ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A0H3YML1 | MFLILLIFXMISVXFFTLMERKXLGYIQCXSGPNKVGYLGILQPFXXGMKLFMKEQFFPMNSNYLIYMICPLFXXIXSLFMWMVFPFYVNTLEMNLGLLFFLCCSSLGVYGLVICGWSSNSIYSMLGCMRSVSQVISYEVTLSLILLSFFLLVDSYSLLSFYYIQVSLWFCVFSFPLFFSWIXCCMAETNRTPFDFSEGESELVSGFNVEXGGGGFXIXFIXEYXSIIFISLFTXVXXLGXDLNSLXFXFXXXXMCFLFVWVXXTLPRXXXXKXXYLAWXCYXPXSLNYXMXFXLVXLXXXYHFFXXXX | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
A0A7C5VLE3 | KGIKDSLFDAIMIGLIFTITQTLVAFFIGPELVAVLGSSVSLISIVIINHFFRKPNGKLRGIFLSVVNYVILLVLVVLTRLVFNDVLNKYPFVITFDIGGHILKVDYLTTPGTLLLISSIIGAFIQGANFKTISMTLLETLDKIKWSSITIVSIVILAKVMGNTGMIISTAVLIATVSGKFYPIFSPLVGAIGTFITGSDTSSNILFGILQKETAKNLGFDTTWIASSNTSGATAGKMISPQSIAVASSAVGLQGLEKQIISTTLPICLVYSLILGMYVWIVSLLIV | Function: Uptake of L-lactate across the membrane. Can also transport D-lactate and glycolate.
Subcellular Location: Cell membrane
Sequence Length: 287
Sequence Mass (Da): 30713
Location Topology: Multi-pass membrane protein
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F0V8T3 | MVNVNPVDAVGESRTRPGVTVAFVEDIAREAGHTLRKFFSDRDKKVDTKESPADLVTEFDKAIEDHLKKRIREAFPTHQFLCEEQRFLLERKSTQSLTAAELGIQKRIDGTTNFVHTLPFTCVSIAFAVNKEVVVGVVYAPILNEMFSAEKGKGAFLNGERIYTSGRRDPSCAVVCCGFSVGTIRKIDMPGCDLAVKTAARDIERCVLNNLTYCSHNCRDIRHLGSTALELCYVAAGRMDAYQSLGPKEWDFAAGILIVQEAGGCVIDFDGKPLELHQRRAIAGSTEELARSFVGNLMAPGLSTAVDGPGVKTLCSAKKP... | Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2.
EC: 3.1.3.25
Catalytic Activity: a myo-inositol phosphate + H2O = myo-inositol + phosphate
Sequence Length: 342
Sequence Mass (Da): 37341
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B4CVH8 | MICSELHPVAFWIAAGIAAGLAVTPLIFLILDKTGKLKPALRSDLWTRYKSWLVLAPLMVGPLLAGRLAAIIGVGVLSLACYREFARATGMFRYRAISAVVALGILLLTFAAADQWYGFFVALSSLTISLLVIIALFADQPKGYIQRVALGIFAFSLFGVCLGHYGYFANDKDGAGQAFLLAILLCVELNDVFAYCTGKMFGRRKLAPQTSPNKTIGGALGALILTSALFATLVHAIVHGSALDQPVHLVAMGMLLSLTGQWGDLVMSSIKRDLGVKDLGVTIPGHGGLLDRFDSLIFVGPAMFHYVNYFLGLGLDQPVR... | 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: 325
Sequence Mass (... |
A0A1C9P9G4 | TSLSVIIRTELGHPGALXGNDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMXGAPDMAFPRMNNMSFWLLPPSLTLLLSSSLVEAGAGTGWTVYPPLSSTIAHAGSSVDLAIFSLHLAGISSILGAINFITTIINMRAPGMTFDRLPLFVWSVLITAVLLLLSLPVLAG | 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... |
