ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
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): ... |
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 | MRLVIKYGGTSISSAKDIRAVANHLNSLSKKNQIVVVCSATSGTTDDLIEISQSIKKENKSKAEQLASKITNRHKQLAKQTIKKADLRKKLLKNFDDDFAELVALIDGMVLLGEVTPRTMDYLFSFGERLSIKLVSMAVNDSGKKSVPLTGKEVGIVTDSNFGESKPLIDTTRLRVSKNVENLFSKKTVPVVGGFVGADQHGHVTTFGRGGSDYSATIIGTCIKADEIWLMSDVDGLMTADPKIVKNAKLLKEVSYIEAIEMALFGAKQIHPRTFEPLLSKKIPMKIRSSFNLKNEGTLVTASPSPSVKNTVKCVSNVRN... | 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 | MIEKLPAWLRDRFPPDKPHLVGVSGGLDSLVLLDVLRTIGYRELIVCHLNHGLRGRESGGDAAHVRRAAGALGLPCEVEKVPVSDLAAISGLSIETCAREERWLFFGRMSQKWGCRTVFLAHHRDDQAETVLARLCRGTGVRGLGGMRFCHEIRTAQGIDLELVRPFLEIPREALREWAVGKGLKWREDKTNAEPIATRNRIRNEALPLLEDIFGRDPRPALARLATLAAAESSWMESLAREALEQARDESGALRVLNVAPLPEAVQRQVLRLWLEDTGLPGVDQADVEAVRSLLTFSPGSSGRINLPKNKHCRRQAGRL... | 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)... |
A0A0R2V9M3 | MPNLHTVRKGLDLPILGAPDALVDGHLRASVYAVRPSDFRGLVPKLAVKEGDRVLAGDVLFTDKADPRIRITSPVSGEVARVERGDKRKILAVVVLADSQQEYRKFTSGTPANREDAINWLLESGAWSLVESRPYGRIANPDAEPKAVFINGMATEPLAVAPAVALAGREEDFAMGLQVVGLLSKRTVLSIAASETAPALTKASGVELHQFKGPHPAGTTSVHINQVSPLNKGEVVWTLNYQDVIILGHLARTGNFKLERVLALSGTGIAKPRAITAVAGASLEAFLNAELKSGNYRVISGSVLTGTKVSKAGYLTYYAS... | 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 ub... |
A0A6P6M268 | MLRLALQVRPSGRFTRPSVLPGPAAAASQRSGPVSCHHLRRYQSNGPARIQSLCHGRREYNSILSNGSWGLRSRMASFSQSMRMYSLPPHQKVELPALSPTMQTGTIARWEKKEGDKINEGDLIAEIETDKATVGFEMMDECYLAKILVPGGTRDVPVGGVICITVDNPDLIPAFKDLTLDKLSSSAPPAAASPDPPPPASPAAAPAPLQVPGSSYPPHMKIPLPALSPTMNMGTVHRWEKKVGEKLIEGDLLVEIETDKATVGVEVMEEGYLAKILIAEGTKDIPLGTPLCIIVQKESDISAFADYSETGVDATPVAAP... | 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
Subcellul... |
A0A520XY27 | MPCWQRMAGIPAISSTSVTVCSPRLTRPCWSGSWSGSTRTVAKPRIAIVGGGIAGLAAAHHLVGEDVEVHLFEAADRLGGKIDSTMLGAEQLPAAADNFLARVPQMKDLAHELGLGDELISPTATNAYIYRDGSLHPLPPTLLGIPADLDVLAESSLISNAGVERARADLSAPDDRPEGDESVGDLVRRRLGDEVHEYLVDPLLGGINAGDSDRLSITYGVPQIRAARDRDASLIRAAQNMRSGLIVGAPVFLSLRGGLQVLIDALADELEQDEWATVHIDSPVADLQRGESGWQIEGASFDAVIVAVPPVPASALLSSC... | 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... |
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: [t... |
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, yield... |
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 ... |
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+)-... |
A0A0G1CXA8 | MPTLDDLRKTRIEKLQELKKMGIDPYPSRVIRDQTIAEAKTKEGEDVSVVGRITGRRGHGKICFFDLVDESGQIQIVCKADKVSEKTFALMELVDLGDFLSVQGTLGKTEAGEVSVFAANFQLITKTIRPLPDKWNGLKDIEERYRQRYVDLLMNSEVKNVFLIRTKIIKFLRHYFDSHSFIEVETPILQPIYGGAAAKPFITHHNTLDTDLYLRIAVELYLKRLIIGGFEKVYELGKDFRNEGMDRGHNPEFTMLEFYWAYTDYEKLMQFTQNMLIELVQDVCQTIELDYQGIKLNFQAPWKRITYREAILEHTGVDIN... | 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
