ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A8T3Q5E8 | MLLTPVWKNPACISRLELAPAVWSWLVYSGSFTKKILALKGAEARFNIKILGEQLELAKKSSYEFSIFNCHYVYSREIQIFLDDYLLMYARSVMPQNVAPFYKRQFRGLGARPLAEMLFSAFPLQRSPFEIAKIHPMQREYVLANEANVSSPRFLWARRSVFSAAQDLLLLTEIFSPSLIELISNCETPIHK | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
EC: 4.1.3.40
Subcellular Location: Cytopl... |
A0A962RUQ6 | MPKRLLVSLSVVLLAACSTPRMPSLSSLPSPRDLPFIYKIDIQQGNVIDQNMLAQLRAGMDKKKVLFIMGSPIIQDTFHADRWDYVYTNEPGGGQPERRQITLYFEDDKLARIGGDVKPAESPLVATLHQDTTIKVPQLRKKGFVEKVKDKIPFVEPTPEEVVEVDVDEAAAEHAGEDTEPEENVNLPTLAEDTPPPRSPYADLQAAPGEGVIVPPDAPTNRKKKGFFARIADSIGIGADDEEIGDEDDDYDPGDPKYRDITDQSNL | Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 267
Sequence Mass (Da): 29475
Location Topology: Lipid-anchor
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A0A6L7VIY8 | MTICVFGAGAIGCWLAARLQRAGLRPSLVARGDHLRALRTSGLRITEDGHTETLQVNARGVEDDLPPQDLIIVTLKAHSITSALDHLTSLCHDETVLVFGVNGIPWWFFHGMDGPFAERTIASVDPGNQIWEAIKPQRAIGCVLYPAAELLAPGEVQHVSGNRISLGEPSGKMSARVEEVMNVLLSADIRASVRRDIRNEIWIKLWGNVAFNPLSVLTGATLDHLATNPGTNAIARRLMEETQTIGASYGARFGMTIDKRLQGAAAVGPHKTSMLQDYLHGKPLESSAMLDGVLELGELAQIEAPTIRMMQAMLAMKLAS... | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 327
Sequence Mass (Da): 35459
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A0A2E0MZA0 | KLLVQSRADYGFFGEKDFQQLLIVKKLVNSLDIPCKIISMSTVRDREGLAISSRNRYLKKDKKLIANNLYKILCESSKNIATGKNIELVIDKAKINILESGFTKIDYLEIRSEKDLSEIKTHSNKKSRIFVAAYINDIRLIDNIAIE | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
EC: 6.3.2.1
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Length: 147
Sequence Mass (Da): 16837
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A0A8T7C2B9 | MNIVDTVNSWIITLSNFLGPNPLLQASIILFLFIIVAWVVTTLLSRIVGRFTKASKTDFDDKLVHMLHRPVFMTIFLVGATLALGRLELSEVAEARSVSVLQSISVWVWMVFALGFSRLVLTTLNSFSNRFNFVDNRTLPLLQNAAFLLISLGAVYGLMSAWHIDVTALVASAGILGLALSFAAKDTLANVFAGVSILADSPYKVGDFIVLGTGERGQVTQIGVRSTRILTRDDVEITVPNAVIGNAKIINETGGPHEKYRIRCKVSVSYRSDLDAVCAILKEVALNQTGVCVSPAPRVRVRTFGDHGIDIELLAWVPQP... | 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... |
A0A928UPF1 | MTKISLSRRSYFSAAHRYYNKQWTEEINKKVFGLCYSEKGHGHNYILDTFVSGPVNKDTGMIINLIDLDALLKNFVNILDHKHLNFDLPYFKTIIPTTENIAGFCFKEIKTLLKDNALSIQLEQIRLYENQDLWVDIINE | Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 140
Sequence Mass (Da): 16389
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A0A952NM97 | MTETRGFRLRFSCAHLYHQPSWDEAQNQRTFGKCFSDHGHGHDYELWIETPLAGASFEKLREAGAELREHLDHKHLNFTIPEFKTQVPTTENLALYCREFLTKKMGEPVFLKLTLFECPWLGATL | Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 125
Sequence Mass (Da): 14598
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A0A2E6YAJ6 | MPIIAHPKLPSLSKLKTEDLVIADASSLAKDINQELHIGLLNLMPDAALQATERQFIRMLGSDENILVHVYPTTVGSSKRGEEFQDYIAKNYNDISTIYASKLDGLIISGTNPSKPDMTEEPFWAPLVEVMDWAMENTNSILCSCLATHALLKYYFNIDRELRGQKSWGVFPHTVANSSNPLIAGLDDSFMGLHSHFYDLPLKKIQDTDLEILAYNSQAGFFLASTTDTKLVLYQGHPEYDAISLLKEYQREITNFLSGLRPDYPPLPENYFSKAAISVLENFQKKVLLTKEQSNFPEARLSELVKVEWRHPGKILYKNW... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-succinyl-L-homoserine from L-homoserine: step 1/1.
Function: Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine.
Catalytic Activity: L-homoserine + succinyl-CoA = CoA + O-succinyl-L-homoserine
EC:... |
A0A0X3P0S7 | MTFVVMSSHVLEFTLEPSVELFPTIKFSLVEFAEIRSIMNGVRLAAFRFLRGSPCLLTRSVTTVVPPEIQKYHPHIGNREIVGYGRNGNPQYLDDPHYPYPSIRFCPQTDEIEVLQAKEKGDWHQLSIDEMKNLYRHSFRMTFAEVQAPHPRYKLAVAWALFVMSGAMLYFCFIKSVVLNLPSCSYAKKEYKDALLYRRLYSRDGPIDGLVSSFDFENMRWK | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 222
Sequence Mass (Da): 25804
Location Topolog... |
A0A0X3NS45 | MRKCKILVLFAALAISCILLRTCLSMYETQNIQTTSHEMTEVVSETTQQPVCGQPNYVGRLNICLKYLDYGDLATKWGLSNDQTIWQNDSNFTDVAYNLERSGRDESPTAVAVWTPANCEQSETLAIVIPFRDRYQNLSVFLNHMHPFLRHQRRRYSIYVIDQIAPHTFNRAALFNIGFLEASRRANYSCFMFHDVDLLPEDDRHLYACEDQPLHMSATINKFNYKLFYNSSFGGAVAMRKEHFEKTLGFANTYFGWGCEDDDMSRRLRFAGLKLTRHNFTFARYTMLKHGKEMGNPENPKRKLRLSKARIMWEKDTYLD... | Pathway: Protein modification; protein glycosylation.
Function: Catalyses the transfer of galactose onto proteins or lipids.
EC: 2.4.1.-
Subcellular Location: Membrane
Sequence Length: 363
Sequence Mass (Da): 42598
Location Topology: Single-pass type II membrane protein
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A0A2D5T6Q7 | MMDPDEALKRLCKGNKRFLSGEVSKEVSANRKQHLDQASGQKPFAIILACSDSRVPVELIFDCGIGDLFVIRVAGNIASSTQIGSIEYAVTVLGTRLIVVLGHSNCGAVIATIDEITKPNSHTSPNLRSIIDNIRPALELELENNFGDKSCLTIEKCVQTNIKASVTSLENKSTILKELIAENKINVVGAEYSLETGSIKFISND | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 205
Sequence Mass (Da): 22189
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A0A8H6YYM0 | MSIPSFPLAQQAQIIRANQRDLYHVTSLKDQVETVLRAWLGTRWLSRWDKEVDLLVKLGYYGLTTARATQTLGEEYTDIWQYSAFQAFCSSVAIDTRRSSSPSNSSRFPRHRKILTYDRLRIPLLGILIGVRLLHRLVTFLRRNMGAGSTVKGKQQESSNTEETFLDERLVSGLIGQADPESELAKPAEEDERTMLDIPSIPDALRAGRNCTLCLEERTDSCATECGHLFCWSCIVGWGREKAECPLCRQSLSLTRLLPIYNL | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 263
Sequence Mass (Da): 29842
Location Topology: Multi-pass membrane protein
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A0A8T3RXR1 | MVKPNFLNELADKLSQLIPPQLANLTNAPNLEAAKAEIERNVRSLLQASFQKLDLVTREEFDIQRQVLEKTRAELNKLEARIAELENQR | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Required for efficient ubiquinone (coenzyme Q) biosynthesis. UbiK is probably an accessory factor of Ubi enzymes and facilitates ubiquinone biosynthesis by acting as an assembly factor, a targeting factor, or both.
