPDVSDCDGTEEPS | Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (By similarity). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs (By similarity). Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1).
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside-ribonucleotide in mRNA + H2O = a (N(7)-methyl 5'-triphospho-guanosine)-nucleoside + a 5'-end phospho-ribonucleoside in mRNA + H(+)
EC: 3.6.1.-
Subcellular Location: Nucleus
Sequence Length: 224
Sequence Mass (Da): 25529
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A0A6A4V715 | MHIAITGNIGSGKSSVSRILRSLGYPVFDADSIAKAQYEKAEVKAAINDYFHEDLYKNGVIDPACLSQLIFQDTRIEARQFVEALIHPLALEDLNRLAIESKEPIVFSEVPLLYESHGETNFDRVLLVTCDDDVADKRLMEQRGLDLKEIRRRRKLQLSPKIKAILADDIIENNDNETSLVDKVSRYSDKIRSVYGKK | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Length: 198
Sequence Mass (Da): 22479
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A0A9D9DIN4 | MYSVLKGTHDVILDEARKYSYVEAVLIKVAELYNYKEFRTPIIESSDLFTRSVGESSDIVRKEMYTFLDKGNRLITLRPEFTAGIVRSMVNNKLFANMDLPVKAYYVGPNFRYERPQQGRYRQFNQFGIESCGVDNFYRDIEVISLGYNALQMLGFKDVKLKINTLGDDETRENYKGALKAYFSDKINLMCDDCKERFEKNILRILDCKVPSDIEIVKEAPKINEFLSENAKNNFQNITKALKEMDIPFEIDTNLVRGLDYYTGVVFEYQYSSSKNKNYGALGGGGHYGKLIKEIGGPDLEGVGLAFGIERLVSIMNDDELFNDIAQDLDIYLMPIGKESFEEANKLTNFLRLNGFSVEVCFENKNMGQMFKKAERRLAKYALILGENEIKDKKVELKNLKTKEQIEVNYDDLIDTLDNLIDEDEHEHLD | Catalytic Activity: ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)
EC: 6.1.1.21
Subcellular Location: Cytoplasm
Sequence Length: 430
Sequence Mass (Da): 49564
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A0A6F8PVE5 | MIYRPAKAYINLSSLAHNLRLIKQLAPNSKVLAVIKANGYGHGICRVAQQLSNADGFAVASLDEALLLRQKGFLHRILLLEGLFTAAELPQVLHNRLDLVIHSQYQLEWLLAHRHSVALNVWIKIDTGMHRLGFHPDAVQSVVQSLMESDNSYQLNFMSHFASADELQVHSQAFTQQQIECFKTHCQAWDYKCSLANSAGILHYPESHLDWVRPGILLYGAGVPIKPRHPFKPVMRLESQVIALKWIPAGDFVGYGNRWQAKKDTYVGVIAIGYGDGYPRHAKDGTPVVVNGERVPLIGRVSMDMITVDLSHQVDKVKVGDRAILWGDALLSVDEVAQCADTIGYELLTGITLRVPFIEVNG | 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: 362
Sequence Mass (Da): 40312
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A0A2E6W203 | MEKNNSKLGDVKHRLSKNSKVQLISAVVVLFFDQLTKFSVIAWIPFGYSIEMLPILSFVFVLNDGISFSLLSGVSRLVLIPLSLAIITFIIWLAQKNSTSNASAIGYGFIIGGAIGNVFDRSLHGAVIDFILFHYSGWSFPIFNVADTGISCGVAILLIDSFFSSKMKK | 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: 169
Sequence Mass (Da): 18516
Location Topology: Multi-pass membrane protein
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A0A960F6Q4 | MSDEKSEEDGKKGKKKKAIIAGVVLLGAAYQFVLKPSPPPEDPAAAGEEVEIEEGDVVPLPELVVNLADTEEIRYLRVGVAVVLEKGVDGGAVEPELPRISDIVIDMASEYTFEELRADGAKQALKDRLSEAARIEFDDSTVARIIFTTFVMQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 153