Se... |
A0A1Q9NVD3 | MTRNEEEDLANRILYHKRKYYDGEPEISDAEYDKLEEKLTNLNSSHPVLHIVGTPIGGKFNHDPPMLSSDKATTLEEVVKWANKVGDHSLSAGYKVDGLSLSLIYENGKLLQAATRGNGTSGDDVTLAVMLIDDIPKTIPIEDRINIRGEVFMKISEFTKVNSKLPKEQRFSSPRNLAVGTLRQKNVSGIENRRLSFKAFEVLGISENKTIQEQNELLEKWQFSRADFEFIEHNNSEEIDRIFLKIENERKSIDFEIDGVIFKYNEYLDRNEAGSTEHHPKWQIAWKFKSEGSETIINDIIWQVGRSGALTPVALVDQVE... | 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(+) + (deo... |
A0A961AT07 | MYGSFQSLLTETLDSIRDAGLYKGERIITTPQSPHIAVSSGAEVLNLCANNYLGLADHPEVEAAAREAIERWGYGLSSVRFICGTQQIHKDLEKALSEFLGTEDTILYSSCFDANGGLFETLLGPEDAIISDELNHASIIDGIRLCKAQRFRYRNNDMADLEEKLKAAAESSRFRLIATDGVFSMDGSIADLKSICDLAEKYDALVMIDDSHAVGVLGERGRGTHEHHGVMDRIDIITGTLGKALGGASGGYTSGRKEIVELLRQRSRPYLFSNSVAPAIVAASLKSLELLTRSSELLDRLRENTAFFRGEIAKTGLTVL... | 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)-... |
A0A963HDK6 | MSENKKAAGGEHDTAPVSDHKRPYRGRFAPSPSGPLHFGSLVAAVGSYLDARANDGEWLLRIEDVDQPRTVPGAADAILRTLAAFGFEWDGEVLVQSRRLDFYHAALVRLQLDGEVYPCACSRSEIAAHAPPRSVDGGLVYPGTCRAGLAGGRAARAWRLRLPDRTVAFDDRVQGRHQQNLAQAVGDIVLLRADWQYAYQLAVVADDAAQGITAVVRGVDLLDSTPRQIWLQQRLGLPTPSYAHLPVVTNAAGEKLSKQTRAAAVDASASNALLSAALDFLGQTVPAKVRAGSLSDLWRWAIAAWSVERVPALRGVFPGQ... | 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 an... |
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-galac... |
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 | MLNWIPTKLFSSKAARDSRSLRRFVADVTEREKRFANFTTEDCQHQTSVWQSEVQALDPDRLDVIDRHLKLIAPDAFALVRQASRLLAERDPEWKLIPFDVQIAGGNVLFQGNISEMATGEGKTLTAVAPAYLRALAGRGVHMITVNDYLAARDAEWMGKLFATLGLTTGCLQNDQSPDQRRAMYAFDITYGTSSEFGFDYLRDNGLARSAGTQVQRGHYFAIVDEVDSVLIDEARTPMIITTIGNTRSSFLPIYVSSVARLVKEQASHCNKMIQEARDLYGDGSHRDTDAAVGMLLYKCRLAQPLHPGLRRMKQDPALL... | 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 c... |
Q4JVE2 | MSNPETLSAKETEAVEAVESTELSAAEANPVDAPDSEAQGFFEKLYNGNGGFRIVQNRGRLYGILVAVVVACLLSILVRGFTLGIDFEGGTRMTMPPAGGATESSVSEIFENATGIAPQSTQTVGSGDAESIEITSERLSEEQIREARSALFNEYHPKNNVGEVTQDAISDSTVSESWGSSITKKMLIALGVFLLTVFLYIAFRMERDMAAAAIICLLIDLTVVSGIYALVGFEVSPATVIGLLTILAYSLYDTVVVFDKVHENTAGLFGSTRATYAEETNLAINQTIMRSINTSIFSLVPIASLLVVAVGIMGVGTLKD... | 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... |
A0A0D6JFF0 | MTATPKAAQASINVTHTSVLAIALPIIASNVSTPLIGLVDTAVVGQLPAPHYIGAVALSSTIFTFLYWAFGFLRMGTTGLTAQADGAGDSVEVGAALGRALLIAAVAGSALILLQAPLSWFAFLMVEGSKAVEGEAHNYFAIRIWSAPAALANYALLGWFIGLGRARIALLLQVLLNGLNAILDAWFVLGLGWNVAGVALGTVIAEIAAAVVGLVIATRVLARIGGFPDFTAVLAPEHLRRAIAVNTDIMIRTLCLLTAFTWFVFQSAASGDVVLAANAVLMQFVSFMAYFLDGFAFAAESLVGRAIGARNRSQFDAAVR... | 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... |