Subcellular Location: Cytoplasm
Sequen... |
A0A965VJF0 | MMRFTTLILALVAVLVAGCGFHLQGTVPIVGDLQHLTLQVTDRQSDFINAMQRNLRSAGVQVGPGSETVLVIERDELLERVASVSARNLPREYELTYSVTFSVKFRGELRVASEQVSVTRDFSFDERLALAKEREREQLRATLAEEAAGIVLQRLASLR | Function: Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 159
Sequence Mass (D... |
B6K3W7 | MFMSVLVTVGSTSFNELIEAVGHKSFYETLVRHGYSRLYVQYGGGKTVFENRDPDVPGLEVTGFDYVADLTPYMEEAQLVVSHAGAGSILQALRRGKRLVIVPNETLMDNHQIELAEKMDSCGYAMRAATSTLAKVVDQACTNSPTPFPEADYSKFRQVMEDVAL | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway.
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP
EC: 2.4.1.141
Subcellular Location... |
A0A962WAN8 | MQPLEGLKVLVTRPAHQAGGLCARIEAEGGTPVRFPTIGIELPQDIRPARERLGRDHWDRVIFVSVNAVQAALELDNRWQTQPLVAVGNATRNALIAAGLSVSLSPDDGFNSEALLALPALQSVHGQSILIVRGEGGRETLAETLRERGAVVEYAEVYRRVIPEADPHALLQSWANGGVDIVTVTSNESLTNLVTMLGSAGHELLARTPLVGVSDRVLQIAASFGLPKPPIVAASAHDTDVLAALIAWRRSSGHKEALSHD | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
E5A8H8 | MDADFSHHPKFIAPMITLQKTNNYDIVTGTRYAGDGGVFGWDLKRKFVSRGANLFADTVLRPGVSDLTGSFRLYKKEVLQKVIRSTESKGYTFQMEMMVRAKAMGCTVAEVPISFVDRLYGESKLGGDEIVEYAKGVLNLWLKV | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of protein... |
A0A3M1WAF4 | MLVIVGLITVEIVLRTLLKTSTLVADEYSGYLMVAVVFFGMAWTLRTDGHIRIGLLTSRLPEGWQKALDLLAHLFVLAFCLYFLMHTGLMVEDTRALDMRADSIAETPLWIPQLSMLAGLVLLTLQVCAEILRRLLSSPTR | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 141
Sequence Mass (Da): 15789
Location Topology: Multi-pass membrane protein
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A0A661GLT4 | MDSRRTPAATRSGSATIHQRAAIAATRPAMTVLAVVAADDSLTMPARQLAAELNLPFNTHPTGEDVLLLRLAADGLSLCDPTSGAALRCDLATGRAGYRRRHGGGVRQALARAVGVRGGVRPSVLDATAGLGRDGFELAGLGCRVTLLERMPVVHALLRDGLARAQPLAADTCGRISLRLADAHNVLTDLARGDTDLRPDVVYLDPMHPPRDKAALVRKEMRLLRGAVGHDTDAGALLGPALAAACLRVVVKRPSRAEALGDRAPDWSVTGRTTRYDVYRAASPGMV | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.242
Subcellular Location: Cytoplasm
Sequence Length: 287
Sequence Mass (Da): 30231... |
A0A1A8I6D3 | ERQKLMREQNILAQVFGILTAPFDETGDGPMLKLNDLGDHRNSHFKYIMRLCYRVLRHSQQDYRKNQEYIAKKFSIMQSQIGYEILAEDTITGEVNVEEG | Function: Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 100
Domain: The receptor contains a calcium channel in its C-terminal extremity. Its large N-terminal cytoplasmic region has t... |
A0A920S3N8 | MIVLTIALFSISVYLSPEARKNIEFSKQNALSNIGIEFFEPGRFITLKDRSVFYSKERYDDNRFVEVFLQTELGDEVSVVTAEYAEIQTNTNDNFLVFFNGKRYQGKPGDIDFRILEFSEHQLPLYINEKNETEKGYFY | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Subcellular Location: Membrane
Sequence Length: 139
Sequence Mass (Da): 16311
Location Topology: Multi-pass membrane protein
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A0A0K1JL63 | MTTGFVAEPGDERLTSAILSDALDAVGRRHQVLSPAIRPVVPGMRVFGRAATVQFAPTTLDSENPYDEAIDFIDELQAGSVAVVATGNSSRSAFWGELFSAAAIGRGASGVITDGCLRDTPKIADLGFPAFTRGNRPIDYRARMRVVAQAEPVILDGVTVQPGDLLLADDDGIVVIPQGAEHEVLERARARAVAERRVLHELLAGDGLRAVWRRHGIL | Function: Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.
EC:... |
A0A2J8XNP9 | METLCLRASFWLALVGCVISDNPERYSTNLSNHVDDFTTFRGTELSFLVTTHQPTNLVLPSNGSMHNYCPQQTKITSAFKYINTVISCTIFIVGMVGNATLLRIIYQNKCMRNGPNALIASLALGDLIYVVIDLPINVFKLLAGRWPFDHNDFGVFLCKLFPFLQKSSVGITVLNLCALSVDSSTKM | Function: Receptor for endothelin-1. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of binding affinities for ET-A is: ET1 > ET2 >> ET3.
Subcellular Location: Cell membrane
Sequence Length: 187
Sequence Mass (Da): 20763
Location To... |
A0A938TTG1 | MNCLGLDCGVKKTGIALGSTITRTARPLDCIAMQVNQVELLLPFVQKWQIELIVFGDPGDRPENKALLNHIVCVKKKLHNLLPSCQIVDWSEQWTSQEARSMMRDFPRLQKQYATDAIAAMLMLQSYLESCV | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 132
Sequence Mass (Da): 14922
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A0A661FP67 | MSGLSAEDLELKSVGNIYHNLSYDELFEHELNNKEGSVASSGTMMIDTGKFTGRSPKDKYFVQQEPSQEYIAWGEVNKPVSVEIFDELYDEVIDYLSGKDLYVTDGYAGASGDTRISARFITEFAWQSHFVKNMFLRPELGELTNFAPDFRVYNASNLTNTKWQGHGLNSEVFVIFNIEKNIAIIGGTWYGGEMKKGIFTMMNYWLPLKGILPMHCSANVCADDEVTIFFGLSGTGKTTLSTDANRQLIGDDEHGWDESGIFNFEG | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 4.1.1.49
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
Sequence Length: 266
Sequence Mass (Da): 29826
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A0A2D8FC62 | MMNKVLVVFGGDSDEKEISALSATSILNNISNDFSARKINLNDLDLNLLDDEIIFIAVHGKGGEDGHLQKALETKNIRFTGSGSDATKKCWDKHLSKNILMKNGINTPFSYYFEKSKTDIREISLAPSKKYFVKPISNGSSLGISKISNFNQLEDAVLLAQKFSNNIIIEEAYEDAEYTVAILDNKPLAPLEIKVSVPSGYYDYEAKYISSKTRKTVVSDSRLIKELKAIALDAYLSHGCRGWGRVDIVSRGEEHAVIEINTVPGFTEKSLFPFAAKHDGISYQDLISTIIRGI | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 294
Sequence Mass (Da): 32... |
A0A496WLA6 | MFSQLSSQGILVPNGFAVTTRAYEYLLNENGLKEQPAEALAGLVPDKPDDLLARAQHCQDLLYNAGIPDRVGNEITQAFDQLVSEYGQALTVAVRSSATAEDLPTASFAGQHESFLNVDGGSIRQTNRV | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 129