A0A1I8AHM4 | MEVFVYDKWNAKILPPYVQGEILTDVKVEMDESRTQAPPLLNEADLIALMDKYGIGTDATHAEHIETIKKRQYVGMNAENRFIPGYLGLALVDGYNLMGYEMSKPMMRAELEQNLKEICAGRKTKEEVLADQLGKYKRIFTVSEMKVDKLSEAFRNYLSIAGRNNRSINNIPGIDPPPQNGPPNPDGAMDATSARGGATRGRGRGRGRGRGARGGGDAPGRQANPPPAPANDATTKMCKCNQPAVKKKVTKEGPNKGKLFWTCPVGYNQPGNCKFFEWA | Function: Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by... |
A0A1I7ZQX4 | MDGMDIFASHTASIWERIGFEDALVEVCDSIMARRSIPTPLSYVPVVEENDLGTVMSFADRAENIRKYLVSVIVHRYGTDRSSAVFRKHVSPDFPNVRQIASESSLCFVNSDEFLDIAQPILHKTVFVGGLGIGPAKPLQEPYSSLLEKGSKGVVLMSLGTIVPTSSIPIPVRQGIFEAFGNFTDFHFIVKVDKEDTESAALVASIPNVDLVRWMPXXXXLDRPSLSRRTERQMDIMPT | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 239
Sequence Mass (Da): 26518
Location Topology: Single-pass membrane protein
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A0A059WYP7 | MISIFVAMTKNRVIGEKDQLPWRLSSDLKRFKELTTGHPVIMGRQTYESLPIKFRPLPNRTNIVLTRNKDFDAPECIVAHSLAQGIEEAKLHNGSDEIFIMGGGQIYEQALPLTDRIYLTEVETTAQKGDTFFPKLHKNDWYIKKAGGFEQDEKNQYAATFYIYDRKETND | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tet... |
A0A257AEF0 | MHFNILKHDLVPYHSILSPKEAKKILEAYKINKDQLPKMLVTDPVARAIGARVGDIVKIIRKSPTAGESVAYRLVVGSPQE | 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: 81
Sequence Mass (Da): ... |
A0A2P0QMR9 | MEYKASVNKLTQPLVTYLIDNADKLRVNVETMANGCTLVDAGIKVPGGLEAGRIIAEICLGGMGTV | Pathway: One-carbon metabolism; formaldehyde degradation; formate from formaldehyde (H(4)MPT route): step 3/5.
Function: Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl-H(4)MPT.
Catalytic Activity: 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = H(+) + N(5)-formyl-5,6,7,8-tetrahydromethanopterin
EC: 3... |
A0A1I7Z2D2 | MFRTTLAMSFVDMWPPFLAPPTCTETGCMVISLAMRLWSVAVALLAVLLLSSSVQSKATGKDYTQYVCKGCEAAVKGFQFLFGKEATQDKVIQLLAFICKYFLDEKSAVCKAMGGQFRDQIIFVIGELIVQPTQLCGFISSECGDFHNPFHANWTIKLPKPPKCNLPQSSLIFPLPDIDYPKEPSSTLRVLQLSDLHFDMEYVPGSEADCDNNICCQSDSSEGRVNMGSYMQPINDKLQLITLNTGYCMNTNLSRQHDELVRXXXXEGVPVNSFAPHYAPKEAQPTWLYDAVSKAEQKWLDYEALKNLEFRGSYIVKIND... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Converts sphingomyelin to ceramide.