A0A832JKV4 | MGSELFRSFEGNYHLMGVGGAGVSALALLLKGWGFEVSGCDVDVEDGYADAVRRRGVRVYRGHSPEHLVLERCDRVVFSKAVDRSNEELVAAIRMGLSVESRSSFLGRVFNAMRSIGVSGTHGKTTTTSMVAFALKGLGFDLTALVGGEVPSWGANVLLGDSDLLVCEVDESDRQMAEYSPYISVLTNLELDHADVYRDVGQIYEVFLSYVMNSKRGGALVYWGDDPLLSRLAGEVSRARSDLALLDYALGSRARLGAVGIRQEGRSALFTLLADGSPVGEVRLGVPGEHNVLNALAAMAVVAAMGLPLSSALGSLEGFR... | 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 | MESTNKEYGAEQIQVLEGLEPVRKRPGMYIGSTDARGLHHLVYEVVDNSIDEALAGYCTGIEVYLRSDSSVRVVDNGRGIPVEILPKYNKSALEVVMTKLHAGGKFDNNAYKVSGGLHGVGVSVVNALSEWLEVEVKRDGKLYKQRYEQGGPTRDVVLIGDAQGTGTTVTFKPDKTIFETLQFDIDVIAGRLRELAFLNKGLKIAIKDEFSQKEQVFQYEGGIISFVEFLNKNKNVLHEKPIYFQKQKDTTIVEISMQYNDSYIENIYAFANNINTHEGGTHLIGFKAALTRVTNDYAKSKAMLKGDDKLSGEDVREGLT... | 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 modu... |
A0A0L7R5I7 | MPKCNTKARYLPATLAWTVLLSTTALFFCFPCQYYVFRWGTWVPVLQGVIIFFVLANFTLATFMDPGFIPKALPDEDQEKSYPAPIYTSVQINGITVRMKWCGTCKFYRPPRCSHCSICNHCIETFDHHCPWVNNCIGRRNYRFFFFFLLSLSFHMLSVFGLCLYFVLERKQQLGEVDTIVALVLMGVVAILIIPIFGLTCFHIVLISRGRTTNEQVTAKFPDGVNPFSHGCLHNCCYTQFAPQYPSLIKPEKYSGKRRGMSTSEISTIGSENQVKTYMDSSNGVRNASSNAYNKLSPGRDGSDTDMEPTASQSADCEPT... | 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 | MTDSRQVVLKALSLLNTGRNLPDALSQAGISKLSPRDRAFARRLAVHAVRHRRRLEQQIQAYLQRPTKDRGVLDLLWLGAAQIDLADVATHAAVNSTVEVAPKRLRGLVNAILRRRLREAPAAPQGLAEQHSFPGWMVARITRDWGDRAGEILDQLNQDPALCLRINRQKSSRAQWLTALSDDSAQSLGSDVVQSDGVVLAQSRELAELPGYADGGLSVQGPSAQAAAHLMQLQSGQRVLDACAAPGGKTAHMLELCPDIVCTALDIEPARVARIEDNLKRLGLQARCMSGDMLEPGDWAGEYDRVLLDVPCSGTGVIAR... | 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... |
A0A7W2H3C4 | MPPWGFWPLAFIAFAMLDQILKETHGATSRFFTGFGFAVGWLFPGTFWMIALTVPGYFIQGFLFSGLFALSTSLIPTSIHRLVALPAAFTLIEAVRYRWPFGGVPLATIAMSQSDSPFGQTARVLGPLFLTAFVIICGMAFAMIWERKWRHTGLIVSVLLIIWGFSTIAPKGSVTSTIDVAIVQGGGEQGTRAINTNEREVFERHVEATGLIQGNPDIVLWPEDVVNVRQLLIDSPEFSELQQLSRNLNSWLIAGIFERTSITSNANASIVFGPDGRVYDRYDKVRLVPFGEYVPLRSLIEPFAPEYLPVRDTQPGSGKP... | 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-[lipopr... |
A0A9E3YCU8 | MQSTGALGAVLMLVAPTDNVLEHVAGAGPMNDAPSIADLDINSSNDWFTQTFRSGQALFVDDTAGWEPKSAVTERALERGVTACWTTPLVTVEGDIIGTFSVGWPDAVEPGDDQLWLFQEFALLAQAVVDRQQSHWQRMALIAHERERIAGELHDDSVQAMTAVSLRLQRLQARLAEHELRQSVVELRHQVDEAIERLRHMLFSLSSPTLEQDGLVITLEIYLETYVEKAGLAWELHGDEALRLPHDVEALAFRLARGALINAIKHARATKVSVSVDRSDDGGLAVVIADDGIGFETGEITAKDKPGHVGLTYAQSLARA... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
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 is... |
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 | MAPRSVHPLPPGSTIGIMGGGQLGRMTALAAARLGYKSHIFSPEDDSPGIQVSAAATIADYQDRTALQSFAEAVDVVTFEFENVPADSAAFLADHALVRPGPQCLAIAQDRLLEKEFINKTAPTTPYRRVTSAEDLAKAADEIGRPAVLKTSRMGYYGKGQVLIAPDCDYAAAWAEMGAEIGILEAFVDLDCEISVITARSPHGGWATYPAVENRHVNHILDTTMAPARLPDGLADQAVAIAHDLAEALDLVGLLAVEMFVTRDQRILVNEMAPRPHNSGHWTMDACATSQFEQLVRAVCGLPLGSVDCHHDAVMKNLIG... | 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-carboxyaminoimid... |