Sequence Mass (Da): 13895
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A0A8T7CGC8 | MTGAGQNAPPGPAACARLIDEAFATYNYHFRTVTQRAAGRFASCDWHGSQRDAVQRIELYDRAVNRLVRRLRSLLGDAATERERWVAAKASYRQRTRNYLDRAFHETFFNSVTRRIFGTVGVDPEVEFTEAQELADEAPKHSAIIRSHRYRGSVWSLMEECLRAFPFQLEWDNFSGSVDRTVAAIEAAMAQQGERYALQGVEFLRPVFYRDYRAYLIGRMVGPRADTPLVIAIKHGDRGLLVDGIISDRKELSILIGFARSYLHVDLDPVRDAVLFLKSLLPAKPIGEVFTALGRAKQGKTERFRTLISHLKNTGDRFVD... | Function: Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is f... |
A0A8X7N396 | MAAATSTAQDTQKMTSDAQRDALAALLRRPSKNSGSSSSSSSQRGPPQPPAPAEKVEEEDTAPPTQAPVGTPRPMPFDPSIPPPSIDPFTLPSAQDLPPPPRKRILTPTHLAHFLTSQTHTDLLSFLRQGAASIVGVQVPADVQTPEPSPIPAAGEGEDKRTGIQSALGLLNTVAGILASHPPHAQNQGGTLGSGSASAQGRFGNPTFRNFHAEISARSDELHSQFFHQLREEDGDGEEERKRKKVARTELKAYFDEAWGNARRIDYGSGMELNFVCWLLILYKLGIFNDSVPSASSSSSDSLAPLAELGPDVFLRVFWS... | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 633
Sequence Mass ... |
A0A1X6NM55 | MVSGAGRPPPPPPPGRWDALAHSNPSNPVVFLEFSIAGQPVGRVFFELFADRVPRAAENFRQLCTGEHRPDGVPVGYKASVVHRILPGRLLHGGDLVARDGSGAGGGIYGGGAPFRDEAAGLAATHAGPGLLCSAAGERDANGSQWFVTFGGGGVGLDGQHVVFGKVVGGGDVVRSVGAVRVSPVGVPSAEVLVSECGEM | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 200
Sequence Mass (Da): 20281
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A0A0H5QIN7 | GDQVCLARLGAAHDINLSGWTLHDFRLMCILSGCDYLPSIEGMGIKTAHRLVLTEKTIDRILRRIRLQGKFHVPKGYAEKVVDAQLTFQHQRVYDIGTRRLTFLHDLPSSKSLADSMEFLGPDLTPELAQGIAEARINPITLQAFDAAPDQEPNPTESPPVKPAA | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: 5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Function... |
A0A4R3DRV2 | MDRIPILSRVLDIIQRIGIVVGVAMIVAMGLLMNIEVGTRTLLGFSTQISDEYAGYFFTAATMLCFLPALRDERFLRVEGLIAMAPPRLRAIAEAFAALIGAGTCAVLADATYDLTAASISFGTRSLQASQTPLAIPQAVMPFCFAILSIAFLEWGWVRSRRLWRGQTVTETHHALD | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 177
Sequence Mass (Da): 19336
Location Topology: Multi-pass membrane protein
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I1YNU4 | MAFPRLNNMSFRLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNIAHAGGSVDLAIFSLHLAGVSSILGAVNFITTVINMRWRGMQFERFPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSVKKETFGTLGMIYAMLAIGVLGFIVWAHHM | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A8T3RRY0 | MKFLVPFLIGCLLSCPVGAAVPSQDDLPDIGSPSSAALSRDHEEQIGREIMRMLRDAGQILDDPEITEYVQTVGDRLVGQSQETDYEFRFFVVDDPHINAFALPGGYIGVNSGLVLASETESELAGVIAHEIAHVTQKHIARRVEAGSRAGLVSTAALLAAILVGAATGASPDALQGAIAITQGTALQQQINFTRSNESEADRVGIGILASAGFDPHGMPAFFETMSRRQGLAMSGIPEFILTHPAPPDRIAESRARAAKYPDVEPEDSPEYELTRARIRVLSAKNSSGALQEIRSLQKSEDTGWSPDALSYGEAIALMR... | Cofactor: Binds 1 zinc ion per subunit.
Function: Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state.
EC: 3.4.-.-
Subcellular Location: Periplasm
Sequence Leng... |
A0A1F3TAP9 | MHLWKGLEIDDLSLMNYLEKLDCEMSNSLKQNLPVKLVTHTLEKFNQALTDDQLYEYLNDAHLSKEDLKDEIDFLRNFLKMSNLKNKIKKELGGYDFWDLKKNMDTACVFEGRRPLGIILHITPSNSNVLAFLAALEGLLSGNVNILKVSSKDSSFSLKALKILGDLDDTGLIKNHLIVLRLNSKQKEIMTQLASVANGVSVWGGDPAVMDIKNMVPAQCKVITWGHKISFAYITKFHFHDKKTLSNLAKDCVRLEQQACASPQCVYLETDSYEEVKQFAKEFYQYLKSESDSKKAESLPADIQAEITNVTELVKLDEIM... | Pathway: Lipid metabolism; fatty acid reduction for biolumincescence.
Function: LuxC is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase.
EC: 1.2.1.50
Catalytic Activity: a long-chain fatty aldehyde + CoA + NADP(+) = a long-chain fa... |
A0A2G6LEK1 | MKNRKILLSDSEIPTHWYNILADMPTKPLPPLHPQTLQPIGAEHLQALFPKALVEQEISSEKWIEIPDEVRDIYTLWRPSPMFRAYGLEKVLDTPAKIYYKYEGVSPAGSHKPNTAVPQAYYNKQEGVKKITTETGAGQWGSALSFACQHFGLECEVYMVKASYYQKPYRKMIMHTYG | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phospha... |
A0A0W7WDU1 | MEDYLGEQVTTDATSHEVLKLGWMNADALRRTLDTGEAHYFGRSRQEMWRKGATSGLVQTVVESRSDDDQDAIWLRVDVGGAGASCHLGYRSCFYRTIPTAEQAGHALTFNENGKAFDPVATYGDVPNPTRL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
EC: 3.5.4.19
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Len... |
A0A3B8WUV3 | MHINYPLYVVASHLLLPVALTRLLIKSRNSPPYRERLGERFGYYRQPRCQKPIWIHTVSVGEFNAARPLITRLQERYPQIPLLVTTTTPTGSAEVRRFSTNLDHCYLPYDLPWVVNRFLRHFKPRLAIIFETELWPTLFRRCQHADIPIIIGNARLSDRSMRGYSRFQPLIRETLRIPSRIAAATNETAQRLQTLGAIPDRTSRVGNTKFDYQPEQEIPEQANRLRDQVLGKNRSVWIAASTHEGEEEQLIRAHMGLLQEKPDALLIVVPRHPERFDRVADLCSDYLSTVRRSSGIQCSDETKIYLGDSMGELPLLYAAA... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A8H6XXU4 | MRIRPIAKFWSAFLKICFEILCIVPISWICGRGHSNFIATSTTITGLQTREIVQSLVVTPGKDFNSKFGHYRHSDLIGMPYGSKVGSRTGKGFIHVLRPTPELWTMALPHRTQILYIADISFIISYLDIRRGSRVIEAGTGSGSFSHSVARSIGPSGHLWSYEFHEARAKKAREEFAQHGMSDIVTLTHQNVCKDGFNLTDAVDSVFLDLPAPWDAVEHAKQALRKDRTTRICCFSPCMEQVLRTVSALNDAGFSDITMYETLVRPHDVAQVPALQSITEVAEKLKKAEGVREIKRLQQIAAGQRSRENPHGEKRKRNEV... | Function: Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA.