EC: 3.1.4.12
Catalytic Activity: a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine
Subcellular Location: Secreted
Sequence Length: 611
Sequence Mass (Da): 70065
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A0A151EVE6 | MIIKRGYILQNGIRKRDIRIEGNEITEIGKDLKGSDIIDASHHLIMPGFVNTHTHLAMTLLRGYADDVPLQEWLRDYVWPKEMKLTPKDCYYGNLLGIIEMIKSGTTCFNDMYFYEDQAVKAAKESGIRAVLSAGMADMGNLKRAEFQLKKSVEFAQTVRKEHLVKAAFGPHSPYACSFNFLSKIQEQAQKLKIPVHIHLHETAEEIRQFQKRHGKTPIEMLDSIGFLASNICAAHVVHTTEKELDILKTRNVKVLHCPSSNLKLANGIAPIAQMVKKGICVSLGTDGAASNNTLDLCAEMRLMALLQKIENPGAMNAET... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
EC: 3.5.4.28
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S... |
A0A4R1FAS1 | MSNKIIKAGFALFTLSSLLFASSSFARPNTFSCAAGNTISKTFSSGAAWDLCWEVRDEEGVVLSDIHYKAANSTRRKVIGEMSLSQIQTEYDDDSADQFLVTDFGLGGNSLQTLNTSMCEGGQLHEYAGRNVLCEVSSANGYIYRYRDNIRRQGSKLEILSASNINSREFIIRSTFLENGTIETGVGITGQFTKTTTDSNAGWPVTSQNKLSTSFTDHFFWRLDFDIGSSNSNDVVEQIKSVPSSDRLTKTKQTQTISSELAASFTPADKKFWRIKDQSETNNANQPVSYEMVLLNYAQQSKGNSSSPWLKNDVYITAYN... | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 392
Sequence Mass (Da): 43679
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A0A513Q872 | MANRRNRRNFQKRRPRGPRTPAETSTVTTTVSTNGQTKPTTKTTTVKTTKTAPRQQNNRQVRNFVRQELRKRVDGPKAAITQTATLTLGTLGTNGSGNLEIEGVAHLNPLLIKEKTAAAGAGPIQALASQYAMWRCLSLRVILVPTVGASAVSGTVARTSLNQPGAPAQTTWSGLGARKHVDATPGRRVEFRLGRRDLQGPRDGWWYTDTSNGVQNSAGPTIEIHSYGKTVSTFQATAWSGELWLVELRATWQFTNWNMNPKLLNLVDTTIPHGNIKLSSSAAGAPVVLTVEKAANAPLETQHAQNPHVTGSPSVSEVIW... | PTM: Specific enzymatic cleavages in vivo yield mature protein(s). VP90 undergoes a cascade of proteolytic cleavages presumably mediated by host caspases and extracellular proteases.
Function: The capsid polyprotein VP90 self-assembles and undergoes a proteolytic cleavage by host caspases to yield the VP70 virions. Thi... |
A0A060C2F5 | MPNVNFEVYAPSFLERFIESHAVMLQGNAGLKPKEGEITSRPWQWPINYRVNIS | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Locatio... |
A0A7V3RKP2 | MEAFVELIENKIRESIEIKQKILSDKKILSDIEKAAKMIIHCYRINNGRVFFAGNGGSAADAQHLAAELVSKFYMEREALPAEALSTNTSILTAIGNDYSFDRVFSRQLEANAKKGDVFVGISTSGNAQNIIEALSICKMIGVKSIGLTGETGGNMTGLCDLLIKVPSIDTPRVQESHIMIGHIICEIVEKSLFGNKK | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1.
Function: Catalyzes the isomerization of sedoheptulose 7-ph... |
A0A059WZM1 | MRKQSFLRLSFGESTLRSAGVTDWLQVAKPDVVFETTSLNHETGQPAIDYLTAALKFGAHAITANKGAIVHGYDELNELAKASHRSFLFESTVLDSAPVFSLFRETLPAVKLRGFTGLFNSTANVILESMEAGRTFDEGVKTAQELGIAETDP | 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: 153
Sequence Mass (Da): 16652
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A0A1I7YLE5 | MLFQRISTRFCFRSALGLRTGYRTASSNTLANTLKKMKEQNQPINPLYVLSNTSPIVKLDCDEAFKSLTEKQKLYAHHISRASFLGSLATFAQVSRESLGIFVVLHRIFEANSPEMLQAKATQIGFTDEEYQAFLIYAVGFFANSGNYKGFGDTKFIPNLPKDKFRSLVAISEDDTTLGSRVPLMSLYNRIEHNLYSISNFVATLGFNDEHITTYHSGFVTKTDCDIADRYMKSRRMEAFNTRLQKTVEDGKPEYTIWVASEKQKETETTEFEGVTFRVKYGDHSDAMMLAVCELEKAKQYADNEIQRGMIGKYIDSFKY... | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.14.4
Catalytic Activity: Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.