A0A2M7JD99 | MSNLITFDSSTIPEIQTDTLIIGMGIAGLSAGIQAAKYGKVLIVAKTSFHESNTEHAQGGVAVVLADEDTMESHVADTLITGCGLCNNKNVKILVEEGPQRIRELIDWGVKFDKNQGKLSFGQEGGHSLKRVIHANGDATGKEILRGLLAKAKANPNITLMRDVFVIDLLVKERVCVGAIIHAPLEALRVILAKNTILATGGTGQIYRETTNSKIATGDGIALAFRAGAVLSDMEFIQFHPTTLYVAGASRFLISEAVRGEGGILRNKNGGRFSFKYHPSGELAPRDIVSRGIWAELKETNSVFVWLDVTHLDFEYLKKR... | 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... |
A0A663F862 | MANDSPAKSLVDIDLSSLRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKKSPPGHDDQLWLVMEFCGAGSITDLVKNTKGNTLKEDWIAYISREILRGLAHLHAHHVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDLWSCGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKKWSKKFFSFIEGCLVKNYMQRPSTEQLLKHPFIRDQPNERQVRIQLKDHIDRTRKKRGEKDETE... | 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
S... |
A0A931ECY5 | MARGKLRLYLGAAPGVGKTYAMLNEGWRRKERGTDVVVGWVQEHGRPQTDAQVRDLEVFPRRVAEYRGQTLEEMDVDGLLTRKPELVLVDELAHSNAPGSKHAKRWQDVEELLDAGINVISTVNLQHLESLNDVVEQITGVTQQETVPDPVVRAADQIELVDMAPEALRRRLAHGNVYPPERIDAALGNYFRTGNLTALRELALLWVADRVDEELNDYRERHNISGPWQTKERVVVSLTGSRGSAILIRRAARMAMRTKAELVGVHVRTDDSLTGRGSQGLVDNRALLDALGGRYVEVVGSDVAPSLVQVARAENATQLV... | 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 | MPSNHLPPDDPASTGSSDASAAPRPSSFASNRAARLVADIGGTRARFALLDEQGAPQQVQILAVADFAGPVEAIEAYLDEVGCNGLQAAAIALAAPVDEQEIRLTNAAWTFARSEMKSRLGLARLLLLNDFTALALALPHLAASELRQVGGGKGVALAARAVLGPGTGLGVSGVVFDRGRWLALAGEGGHCSLAPADGRESAILALAWRELQHVSAERLLSGSGLPLLHRLVAEVDGRACVALTPAEIVAQALANDDVQCRAVIDTFCAMLGSMAGNLALTLGARGGVYIGGGIIPRLGELFDRSPFRARFETKGRFAAY... | 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 | MIDFTAMILTVGPELWLVAIALIGVLVGATLKDRFNSVSIKFGALALFAAAAFSLMNYEGGEAFNGLVRTNTFVNFAKFVSYVLAGFALLTSEGFLKRHGTIRYEYSLLILLASFGMGMILSAADLMTLYMGVETLSLSSYVLAAFHRDSAKASEAGLKYFVLGALASGMLLYGASLVYGFSGSTEYAVIAAADPSIGMMFGMVLMIVGLAFKVSAAPMHIWTPDVYEGAPTPVVAFFASAPKMASMVVFANVMFTMFGDVIDQWQLIICIIAGLSMIVGSLGALTQTNIKRLLGYSSIANMGYALVAVAAGPELGAGPL... | 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 ... |
A0A059E3Z4 | MSTDSPDQSAQEPTLVESRNRTSRRPGKWRISNIIDGRALRVKLTAAALDNIGDAQAMRKAALDHLHGAMFRGRMIAQERLQQGAEGLDTARLLSAVQDEVIHALYDFTTTHVHRARNPTEAERLAIVATGGYGRGVMAPSSDTDLLFLRAYKASPHTESVIEYMLYALWDMGLKVGNAFRTPAECVKSAAEDVTIKTSLLDARFMCGDQALFDEMQAKFKKDAVEGKDAEFIADKLAERDARHARQGDARYVVEPNIKEGKGGLRDLQTLYWIVKHIYGGRTLEDVMKGGPFTRSEYGSFIRSAKFLWTVRCHLHFVTG... | 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 ... |