Catalytic Activity: adenosine(58) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(58) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1... |
A0A5C1IYB9 | NHKDIGTLYFIFGIWSGMLGTSLSMLIRLELSTISNLIGNDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLIPIMLGAPDMAFPRMNNMSFWLLPPSLSLLLISSMVETGTGTGWTVYPPLSSIIAHTGSSVDFSIFSLHIAGISSILGAINFISTMLNMKIKFLKFDQISLFIWSILITTVLLLLSLPVLAGAITMLLTDRNLNTSF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A3P7C9W8 | MALGLMHPAKVTGGDEMEEVEEEEQKTFPIAHDLDAQERTNDVLLPVVGTEADTGPLSSPVKVRSSPSFASMGLSVNVLKGLHAAGFQQPSPVQIKAIPLGRMGLDMIVQAKAGTGKTVVFSVVLLEAVSPEKNAVQAIVLSPTREVALQSMNVIRQLGQFIDGLQCHLFVGGRPPPPPPFAHSSSLPFLQLPIKCVGMLSVLLVPTTISVIFTLGDCKIVFFGTGLPLSEDIQKLVNCHIAVGTPGRLKYLINAGHLSCHSVRLLVLDEADLLFSGNYTLCAGNEADLLSGKNTFPAAINYIWWSLPEVKQVLALSATY... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 804
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 88626
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A0A8T3UZA1 | MDIQMILIACVTTLYFILPAYFSNGGGLVFGGGIPVDFGKSDSKGNRWIGDGVTWRGMIGGTIIGIITGAVQGYFGPQIIAEFGDYIITPIITSIPEGILIGFLLGFGALLGDAIGSFLKRRLGIGRGKPAPILDQLDFLIVALILVSFVVKLNWLFVVIAIVMTLVIHLIANTGAYLLGMKDVWY | Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Function: Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal... |
A0A964LSK6 | MRGHPHGCPRFFRPLSSNFSQRIETMTDRNFDELADRFETKLYGHWRGQIRLQLVTEALLQDANCLQQSQPLRVLDAGCGLGQMSLLLAERGHHITACDVSGILLERARARIAAANPELLQHIDFHCCPLQSIGAHVEGQFDLIIFHAVLEWLEDPRAGLQSLLPLLKPGGEMSVLFYNRHSIIFKNLLRGDFRRIDEQDFKGDSGSLTPINPLPPADVAAWLHAMSLTVTSQRGIRTFYDYMEQNLDKNKPAKASLDDIMRMEKKFSTLEPYRSLARYLLWHCRKTPEGI | Function: Catalyzes the methylation of 5-carboxymethoxyuridine (cmo5U) to form 5-methoxycarbonylmethoxyuridine (mcmo5U) at position 34 in tRNAs.
EC: 2.1.1.-
Catalytic Activity: 5-carboxymethoxyuridine(34) in tRNA + S-adenosyl-L-methionine = 5-methoxycarbonylmethoxyuridine(34) in tRNA + S-adenosyl-L-homocysteine
Sequenc... |
A0A5D2MS95 | MSSKVSAFCIIIFLLFFTLYSAAAASQDLGNEKERDEMDGSCQGNTEEEDCLMRRTLIVASLDYGAVRHQTPRP | PTM: PSK-alpha is produced by endopeptidase digestion. PSK-beta is produced from PSK-alpha by exopeptidase digestion.
Function: Promotes plant cell differentiation, organogenesis and somatic embryogenesis as well as cell proliferation.
Subcellular Location: Secreted
Sequence Length: 74
Sequence Mass (Da): 8249
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A0A661FS72 | KVARAVDKVLCLLPFEKTFYDEHDVAADFVGHPMADNMPVDLDTATIRLVLGIDAPMVVAVLPGSRHSEVSRLGPIFADTCVQLIRKHPELRFITPMVTDRLKQLFAKHLDAVGISDRFLITDGDAQSAIAASDLVLLASGTASLQTAMLRKPMVGAYRFSVLTYAIAKTFKLVNVPFFTLPNLLTVEPLVPEFLQAEATPAALATAVTDLLDDPERRAMIKKRFTELRSELALDADNCAASAVLELANRSG | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.4.1.182
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydrox... |
A0A2D4TSY2 | MTDKSRDFSHRHIGLKNPDIQHILHDLGYQSLAGFLEDLMPDSIYDLDKIDLPNPLDEPAALKTLKGISKQNKVFKSFIGQGFYNCNVPNVIKRNVFENPGWYTSYTPYQPEIAQGRLEALMNYQTMISDLTSMDISNASLLDEPTAAAEAMMLANRVSKSKSNKFFVHSSSFKQTISVIKSRAKPLNIDITVGEEMDEGVEYFGCYYQYPNADGGIEDLAEVSERIHEHKGLLIIGTDLLALTLIKAPGEFEADIVIGSAQRFGVPMGFGGPHAGFMAVKDSFKRSLPGRLIGLTQDQQGRPCYRLALQTREQHIRREK... | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
EC: 1.4.4.2
Catalytic Activity... |
A0A3A2ZM52 | MEKYKLDIYTADSIPKSDFESSFRLVELTSSGDYANSGTGWSPTKKKREMKLPDMKYLILRRGSDGEAARDEGESRSTDCAQGRGEVLGFLSFMVTYEDGKEVIYCYEIHLSPAVQGRGLGKHLIKRCEEIGRRIGLEKSMLSVFRSNRRALNMYTTSGYTVDEFSPPPRKLRNGTIKEAEYLIMSKVLKNSGGDERERSGQGQ | Catalytic Activity: acetyl-CoA + N-terminal L-seryl-[histone H2A] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[histone H2A]
EC: 2.3.1.257
Subcellular Location: Cytoplasm
Sequence Length: 204
Sequence Mass (Da): 23020
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A0A3M1KFZ4 | MPMDDDSSAFEMQLSQQAESLLAHVQKGDFAGAVQVIAELNETRDKTLYHEVGRLTRSLHDSIRNFNIDAGTKAQREEMSKIADASDRLAYVVEMTSKAANKTLDLVEEAMPIASSLKSEAHELKKEWEKLRRKELTPDEFRALYKRIDVFLSDLEGKSDQVYGYLSDILMAQDFQDLTGQVIQKVTDLVRQVEDNLVKLVAMAGKVDRITGIQHDLEEQEHDESAGHGPQMNTEKRDDVVSGQDDVDDLLSSLGF | Function: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P).
EC: 3.1.3.-
Subcellular Location: Cytoplasm
Sequence Length: 256
Sequence Mass (Da): 28787
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A0A962TD81 | MRILLLGATGQVGWELAQVLPAHGELYTTRRGAPTGGNNDFQLDTQDLGGLLALLDRVRPDVVVNATAYTAVDRAESEPELAMRLNADVPRALGTWAAGNDCLVLHYSTDYVFDGSKPEPYVETDTPNPLSVYGRS | Cofactor: Binds 1 Mg(2+) ion per monomer.
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NAD... |
A0A523MB66 | MPEVGTSDQSGRTLKLRIVSALIAAPLAVAAVFLLPPTSFALVFAVLAGIALDEWGRLAGYSTWRGRMVYLLVFGGLCVALAQMPGAAVAALAVMGVGWVIAAGIVVGYPRSAMVLRAPGVIPGAGLLVLTGAWLGLVSLRAQPGLGAWLIIWLFVVVWSADIGAYFVGRAYGRHKLALAVSPGKTWEGAAGGLVCSVLLATGLVGIVPALHMVSLSLTDWALLAFALGAISIVGDLFESVLKRETGAKDSGTLLPGHGGLLDRIDALLAVLPSFALFVLLMLRN | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 285
Sequence Mass (... |
A0A0W7WII3 | MHRFVFGIARFMALLGGAVLTLLILITCLSILGRALNSGLHSDLVMGLVPGLAQGLIDLGIGAIPGDFELVEAGMSFCIFAFLPFCQITSGHASVDIFTNALPRGANRVLEALISILFAWALILIAVQLGAGMQRKMPNDFGAVQTSLLLQFPIWWSYAASLVGATAAAIVSVYMAVVRLYELLTGRVIVADALGANH | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 198
Sequence Mass (Da): 20972
Location Topology: Multi-pass membrane protein
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A0A1F8P4Z1 | MKRSKTQDVFDVTFIGAGPTGLFGAFYAGLREMSVKVIDTLPQAGGQLIALYPEKLIFDTPGYPSILSRDLVSNLVKQTERWEPTMCFDEHCLGLRRDTLPGSEKGESCWVIETDRDLHYSHTVIIAAGIGAFRPVKLENESIDSFEGRGVHYMVKDLDSHVGERILIVGGGDSAVDWALALEPIAEHVTLIHRREGFRANDSSVNALKNSTVDVQLFYELRRVEGKKQVEGAIIFDNRTGEEKALQVDSIIFALGFKADLGPIREWGLDTIGRRYIKVNSKMETNLPGVYAAGDVALQEELDPLNLIVMGFGQVTVAVN... | Cofactor: Binds 1 FAD per subunit.