Sequence Mass (Da): 16602
Location Topology: Single-pass membrane protein
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A0A9J6RDS5 | MTIYLDAVWLLNLLLDFMILRLTARLTKTNIRPVAMLMAAVVASAIVPFSIYFPDSVFVHPIGKVIYSMLIIWVGFGWKNIRRFMHIWFTFYFVSFGIGGGLTGIYFMFSRSVYLSNGNLITWNSGYGDPVSWLFVILGFPIVWLFTRSTMDKQSLTNYRQDQQFKVMITMNHKQVVTSSYLDTANHLIDPMSKKPVVICDQTVIEQMFTDSEIEQLKNVQETLDVTSLDQHLVDQVHFVPYQGLTAGQRLLLVIKPNQFILFDQEEMYTCTKVLIGLQFDHLTPDETYHCLLNPQIFKELSLQSA | Function: Probable aspartic protease that is responsible for the proteolytic cleavage of the RNA polymerase sigma E factor (SigE/spoIIGB) to yield the active peptide in the mother cell during sporulation. Responds to a signal from the forespore that is triggered by the extracellular signal protein SpoIIR.
EC: 3.4.23.-
Subcellular Location: Cell membrane
Sequence Length: 306
Sequence Mass (Da): 35313
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A0A663F5H8 | IKSMLFGFLLVFLGLALPGSQGKVIPRCDLVKILCQHGFEDFWGKTITDWICMVKHESSYNTKAFHDNGVSRDYGIFQINSQYWCEDGKTHGSKNVCHISCSNDNNEDDIQCAKNISVQRRQKKILLLTGGGGGGGRQWMRSCIW | Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
EC: 3.2.1.17
Subcellular Location: Secreted
Sequence Length: 145
Sequence Mass (Da): 16348
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A0A4U1C535 | MLLPVQQFKDFVNSYTLFMPQDKILLAVSGGKDSVTMAHLFASAGFKFGIAHCNFNLRGEESIRDQNFVKNLADQLGVSFHLQAFETEAYAKEYKLSIQMAARDLRYEFFYSLKESFGYQKIAIAQHQNDAMETVLLNLIRGTGIAGLHGIKVQHHDIIRPLLCFNSADIEEMVEENNISFVEDSSNASTKYARNKIRLNVIPEMKQLNPSLEDTFQKNLDYFSELEELLIETVKNHQAHLFKFKDQHIEIAINDLKKVHPQKLILFELFRPFGFNITTIQNLINCLNGESGRKFFSDTHCITVDRETLTLKTKAQFILREQFIKADQHEAVIGNYHLSIDELASKPLSLIAEAHSIYVDAEELIYPLKLRAWREGDSFKPFGMHGEKKVSDFLISQKIPLDDKKSIPILVNGDGKIIWICGYRSDDRFKVKSNTKKIFILEVHKN | 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: 446
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): 51229
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A0A059EDJ2 | MDEFWRNTVDQAQAYGPQLIKAALVMIAFIIGAFIVRWLIAAAIDRTGLAKKANASTATSDSKSLGTSLAQAAFWVTILIGLMQALAIAGATQISSALHGVIDPILSYLPNVIGAALIFGIFIIIANVVRETLKAVLVFGDGMPERFGLATGRVNISGIVASVAFAVLVIIGAIMAFDVLAIEAISAPANELLTDIIGIIPNVLAAGVILAIFVLIGRFVANLVLKTLPGTGVDSAVSELGLLKGADGGLTASTVIARVAMFLIVLLGLVAALNALGIESLTYAMNVVLDMGVQIIFGALIIFAGVFIAKLVSSAMDSTGAGATDVTARVMKWIIIVLAVILGISRMGLDPTGGVFILEVAKWIVIGGAAAFAIAFGWGGREWAARILESWRSTR | 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: 395
Sequence Mass (Da): 40971
Location Topology: Multi-pass membrane protein
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