A0A0G0ARU8 | MGNIKLENSNPKNLLKTNNIKLENAGSIHKFTVKPEEENLRIDTFITNQFKSYSRSFFEKLIELELVKINNKIINKKSWPIKENDIIELQFPEEKNRDQELNKLKDLEINIVYQNQHFAILNKPANLAAHPSNNNTETITLVDWIIANIEQISNVGFDSRPGIVHRLDKDTTGLMIIPKNNCSHAYFADLFKKRKIEKSYLAIVHGHPEKTGEIDIEIARHPREKTKMTHVTSSNIAKIKGKSRNAKTMYEVLEYYDGYALVLAKPLTGRTHQIRVHFCSIGHPLLGDAVYGKSSKIMARHALHAFQLEFEFEDKKMKFE... | 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 | MASNCFKKPVVLVVLDGFGHSNEHSYNAVYAANKPNIDKWLRQYPNTLLHASGQYVGLLPGCIGNSEVGHFTIGCGRVIKQPLVVISEAINDGCFFENKVLLEGLEKVKNATGSLHIIGLLSDGCVHSDIEHLYAFLLEAKEQGIKNVYIHAFLDGRDVGPKTAGKYLTDLNNFMKKNNIGVLASIHGRFYAMDRDKNWDRTEKTYKVLVGDAENSFNSVFNDKNIDLNWESILNSSYAKNVTDEFIFPVNILPEGQGVIKNGDGVIFFNFRPDRVKQITKCLLGQKNDVFEVRNIGLSCFVTPVEYGKDLETDVMFKHS... | 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
Sequ... |
A0A2D7A673 | MKAPEFWKSGSSSMLPSVLAPLSLLYQLGANLYRSNTIPGLKTSAPVICIGNITAGGTGKTPVAIDLGKRIKKIGAKPHFLTRGYGGKTIGPLRVEKCHKAAEMGDEPLLLSRLADTWCSRNRAEAAKMAVKRGAEVLIMDDGLQHTSLHKDFSFLVVDGGFGLGNGRLLPAGPLRETLQAALPRINAVICLGEDVTNILREIPAHIPTLTAVIEAGTAADGLVPQVEPHKVTKVSYLAFTGIGRPEKFYETLIKAGANLADTVSFPDHHPYTTNEILNLKQKAKQLNARLITTEKDIVRLDSKERDDIVSLAMRLRWDD... | 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 te... |
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 provi... |
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 | MKLAGALVAGGRSTRMGSDKAFLDWNGRPLYVTQLEKLHSIATPGRLLLSARRGQAFPDYLTDVTLVWDTSDDLGPIGALRDCLKRLAPDENLLFLAVDLPRMSESFLDRLRHLADETGSGIVPKVEDQWEPLAAIYPHAILPLVDDQIERGELSLQRLCDRAEAEGWIAACPVPANEIANFANVNTREEFDLIQQGQFDHPTLLNRFSLEKGFVETHDRLAAEEPLEIRVEEKSVAVVMRTPGHDDELAAGFLLTEGVIRSSADLFEIRRCRDIAEPHLSGNVIAVQLAPNHEADLEKLTRHVFTSSSCGVCGKATIES... | 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: Cytoplas... |
A0A927X4M4 | MAKVFALAGNPNSGKTTLFNSLTGATAKTGNWPGVTVEKKTGKYREDTIVDLPGIYSLSPYSPEEIVSRNFVLKENVDCVINIVDGTNLERNLYLTLQLLETDVPVVVALNMADILNKKGVEIDVDKLSMKLGVPVMAISALKKNGLDDLIALATKAANDGRAGKTVLRSKELADVAAMLDKHKYFNAAKLIENDELICSEYESLKESVNSIRAKDATSYAEDFANERYSYISNEIIKNVVVKAKDVSNRTEKVDKVLTHRIWGLPIFLLIMFSVFHLTFSEDFLFLSALGIIPEGAFDIPIIGDSAIASPGIILFNIMD... | 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 | MNDLAQGSPPSPGSVTHVRVGLLGCGHVGAALAVLVAERRAEVGRRRGLDLEVTRIAVRNTAIDRDVPVADGAFTTDAAAVVCDPDVDVVVEVMGGVEPARELVSAALSAGKPVVTANKELLANHGAELYALAAASGVDLLFEAAVAGAIPIMRPLRESLAGEPIQRVMGIVNGTTNFILTRMADDGASYADALAEAQSLGYAERDPTADVEGYDAGAKAAIMATIAFGARVVAGDVYHEGISGISVADIEFAADLKHCIKLLAVAEQTVADDGEAQIGVRVHPTLVPLDHPLASVNGSFNAVFLEGGAAGDLMLYGRGA... | 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 | MNLIIGLIAFLFMLSVIVIIHELGHFAMAKKFGVFCKEFSIGMGPALWQKEGKETTFSIRAIPFGGYVMMAGEQDGSQDESEDDWLKDVPAARRLNNIAPWKQIVIMLAGVTMNIVLAYALFTGLAMARGYVVEDAKPVVYEVVENSPAAKAGLQKDDEIIRVTNGSESIEPQRQFDVIEFIQYNPTESTYTIARGNETLDVKITPRYNKDTQTYEIGSIATSYARPIAWYEAFKVGWDDMVDSGSSIFRSLGQLVKGKGYENLSGPVGILNLTKKTTEMGWMSYLSLFALISLNIGIFNLLPIPALDGGRVLILLIERI... | 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 | MPDTIAAISTPLGEGGIGIVRISGKNALSIADKVFRSPQEKKPSKFESHKLHYGHIIDSEGRIIDEVLLSVMFADRSYTREDSVEINCHSGIVVLRKILDLVIENGARLAEPGEFTKRAFLNGRIDLSQAEAVLGIIEAKTEAGLRAAIGQLEGHLAVKIKEIREALLDIRTQIEAEIDFPEEDIPFVAPEEVLKKAERAKTEIEKVLEKAGQGIILRKGILTAICGKPNVGKSSLFNALLKKDRAIVTPVPGTTRDTVEEVIDLKGIPFYLVDTAGIRESENLVEKEGIIRSQNSLKRADIVLFIIDGSRDIEKEDKQI... | 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