EC: 1.18.1.2
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Length: 348
Sequence Mass (Da): 38364
|
A0A2E1J1K3 | MMNLKKSISFIGMAGCGKTTIGRLFSKKHGVNFIDTDHLIEKRLKKTLQDIKDEKGYMYLREIEQEIVLAIDASTKIISTGGSVIYSDQAITHLKKISSVIFIDTPYKLIKKRIGDASNRGFSVPNGFSVKEAFDERMPMYQQHQDFTVNGANSADYIIKSIEQWI | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
A0A3D5DG06 | MILSNRGFFLLIVIGGMGLLSFGYYLEFYQDLLPCPMCILQRLCYGAIIVVALAAAIQGPARAAGIFYCAGVAILASLGAVIAGRQTWLQHLPPELVPECGPGLEFMLEMYPLRQAIEKALMGTGDCADVSWTFLSLSIAEWSLACFSGIIFAALWQLMVNWGHTDA | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Subcellular Location: Cell inner membrane
Sequence Length: 167
Sequence Mass (Da): 18113
Location Topology: Multi-pass membrane protein
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A0A534CSW9 | MPDPRKSQQEVPKYRRIRLHSRGFSGPKDSRSRELGHELLAFQSNAEHELIQRIQRAPADAVAFIIINPGALTHTSIALRDALAGAALPFIEVHLSNIFAREPFRRHSYVSDLAVGVITGLGACGYEAAVRAAAARLARSP | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Catalyzes a trans-dehydration via an enolate intermediate.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 141
Sequenc... |
A0A432EQ66 | MKHKAAEALKTLERYVELISSGRYDQKISIDDPDYKGLADKLASLAATMQESVQDVDSKVRHQTERLEQKRGSLEILYDVASTINESHDLQQLLTGTMRKLMGVVGAPAGAAKLLDENGETRLTRYVGIHDERAADREGSGLFGAFNGAAPQLVRKELGENESDDIRSLLSKDVKGVISIPLRYQDRTVGVYHLLTATPGVAATEEMQELLETVGKQLGFAIEKARLDAESKRLSIIEERNRLAHDLHDSLAQTLVSLRFQVRNLDQTLQQNGDYASIHEIERVEASIDEANSELRDLIAHFRSPMDKLGLYPALDRVIK... | 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... |
A0A973DQW5 | MTEFKNVTALAQSNVYFDGKVISHKIILADGTEKTLGVMMPGEYTFDTNVAEIMAVTAGEMNVLLAGANDWQIFRAGESYQVAANSQFKLKITAVCDYVCSYLPRLV | Function: Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
EC: 2.4.2.1
Catalytic Activity: a purine D-ribonucleoside + ... |
A0A6B1H931 | MFAESSPAELGRLNFDNRFALALPADPESDNFRRQVASACYSRVMPTPVSEPRLVAWSPEAAALLDLSAEVDQSGLFAEVFGGNRVLEGMDPIATCYGGHQFGNWAGQLGDGRAINLGEVLNRRGERWTVQLKGAGPTPYSRTADGLAVLRSSLREFVCSEAMFHLGVPTTRALSLVLTGDEVVRDILYDGHPAPEPGAVVCRIAPSFTRFGHFEILASRRETDLLRRLVDFTIETDFPELADEGEAKARTLAWFAEVSDRTADMIVHWMRLGFVHGVMNTDNMSVLGLTIDYGPYGWLEGYDPTWTPNTTDASTRRYRF... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
EC: 2.7.7.108
Catalytic Activity: ATP + L-seryl-[protein] = 3-O-(5'-adenylyl)-L-seryl-[protein] + diphosphate
Sequence Length: 423
Sequence Mass (Da): 46898
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A0A2E0IB87 | MFSLKLNKLEAKRTLRNLAGIVVGMFAFGWLLVPMYDVFCEITGLNGKVTGPSSLSEESLAITEQRELLVQFMTHNNESMPWFFDSEKSQMRVVTGNQYEATFVFHNTTGKEMVGQVIPSVSPGRGAEYFHKTECFCFERQVLAAGERIELPVRFIIDPALPKEIGSLSLGYTLFDITDRVQTNNEIAKL | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Subcellular Location: Cell inner membrane
Sequence Length: 190
Sequence Mass (Da): 21411
Location Topology: Single-pass type II membrane protein
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A0A1F5DMV6 | MNTLLLPESLRSELKTPLGELYRGEPTETTAKLRDKLMVKPPLLAVVGDFVAANVIAAGLFPDIVVVDNKTLRVQIKPVVHGLKEVKVPNEAATINAKAWLALRTAVTLKRRVAVVVEGEEDLLVLPLLAEMPLGSVIAYGQPHEGLVAVTVSEERRDWARGFLNRMEMKRQ | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Function: Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
EC: 2.7.1.237
Catalytic Activity: 3'-dephospho-CoA + GTP = CoA + GDP + H(+)
Sequence Length: 172
Sequence Mass (Da): 18950
|
E4ZQ06 | MDMVQPRMHAHIGSLMENSSPNINKSFFLSTCSHANNRVRYEQEGDYRVQFDKHAIFKSRCHRPASVHSGPEALWSLLAHFVSPPEALALTDGTDVEELAGLASMSTQVFQKSKSATEHTDMGRQDRRAASQFLKERSSYDLNLEDYEISAKTHDSIAWEVVHARPKLCLGECSPQTSIPQGSHELPDGTYNIATPIAAIVLTMSSKFTYLRAARLAARHPCRQRTFASAASSRADHVRIVEVGPRDGLQNEKKTIPLATKIELVERLAQTGLTTIEAGSFVSPKWTPQMANSAEILEHVLNRAPQSSRPITYQWLLPNV... | Pathway: Metabolic intermediate metabolism; (S)-3-hydroxy-3-methylglutaryl-CoA degradation; acetoacetate from (S)-3-hydroxy-3-methylglutaryl-CoA: step 1/1.
EC: 4.1.3.4
Catalytic Activity: (3S)-hydroxy-3-methylglutaryl-CoA = acetoacetate + acetyl-CoA
Sequence Length: 576
Sequence Mass (Da): 62619
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A0A0X3PY48 | MPSSVKQHRATGMKEYESASTVSSFIRQYVHYRPQIAILCGTGFDAIADLISSPRILRFDDIPGFPNCEVIGQEGKFVFGKIAGKDVVMLQRRFQSSNTENNNTLSLPIRVAKLLGADYLIIMTVVAAVNPSYEVGDVMMVSDHVDFASISTRSPLICQSNSWYGADFEPAFDTYDRRLRDITRSSVNELNTPVCLHEGVYFHMATSSLCTPATTRMLQTVGCDAVGPKIIQEVLAANYLKLKTLAIGLVTYARNDYRRSPVEATKIARICFPKVSQLLEQVIQNI | Pathway: Purine metabolism; purine nucleoside salvage.
EC: 2.4.2.1
Catalytic Activity: 2'-deoxyguanosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + guanine
Sequence Length: 286
Sequence Mass (Da): 31773
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A0A496VZL2 | MKILILGGTGMLGHMAYRVLSKHHEVYVTCRNSFKNTLILRSLVKKQNCIENVDALDIASLGKRLQELQPQVIINAIGIIKQKKAAKKPILSIKINSLFPNEVAQLADEINAKLIQISTDCVFSGNLGMYTESSPEDPIDLYGRSKLLGEVTYSPHLTLRTSIIGRQLQGDSSFFEWFLKQKNGSVNGFKHAIYSGLTTQALCQIIHQILTQCFQLSGLYHVASQPVSKYDLLTQLNLMMNLNVTINPDTQFCCNRSLDGRPFILKSAISIPSWENMLSQLVLDVPHYEEIITV | Cofactor: Binds 1 Mg(2+) ion per monomer.
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NAD... |
A0A389M2E7 | MEAKTGSILAQSNGYSLLEPASITKIMSSYIVAQAIEKQEIALTDKVIISNYARSQEGSRMFVEKNSAVSVLDLMRGMIIHSGNDSTVALSEHVAGTEAQFVVRMNAMAVQMGLKNTHFKNSTGLPANGHLTNAYDIALLSRHLIYDHPDIYKIYAEKTFTWNKITQPNRNQLLFTDPSVDGIKTGHTSAAGYCLVSSSVRDNFRLIAVVLGGAKEKDRYDASKALLDFGYREFIRQKIYTKEEIIANISLREGTANTLAVGLPEDLELTFKKGRYQDITAQVKYNIITAPVKKGTVVGDLIFTLDAKVLLSIPVVALQS... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
EC: 3.4.16.4
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanin... |
A0A3D5DCH0 | MNLDNFRLLRDPGHFLALGGGSGLLPKAPGTAGTVVGMVIFWPLAALDNYVYTGLVLALFALGVPLCSRTSLAIGANDHPAIVWDEIVGILLTMAFVDPNPFNCILGFLAFRIFDIFKPWPINVLDQRVRGGIGVMLDDVFAALYAGLTLVFIEYISYI | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
Function: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG).
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate... |
A0A3B8WUZ0 | PYYLRFMERFPQIDVLAAAPLDDVLSHWSGLGYYARARNLHRAAQEVVEQFDGQLPATAELLTNLPGIGPSTAAAIVALTWNRRATILDGNVKRVLSRYHRVAGWSGESKVQQQLWRLADRQTPVTNCRSYTQAIMDLGATVCRRRNPDCHNCPLSADCGAWQHNEVALYPASRPRKERPHKSWRMLLISDPAGALLLRQRPPSGIWGGLWSPPEIEVAQTDIGSWSADQLGFTATPITELEPVEHKFTHFDLTLIPVVCQARQGVTGSIMDRPGQLWYNHATHQIGLPTAVSRVITRYSEYLSGVTGP | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Adenine glycosylase active on G-A mispairs. MutY also corrects error-prone DNA synthesis past GO lesions which are due to the oxidatively damaged form of guanine: 7,8-dihydro-8-oxoguanine (8-oxo-dGTP).
EC: 3.2.2.31
Catalytic Activity: Hydrolyzes free adenine bases from 7,8-... |
A0A2E9NW30 | AEAVGRRRNEAAQREADSRINFDQAIKNWLGLLILLVPVAIFFTLGAIGYFDPPRSVDRIEAHVRQLELEAAEARRKAERMVSPVPDSELFYRPAPELSDSIYMEIERPLVTVLNGSDKRLRIKFAIKSSANAQTIQNMKKHQIAVHSAMIDALLGLKESSLSKPNFANDLAEKLKTVANNALQKYEGYGGVEELIFTEFEVQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell inner membrane
Sequence Length: 203
Sequence Mass (Da): 22797
Location Topology: Single-pass membrane protein
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A0A2D9SPG0 | MLSFSLQFGYAHDLPSVXARXKSQPSDFMVVEQSIAATSHGEHVYLRLRKTNMNTAWLAKCIAETANVTVKDVGYAGRKDRFAITEQAFSCXLPGKQVSQWDRLEDDQVKILAVXRTSRKXRKGXLYGNXFVIRLRDVSGDLTRKXETXKSQGVPNYFGEQRFGRSMNNLRQAELLMSGKRRHCQQRDXMLSAARSYLFNVNLSRQIAEQGWRSIGDEQQGVLFGLSRDPQTGELDLPEYCAHWVAGLRGFRXXSGLRNXKLVLREMSWDXLGRDWQIRFVLPPGAYATSVLRELVXDGXSGSGC | Function: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
EC: 5.4.99.27
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Length: 305
Sequence Mass (Da): 34510
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A0A3M1UTP8 | MTRIFSRVLAGLILVLVLAATNLQAAPQLLDRIVAIAGDDVIMLSELRDKARELAAELQRSNPRSMPSDSQIVNKALEELILEKLQLAEAKRLGITADPETVDKAIERIARNNNLTVSQLKEALAAEGMDFQQFRNRIRDQIIISRLINREVTNRIQVSKSEIDQYLAREEAAPDEKREVHLMHILVATPDGASPEQIARARQRAEEARKRLDAGEDFAEIAREFSDARNAIRGGDLGWARIGQLTPAVAEMVSKAREGDILGPFRSGAGFHLLKVAGFRGGKRTARKIVPQIHARHILIRTDEVTSDADARQRLEQLRA... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
A0A972LA43 | MLKQRLITASILIPLVVWGIFSLSNATFAWILAVIVLAGAMEWAALIGLTQPLQRALYAALVALCMAVAFLLSKVSGGALFGVLLPALLWWLVALGWLARSDGARNPAVANRAMGRALLIDCGVGIVLLVPAWLALVLLHGMDGGPGYLLFLMVMIWAADSGAYFSGRRWGRSKLAPSISPGKTWEGVAGGLALVTLLALLGGGMLFGFSIGGLLLFLPLCLLVVLFSVAGDLFESMFKRRIGVKDSGRLLPGHGGVLDRIDSLTAAAPLFLLVLLVMGLSL | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 282
Sequence Mass (... |
B8Y3S3 | LPPSFVLLLCSSMVEGGVGTGWTVYPPLMGPIAHGGSSVDLAIFSLHLAGLSSILGAINFITTIFNMRSPGMTLERMSLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDPAGDGDPFI | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A962R719 | MTAATFVDFLTRVRAGLRACRHRRLVLCVGDGSWRAEIDAGFVMTEARLWRLGEGLPGGMSPRQAAQRLGQECDILLVDALTGLDPDALGALGGCVVAGGVIVLLTPPWQEWAANVNPMNAHLAVAGWPENAIGDRFNTRMRRLLDEHPEVIRVIQEAPLPDLEGSDWVTGERGVGERNQLEGRALTRDQESAIEAVCHVVRGQRRRPVVLTADRGRGKSAALGLAAARLFAEGCQRIRVTAPSKEAVATVFAHAGAIPEGAELCFETPEALIDAPPPLDLLLVDEAAGIPTGQLKALLRQYPRLAFATTVHGYEGTGRG... | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Catalytic Activity: acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O = ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) + phosphate... |
A0A962RFJ2 | TPPFGFALFYLRGVAPPSVKTIQMYKGVIAFISLQLLALVIVGLNPPLVNYLPNRVSLTSETAPPPINPRLQHCLETQVFARYDTEGDRLRAAIARAGTLDLSVLPDKERRDLEASLASAARTFELVDEVRSADAAVVARMDAYKPLHREVRFLEGQIRRLQTELAETRQRLDRLSRNPDAETGSKSVLEERAVAIESQIETLRGAVPSDWAQTSKAFSALTTAEVKARRQYRANVDQAYTPVAELIALLDDAAALAALQPEFERLARELPGLDPQAASARLDALSDEIGALEGTSRIRSRLSRARRELRGDRPDLERAV... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 389
Sequence Mass (Da): 43272
Location Topology: Multi-pass membrane protein
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A0A7C6F1U3 | QVQFNAPRVLPLSSYKDNNLAAALGSEQKFGGAGDSSQSNSLTGNISVSVIEVLSNGYLVVRGEKTVSLNQGSEYIRVAGIVRPQDIAPDNTVLSSKLADARISYGGNGVVAESNRQGWLSRTLGAIWPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 130
Sequence Mass (Da): 13739
Location Topology: Lipid-anchor
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A0A8T7DAU9 | LDHQGMVLDFSDVKKKVKQLIDDDFDHKLVIPEKYDGSSSKTSGKRLQNTFRLIDGRKIVHIAPESAYCSLPCEEINEQQMAEAITEKLGKILPDNVEQIDIRLYPETIDGPYYHYSHGLKHHAGNCQRIAHGHRSCIEILEQDDHRHDLELEWSERWRDIYIGTRSDIHEQYSENGTDYIHFRYTACQGLFELIIPARCCYLVDIDTTVENLAGHIAGELKVSQPGSQFSIYAYEGIEKGAISNTF | Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 247
Sequence Mass (Da): 28340
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A0A2E2HET9 | MEIETLMAEPKSRDKLPGVLCLNPGSSSLKWAFYCSTTQKKVLKTGTVSLERLSKELLVILKKYEVSLVVIRFVHGGTDFYEPVEVTSKVYGELCSIKSFAPLHINTSLLCSELVTNNLKRVKQVAVFDTEIFKELPEAAQLYGLPESLRDKYGIRRFGFHGFAHAGMLEVYQELTDSAPHKEQRIVTIQLGSGCSMAAFLNGNPVECSMGFTPNDGLLMSTRSGEVDAGLVTWIQRQEGWTPDETDIYLNEKSGWAGMSGEGSDFSVILRSQKLSSERAVRLFIHRVRKNLGSFFAVLGGLDAVLLSGGIAENATHFCH... | Cofactor: Mg(2+). Can also accept Mn(2+).