S... |
F0SBY0 | MATIKASVPKGTRDFGPIETQKRNYIYNTIKSVFRKYGYQEIQTPTMENLDTLTGKYGEEGDKLIFKILNSGDFYEKASAKKTAEGDFSSKSILPLISEKALRYDLTVPFARFVVMHQNEITFPFKRFQIQPVWRADRPQKGRYREFYQCDVDVVGSDSLLNEAEFICIYDEALSKLGLKDFSIKINNRKILTGIAELIGKPNQIVDMTVAIDKLDKIGLDGVEKELLSKGFTGADLEILKPVILLNGSNNEKLAQLKMVLKDSLNGLKGIEEIETVFSYLAGFDIKTAKVELDLTLARGLNYYTGCIFEVKTNEVAMGS... | 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 | MEDFMKIETKNIVASKYEVNVVMEGTEWTTEVDKAFNKLAKNVSVPGFRNGKAPKEMIKKHLSQQKVYSEAIDSAMQIAYQKALEESKLQPIIRPSVEVKDFAEDHFEVTFVVTIAPTVTLGQYKDITVQKEEVSVSEEELSRALKNVQERNAELTMVTDRAVEKNDIVNIDFTGYVDGKEFEGGKAKGYSLTIGSNTFIAGFEDQIIGMRTGEEKDIFVVFPENYVPDLAGKNATFKIKLNDIRVKVLPELDDSLALDADIENVSTLEELKNHLTADIKKSKQQQQDSKQFQDLLNKIVEGATVEVADTLVNAQIDYKV... | 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
... |
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 | MSEEKKDSELKPEEAAKTNEIPSADEKKEADSSAAISRDDAQKQSPDKPSSTAPSEASTGASEAENVQSPASGDEAPAAAAKPANSDSAKPDGDAAPAASSADAEKEAKIKAAAEAREARARERAAKAAEAGEGGAEAAAPAASGGDADAEKEAKIKAAAEAREARARERAARAAEAGEGGAEAAPPAASGGDADAEKEAKVKAAAEARAARARERAAKTGEGADAAPAAPKEPSPKQPVLDRLVQLLKDHVAEDAVEEASINERGGHRPTIVVKGDHWPAAAELLKSSPELDLNYLRNLSGVDMETHLEVVYHLISLNS... | 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 hydrog... |
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 | ERVRRALPEAAPVRFACELKIDGAAVNCVYRGGTLEVGATRGTGEVGEAITQQLLAIAKVPYRLSDEDPPALVEVRGEVYYPLAAFEQMNAERIERGEATFANPRNAASGTLRQKDPTRVAGRPLALFVHSLGRVEGRSFVSHESFLDWALVAGLPVASSTVFVDDIDDVWRAIERFTIERHSYGFEVDGVVVKVDDLAQRSVLGATPRAPRWAIAYKMPPVEQQTKLRAIEVNVGRTGKVTPFAVLEPVAVAGVTITRATLHNEAQIHLKDVRIGDTVVVRRAGDVIPEIVGAVVSERPPGAVPWTMPARCPFCGEPLV... | 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(+) + (deo... |
A0A2C5Z5D3 | MAPSKSAFDSKVILQTGSPRGRDLSIKLSRPSQTSSEAWFNKTQPLLDVLSPTPQETDDDYRRVKIAVIDTGISPDHPLINDFIVKNFVETPNGRVRDDPKHGTDSIDLILTMLDTAKIYVARVFQAKEGDQLTPGYMAEVSRLPSGSLLYVDIISISAGFEHSHAKLAEAIRRASAADPEILIFAAAANWANTQSVAYPARLTGQVFCMFSTNGALRNSRDFNPNALDNADNFALLGQDVKLNPLSREGLSGTSIATAVAAGLAGRIIDFTRHADSRGHLTQQHRNKVASKLGLREIFHFMSQDHKDLEYRCVAPWELL... | 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-diacy... |
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 ... |
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... |