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
EC: 2.7.2.1
Subcellular Location: Cytoplasm
Catalytic Ac... |
A0A661GMR6 | MKSVIHAIESFNIWIGRAFGWCILVLTLSVVYEVFVRYVLNAPTVWAFDMMVQMYGALFVMAGPYALAQDTHVRADVVYRLIPVRWQARVDFVLYFVFFFPGMLALFWYGWEIAADSWRYKEVSWNSPA | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 129
Sequence Mass (Da): 15122
Location Topology: Multi-pass membrane protein
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A0A7C1BTQ1 | MKKLLIIMTCIASLTIAACSRYHLVHKIDVQQGNVITQDEVNLLEPGMNRRQVQFVMGSPMIADVFHQDRWDYVYLLEPGYGETTEERVTLFFEDDQLSRITGTLHPDEAGSAAPSRPKQVTLVVPPEERVDPGIFNKLWHWMTFRKVGEASYVSSHDPGYSRTNKPSPVSSSEEQEHILLHRSEQAPAPFFITLPSAARCFLTCLGSAINGR | Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 213
Sequence Mass (Da): 23999
Location Topology: Lipid-anchor
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A0A2J8VX17 | YSERHGWGYLVPGRRDNLASLPTGTTLESAGVVCPYRAIESLYRKHCLEQGKQQLIPQEAGLAEEFLLTDNSAIWQTVEELDYLEVEAEAKMENLRAPVPGQPLVLTARGGPKDTQPSYHHGNGPYNDVDIPGCWFFKLPHKDGNSCNVGSPFAKDFLPKMEDGTLQAGPGGASGPRALEINKMISFWRNAHKRISSQMVVWLPRSALPRAVIRHPDYDEEGLYGAILPQVVTAGTITRRAVEPTWLTASNARPDRVGSELKAMVQAPPGYTLVGADVDSQELWIAAVLGDAHFAGMHGCTAFGWMTLQGRKSRGTDLHS... | Function: Involved in the replication of mitochondrial DNA. Associates with mitochondrial DNA.
EC: 2.7.7.7
Subcellular Location: Mitochondrion matrix
Sequence Length: 382
Sequence Mass (Da): 42160
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A0A8T6HY15 | MTGLELNLQIALIALGIAALVLIYLYSRFHDKGMRRSRARSAARNGPERESDAYMTDEEYRSRQEIPDFLGGSESGGTPKAGIGDPCGGSKSSRMADHSEFPDEGSSPDDLEPDRSVGVHGVRHSDEDNDTESPVLTEQIYPDQPELFSDPQTSPDDRAEFSDFGARGEAVTDGRADPPMIDPVRDVFEDSAGEETGVQPGNGARQGREPSISLDPLPEAEEDGSHAPHDLFVDSAKDRSRGGKAVPSESRFASILKGTGFFNRFRKQKSVQHLKSDDSDEFQDGSDSEYDDVPDESEVVALRESEEYSEPEHPPEPEPA... | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 6... |
A0A0B1RL15 | MSARLSRSRVFTEVVEFRSPLAYPSWRSVTDMQVEDHVHCIDLDGGGWGAVRRELLRVLTTPMDLRRPPWEVYALTGARAVPGIDDGATFVALKFHHSMGDGVEAVAIGRKLFDAPDVLADCSDRDQKFTAPPNFVRQVGMLPGQITKMLLAARRARNAVAELGTLDELPSLPEARANRFNELPRNNDLAFDLARWPLETVHAARAALPEATVNDFALAVIAGAMRSYLREHEELDGSSVVVGVPMSLVPLASRWTSKDEASNQFGMILVDLQADEPDPVVRFAGIVAGTMHEKRRSRNSLVLAATTALDDYPWWAAKRV... | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 425
Sequence Mass (Da): 46096
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A0A964PMG5 | MVKRVRRAYSALFACALPLLLVRLWWLGIVNPAYRLRWRERLGWYSHPRPAVRPIWIHAVSVGEVNAAAPLIKALRERDRDIPILLTTTTPTGYDTVARLFGQGVQHAYFPYDFSPIVVRFLNYFTPRLLLLMETELWPNVIHACGARRVPVCLINGRLSSKSARQYALIRPLVQPMLAGLWHAAMQSDTDALRLIGIGARPEAVSVTGSLKFDIYIPPSVYEEAAALRRNLGQDRPIFMAGSTRPREEDALIEIYAELKERFPNLLMVLAPRHPERFAEVAALCEVRGLKMQRRSSGTECVPSIEILLLDSMGELVRFY... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A349X6B4 | MSQTVLDDCLKRATDASFNRITVDGDTSTNDAVVLSATGKAGHALLYDSSSDDAKAFYVAVHDVLLDLAQAIIRDGEGATKFVTVEVKGGKLQSDCEEIAYSIAHSPLVKTAMNASDPNWGRLLMAIGKAPTKYFDIDVLNLAINGLALIERGQPHPDYSEEQGQREFQKEEITISVDLNLGGESYTVWTSDLSHEYVRINADYRS | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and ace... |
A0A351SAY6 | LIFAAILAISSMVILSTLVNLLTAFLTFLSMIGYAFIYTVYLKRTTPHNIVLGGAAGATPPLLGWCAMTGTVTIEAILLFVI | Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
EC: 2.5.1.141
Subcellular Location: Membrane
Sequence Length: 82
Sequence Mass (Da): 8720
Location Topology: Multi-pass membrane protein
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A0A351CMR1 | ACSIPPYSLSKEVLDKMRDHVIAMAKELNVVGLMNTQLAYQDGEIYIIEVNPRASRTVPFVSKAIGEPLANIAALVMSGISLKEQGFTKEVIPKHYSVKEAIFPFNKFLGVDPILGPEMRSTGEVMGIGKDFPSAYDKALLAANDRPPESGKVFVSLRRLDRDKLVDLGKKLTTQGFSLIATRSNKETLNNAGLECEMVNKVSEGSPNIIDMIKNDDIDLIINTVEDSQGIEDAAEIRCQALIHKVPSTTTVAAAFAMLDGLKTHKEIKVIKLQKLH | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
EC: 6.3.5.5
Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Length: 277
Sequence Mass (Da): 30348
|
A0A3A2ZQ46 | MAFTSYHVQIINRISSGYPVWYWYIASQLLDHFAKSQSSKPKKYGRIVPIVVQSMVAT | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 58
Sequence Mass (Da): 6693
Location Topology: Multi-pass membrane protein
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A0A7C1UVT0 | MKKILILIINITFLVVTGCSRFIPAYKIDVQQGNILLKEDVDQIRPGMDQKKVSYILGTPAIKDPFHPHRWDYIYTLKKGNGKYEEKNITVYFEKNKLVRTEGSVRPDPTTAKSPDKYKKSAVMTVNPVIREKPGWLKRIWISFFGSEEDLESLD | Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 155
Sequence Mass (Da): 17933
Location Topology: Lipid-anchor
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A0A481W7H3 | GLISHIISQESGKKETFGALGMIYAMMAIGLLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSRLTYSPSLLWSLGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGLVQWFPLFTGLTLNDKMLKIQFLVMFIGVNLTFFPQHFLGLSGMPRRYSDYPDAYATWNIVSSIGSLISLIAIFILLFIIWEAFSMNRKSTWATNLPSSIEWLQSMPPAE | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A3B8WTW6 | EVAEMVYKCTEYYAPEDEYSLLWNDPELAIEWPMPEMALLSDKDLAGNTIASSPTFA | 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: 57