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 | MYFCVNDLQNNECKEYFTEPQIVGTYCFDGNRCYHSDLSQLKYYKEPRNLNNVDFNLDDNLNTIQKLDNINKKIDYLLKWISENFNHLQMERSKNRRWLEPEFVCYRGVLSNLLATPFDSRDGWIICASKFKGTIYLCGFDTDKKKRYEINKNEFHKRCTSWGYKFEQYLVSDSPSENPDLSKPLNQNEEFCCVFKSRLGNNILLYGAEVDAVCSEHPIQDTLIGKKVELVEMKTMHHNALNLYKNSIASYRAHRTLKWWVQSYLVGIDKIICGLRDNNGIVHSIQKFNLNKLVKDSKHDWNPEGCTSFCTGLLERMKAV... | 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 | MGKSLVIVESPAKAKTINKYLGKDFIVKSSVGHVRDLPTAGQSSGAKAKPVSTKGLSAEEKARIKKEKDRKSLIKKMGIDPYHGWEANYQILPGKEKVVSELQKLAKNADHVYLATDLDREGEAIAWHLREIIGGDEERYKRVVFNEITKNAIQQAFESPGELNMDGVNAQQARRFMDRVVGFMVSPLLWKKVARGLSAGRVQSVAVKLVVEREREIKAFIPEEYWDIHADTVTKAASDFRLMVAQRSGEAFKPQNEAETKAAMSILEKAEYEVCKREDRPTKSKPSAPYITSTLQQAASTRLGYGVKKTMMLAQRLYEA... | 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 ... |
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 Le... |
A0A960F6M7 | MSGFSNAYRNNTNVNFPRMWPRAALVIGALLLISVVALLVRGLNLGIEFEGGAAWEVDAHGVSTAEARDALRPLGLADARIQTGDDILRVRAELDQSDQKVDEVSQALSDLTGTPLDEVNQTVVGASWGDEITKKAVRALIVFFIVIAIYITLKLEWAMAVAALFAVANDIVVTVGIYALFQFEVTSATVIAFLTIMGYSLYDTIVVFDKVKDNEGRLAATGKLSYPGLMNMSLNQVLMRGVNTTVTSILPVLSLLLVGSLILGAVTLQEFGIALLIGLLSGALSSFFIAAPVTVWLKERFDSRYAEARERAVARAGGTK... | 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... |
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 M... |
A0A2C5Z5J7 | MPPRRWARRLERACCTLGTYVPVAFVYGMTTWAVWVVIVIGGAEPVSRWRGTPSSVVGLALYLLLNWSYTTAVFTSPGSTTTDDGYGLLPTAAARPSASSLTVKSSNGQVRFCKKCQARKPDRAHHCSSCRRCILKMDHHCPWLATCIGLRNHKAFLLFLIYTTVFSLYAFALSGSWLWSEVVVESARYVDSLMPVNFIVLAVVSGIIGLVVGGFTAWHVLLACRGQTTIECLEKTRYLSPLRRMHQQQALPPPAQRLVDMHANALPGVTRPEEGESSVAMVASADGGCDDDDAEVDVEAGALFAGRRPVSYADRERQQT... | 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 | MTIKDHIKHRFAAIYNTPPVAVYFSPGRVNLIGEHIDYHGGLVLPVALSIGTYGAYSLRDDDEVRLYSTGYSDYPITINLGDLSKDSFTGWANYVRGVFQVLKDEGYHVPHGLNLYLESDMPTSGGLSSSSSLELLIIKMLNDIFNFGIDRTKMAVLGKKVENEYIGVLTGIMDQFVIANGKKNNALLLNTNTLKFDYIPLDLKDYQLVIVNTNKRRGLADSKYNERWNETMGALKTLKNHFKINNLTELKSSDLPQIEKLLDPLLFRRVRHIITEQERTLESAMLLKEGKIEEFAKLLTASHNSLRDDYEVTGLELDTI... | 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
Sequ... |
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)-dimethylall... |
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 Topo... |
A0A7Y2DNZ0 | MSRPIDLTTKPSIHVIGCGGTGMAPITAVLAHLGLSVSGSDQRPSATLDALSDLGVRVTVGAGYDDIDDEAVLVRSTAVPDDHPEVAAALLTGRPVHRRADVLAAITDIHRTVAVAGTHGKTTTSSMVTAALAGAGVDISSIVGGKILGLDQPVPGAVLGEPGGVLVVEADESDATFVELVAEVAVVTNIEPDHLEHYGGEAGLLSAFDTFLTNDGLRAAVVCADDPGVGAALDRTQADRSRLVTYGQVAGCDVGLHFDPPAATVRIDGFERRLEPRLPGLHNALNLTAAFAVAAALDLDLESAAAALDRFEGVGRRFER... | 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 | MDSFMLGDEGVRDRIRQAEEFLDPNDPQVRSYRSDIILMLQKNERRLTVNLDHVRNHNAELAQGLLEQPFDYTLAFDQALKNIVQALPQARPDQSAKDTVYYCAWAGSFGLNACNPRTLSSHLLNYMVSIEGIVTRCSLIRPKVVKSVHYNETKDRFHFREYQDQTMTNGVTTSSVYPREDDDGNPLITEYGFCTYRDHQTISIQEMPERAPAGQLPRGVDAILDDDLVDRVKPGDRVQLVGIYRTLGNRNTNHNSALFKTMILTNNVVLLSSKSGGGVATATITDTDIRNINKVAKKKNLLELLSQSLAPSIYGHDYVK... | 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 tha... |
A0A960T0Y0 | FYLAVILHDTGRAENVREHTDGSAILAARLCNRLQIQGARRRLIMFLVDNHLTFWRTATSRNLDDPEVIAEFAAIVKTPANLDALLLFTYIDSNGTAPDAWNGWKESLMLQLHTATHAFLDSGREQYEKKLNADRLALRKEVTGLMREDYHADVRKHFDRMPAAAFHFRQAAHIVTQVRTVRHFLQRESENKDGIAFNVKWIDHPDRGNTEMVIVTRDRPLLLEKICCALASEQINILSADFFTRSDGVVVNIFRICTTNFEPVSSAETRKRFLQTFDKILHAEKFEPEKYLKRRANFLKARNDHDIPVPVRAYVSNELH... | 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 ... |
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 ... |
A0A345DBE8 | MPTAAPSHALDRTRYQAGRSMLFSQFTANNSPTRAVRRLMRELTHLTDLCVLEAWAHCIGTLPDNLRHSSSLIAIGGYGRAELLPNSDIDLLVLIKTDHLPAESKAQLSLAIEQWVSMLWDMGVTLSHSVRTIDECIADALEDLSIQTSILEGRYLAGDKKIHQTFYAAFNRHFDLLTFWREKMAEMRQRHSKFDDTPYSLEPNCKESPGGLRDLHLMLWLAKAANIGQTWQELHHNNWLTASQLRLIQRSENQLLAIRAHLHILSKRMENRVLFDLQTPLAHAFGLFETDGKRAGEHLMQRYYLAARAIYQQCALFVQK... | 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 ... |
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 canonica... |
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 Le... |
A0A9D9DIN4 | MYSVLKGTHDVILDEARKYSYVEAVLIKVAELYNYKEFRTPIIESSDLFTRSVGESSDIVRKEMYTFLDKGNRLITLRPEFTAGIVRSMVNNKLFANMDLPVKAYYVGPNFRYERPQQGRYRQFNQFGIESCGVDNFYRDIEVISLGYNALQMLGFKDVKLKINTLGDDETRENYKGALKAYFSDKINLMCDDCKERFEKNILRILDCKVPSDIEIVKEAPKINEFLSENAKNNFQNITKALKEMDIPFEIDTNLVRGLDYYTGVVFEYQYSSSKNKNYGALGGGGHYGKLIKEIGGPDLEGVGLAFGIERLVSIMNDDE... | 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 | MIYRPAKAYINLSSLAHNLRLIKQLAPNSKVLAVIKANGYGHGICRVAQQLSNADGFAVASLDEALLLRQKGFLHRILLLEGLFTAAELPQVLHNRLDLVIHSQYQLEWLLAHRHSVALNVWIKIDTGMHRLGFHPDAVQSVVQSLMESDNSYQLNFMSHFASADELQVHSQAFTQQQIECFKTHCQAWDYKCSLANSAGILHYPESHLDWVRPGILLYGAGVPIKPRHPFKPVMRLESQVIALKWIPAGDFVGYGNRWQAKKDTYVGVIAIGYGDGYPRHAKDGTPVVVNGERVPLIGRVSMDMITVDLSHQVDKVKVG... | 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-, ... |
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.-
... |
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 | MLLPVQQFKDFVNSYTLFMPQDKILLAVSGGKDSVTMAHLFASAGFKFGIAHCNFNLRGEESIRDQNFVKNLADQLGVSFHLQAFETEAYAKEYKLSIQMAARDLRYEFFYSLKESFGYQKIAIAQHQNDAMETVLLNLIRGTGIAGLHGIKVQHHDIIRPLLCFNSADIEEMVEENNISFVEDSSNASTKYARNKIRLNVIPEMKQLNPSLEDTFQKNLDYFSELEELLIETVKNHQAHLFKFKDQHIEIAINDLKKVHPQKLILFELFRPFGFNITTIQNLINCLNGESGRKFFSDTHCITVDRETLTLKTKAQFILR... | 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)... |
A0A059EDJ2 | MDEFWRNTVDQAQAYGPQLIKAALVMIAFIIGAFIVRWLIAAAIDRTGLAKKANASTATSDSKSLGTSLAQAAFWVTILIGLMQALAIAGATQISSALHGVIDPILSYLPNVIGAALIFGIFIIIANVVRETLKAVLVFGDGMPERFGLATGRVNISGIVASVAFAVLVIIGAIMAFDVLAIEAISAPANELLTDIIGIIPNVLAAGVILAIFVLIGRFVANLVLKTLPGTGVDSAVSELGLLKGADGGLTASTVIARVAMFLIVLLGLVAALNALGIESLTYAMNVVLDMGVQIIFGALIIFAGVFIAKLVSSAMDSTG... | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
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