Sequence Mass (Da): 6460
|
A0A3A3A9D5 | MRLLNAATTLCALFLPSTLVYADSTSSRLSLPPDFKPPQVFKNTNLVRNTNLEKGYVRETVNVVVENIGKKPQSDYYLPFPTNVYDKVGALEVRDKKAPEKGRFDVETTEVELSR | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 115
Sequence Mass (Da): 12966
Location Topology: Single-pass type I membrane protein
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A0A8T7JAQ4 | MQADYSDANVAHWCQQFNIEPSADSPWLITWNDGLQLQHKQQQALWLQLSFTDGRIGHRTQQAKFQSEPVLKAMKLKPNNQAMVIDATAGLGRDGFLMASTGATVIMYEENPILAMFLTEGLARAAADAADVTERITVHCANAIKALPTLTADTIYLDPMYPSRKKSAAVKRDMQVLHTLLPPPGDADDLLESARQASVKRIVVKRPKTAPVIFTDGLVGQQKAGATRFDLYAPLYPIDR | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.242
Subcellular Location: Cytoplasm
Sequence Length: 240
Sequence Mass (Da): 26473... |
A0A7C1ZAD3 | MSNVNIFIKGMTCDHCAQDVQDALNALDGVNATVSFANSMATVKTHENTDTNRLLVAVESKGFQASLITGDLHIVIVGTGSGAFAAAIKSVEQGAYVTIIESADIIGGTCVNTGCVPSKISIRGANIAYQQAHHAFDGIPFNTPVIDRKAMVAQQQAWVEKLRYAKYESILESTPGIALMRGTARFKDSKTLIVAMHDGSETEITGDRYLLAVGAHPMIPAIDGLADTPYWTSTEALVAESVPEHLVVLGGSVVALELAQAFRHLGSKVTIMARSTLLSKEDAEIGEGLKAVFENEGIIVELHTVPDAISHDGSNFTVG | Cofactor: Binds 1 FAD per subunit.
EC: 1.16.1.1
Catalytic Activity: H(+) + Hg + NADP(+) = Hg(2+) + NADPH
Sequence Length: 319
Sequence Mass (Da): 33821
|
A0A2D8FDJ1 | MKIKVCGLTREEDIVSLLNSNIDYFGFNFIEESPRYVEQKWAIEMYHKYNLGEKFVALFRSDRADILNNIITYSPESTLQIYGDLKTDHFLHKLLIPVSVTTLKQNAYKDLLNPNKHKYLVDNMINNLGGTGKKVDLNSIDKNLFPTIMIAGGIGIDDINNLQNLNFWGVDINSKIELSPGIKDQDMIKILGDFIEK | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Length: 197
Sequence Mass (Da): 22545
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A0A6L7TGK5 | MNEEESLETEQLLESIQTLKSSNTNRTLERQRSKLLNRIGRELERRGELLHSLLAYRHSSVHPARERQMRVFHRLDQIFEMEELRMEITEKPWTIEEKLFAEKFKCKSRVDVKYNTNEQVLTDPSTDNIEIFACSEFEARGWAAWHLENHLPSALFGLAYWDWVYAPIQEAFVNPFQIGPRDLYTPEFFAVRRELCVDPLMDSMPLIQRLEQTFEQKFGISNPLVNWKIFDKSVLETIVRCMGEEAIRKLLQLMLPDLRQMRSGFPDLFVVMPDDTFEFIEVKGPTDQVRPNQHIWLQALASMELPVSVLKYKAVA | Function: Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Catalytic Activity: Hydrolytically removes 5'-nucleo... |
A0A6L7L150 | MTYAIGIMSGTSVDAVDAVLLEIPPDGNPVLRETATRDFPAELRHTVLGLMTPGENEIDQACRVHVELGKLYAEIALDLVGRAGSVTISVIGCHGQTVRHRPDGPHPFTLQLGSGAVIAGRTGIPTVTDFRSADIAAGGQGAPFAPFFHRAVFSSDMSCRAIVNLGGIANVTLLPRDRSEPVTGFDTGPANCLMDLWTRRHLAKPFDESGAWAAGGALDEHLLGQMLADPYFSRPPPKSTGREYFNEAWLDRALAGSGEPVSPANVQATLAMLTARSISGQLPPAVDALYLCGGGCANPHLRALLGEESGLPVDDTSALG... | Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the... |
A0A2E9NVH6 | MAYYGESHIGRLKTVYRRGLGFRYGRQMQTIAGVHFNLSFSDDFWLWKAALDAHPDESNIRTIRDVGYFRTIRNFRRIQWLIMLLTGSSPSVDESFRLLATDRFRISGRTRIAEGATSLRMSDLGYQSAAQESINICFNELDTYCNTLFNAVHCPWPTYEGLGLKDKNGFKQLNVAVLQIENEYYSSIRPKRIQQPGERPVRALINRGIEYLEVRAIDLNPFAQNGITEYEASLITLLMTASALADSPFNSPEERIAIDRINARASWAGRRTDQRFDERSSLKEVGIQFLATLDPVAESLNHAFQSNSFTGALEDAQLRL... | Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 401
Sequence Mass (Da): 45672
|
A0A1F3ZPR2 | MAALERFLDRAATWLVTLGAILVGMMALHVVLDVGGRYIFNFPLPGTVEFVSYYYMVGVIFGPLAFVQSQRGHFFAEVFTRRLPARAVAALDAACVLITALLLGFLAWRTAAYAWAHTETRSQVQTAYYTIATWPARWMVPLGLGLMALYALVQFVRGLAGRKSRTR | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 167
Sequence Mass (Da): 18581
Location Topology: Multi-pass membrane protein
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A0A2E1J3Z7 | PIAVGRILYKSIKDKDYRLNLSQRFGIYKINPSKKKVIWFHAVSLGEVIASEKIVNKLLENAEVILTVTTPTGLRHARKIYEDRLKICYAPWDSLAFMNRTIHSFKPSAIVIFETEIWPSMVHCSFKKDIPIILCNGRMSQRSFKSYARFKALVKTTLQRFSFIFVQSENQAKRFFELGANIEQLKIASSVKFDSHQLNEEFSNRDHEVEKNKVLLFASTHRGEDERLIKIYKNLKPMIANLRLVIVPRHPERHIEIEQILTKEGVNHSSQNNSKLEFEDNEVIVINAIGILAKLYAKADAAFIGGSMLGDTGGHNIIEP... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A2E8VQ74 | MRSSPVYRLLVAVCAVFIVHTSAAEESGGEALYVKITPGFVINYGAPSINRLKYAKVGMSVRVGDAEASDVVEHHLPALQDSMVMLLSAHPEEGIRTVKGKERIRKEALKRMRELLNREEGAPLIEDVLFENFVVQR | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell inner membrane
Sequence Length: 137
Sequence Mass (Da): 15219
Location Topology: Single-pass membrane protein
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A0A661E200 | QLGLTEDEVLARLETLQAAGLIKRMGVVVKHRALGYRANAMVVWDIPADEVERVGALLADESCVTLCYQRPRRLPAWGYNLFCMIHGRERGSVLRRLEQIVAHHGLEKIPHTVLFSGRSFKQRGAHYVETDNVGAGLPANRVARCTSVSVRGQARSYGSCLNLEDRNDG | Pathway: Porphyrin-containing compound metabolism.
EC: 4.1.1.111
Catalytic Activity: 2 H(+) + siroheme = 12,18-didecarboxysiroheme + 2 CO2
Sequence Length: 169
Sequence Mass (Da): 18780
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