Sequence Length: 751
Sequence Mass (Da): 85617
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A0A660T952 | MNNFHTHTWRCKHASGTVQDYVDAAKKNDMKILGMSDHTPLPDNRWSHVRMDFSELDAYEEEFKKVETDDITILKGLECEWDPIYQGFYSDNLLGERNFDFLIGAVHYIKIDNEWSYLGEIRTAKDLSQYAKILIETMRTGLFSFIAHPDGFGAGYLEWDSNAEACAIDILTAAEELSIPLEINGYGLRKPKILNLKGSRNVYPLLDFWELASKFDITAICNSDAHRPEDVDASLKECRAIADRFNIKVIDDIRK | 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: 255
Sequence Mass (Da): 29267
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A0A0X9L4R5 | IKHYGGVENSDYPKVQEVVNQFIAGTLDKITAGAKKAASDATDRAVIGGVVKSNAGTSVDATSVNALVKGIKEIVDLVIKEGNGQADKITPVDYDKKKIDKLFGATTDAAQGAEDKHVAAAASASIGVV | 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: 129
Sequence Mass (Da): 13211
Location To... |
K2CYW1 | MQKYKKYFYWYILPLFFSLSPLILIYSLNLFAQPFNLYLLLLPSVAVSSYFGGLKGGILATTLTSLGMNYLFIVPNFTSLEIPQVLNLTFYILECIAVTVFITQGYHSELLQNYKTKAENLSKKLIKIQEDLTSAQSEIKLRDEFLSMASHELKTPLTSMLLQIQSALHNIKNVSLANFSVANLLKMLESVETQTERLSKMINDLLNVSLITTGKLELEKENFDLSKTVREVVNRFVEKLEKEGYTLSLEADKEILGNWDKLRIEQVITNLLTNAIKYGDKKPIEVRVINFNKSGKIHVKDQGIGIPAELQKKIFEKFER... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 368
Sequence Mass (Da): 41687
Location Topology: Multi-pass membrane protein
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A0A1I7Z6Q3 | MRFCSISVLIRSFSHPLPASSMSPIPILSSFFSAIQSFPLPEMITDVQLGVMANVLGIGMFLLVVLFHYITANNARRGVSNTAGPN | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
A0A2T5Y4E1 | MLIVGQHGEGYPTIQEAVHAVRDFYESPVTIFVHKGIYHEKLNIPSWKHFIHIVGEDRDSTIITNDDYSGKRNVQNEFLTPFNTYTSYTVLVAGNDCVIENLTIQNTAGEKGQAVALHIDADRTHIRNCNILGWQDTFYLARAGSRNFIDQCFISGSTDFIFGAATAVFSKCTIESLKNSYITAPSNSQDHPYGFVFLNCDLRAKNEQVNQVYLGRPWRSNAKVLFYACNLGSHIVAEGWDPWNGDTMFPDKYKTAVFLEINCRGEGFKQLSKRVPWSKQILNNNYKQPSLSSIFTDWKPTENSN | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
EC: 3.1.1.11
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Length: 305
Sequence Mass (Da): 34615
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A0A924IN21 | MRPLTGKRVLITRAHPGAETLANRLTALGAEVVLAPTIAIEPIADPAPLFAQVARLTAADWVVITSPTAARLWALCTGTVTVPARLAAIGEATAAELRSQGLPVAFTGARATGAALASSLLSLGPTGRFLLPRSDKAVADLPIKLRSAGADVIECDLYRTVSRPWTADEVRAVGAGVDAVTVMSPSALDGLLSQPGVTLWLSRARLVAMGPTTASAVTARLGRPDAVADPPSIEALIASLCAVLGHTGG | 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... |
A0A7C4N204 | MNIQTIVTLFDWRSLIDIPILSFIVFLFYTTLRSSGSWRIGLGIIVALLFYLVARFIRLPGVEWIFNNVSNIALIALIVIFQPEIRKIFERAASAFKVKKLLKESSGFINEITKAAFVLAGRRWGAIIVIPGKDDVANKINGGIIINAEISVPLIMSIFDPHSPGHDGAILVENGKIVGFGYRLPLSSSEKLDYQFGTRHHASLGLSEMCDALIITVSEERGTVSIFHSGSYMQVDNEEKLESEIKSHLQNLSFLFPVSSKQRSRSIRLAEAFLSLVVGCCIWLAIAINASQVIHRTYTIPLQYNLPSKMVIIGEKPQTV... | Function: Catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP), a second messenger used to regulate differing processes in different bacteria.
EC: 2.7.7.85
Catalytic Activity: 2 ATP = 3',3'-c-di-AMP + 2 diphosphate
Sequence Length: 478
Sequence Mass (Da): 53311
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J8IW48 | MKIKKNNKGIKFLACLLVSLCIINYSSISFAETQTGNANDATKNASGIDTGIASLKYDSRDILAINGDRVESFVPKESINSNGKFVVVEREKKSLTTSPVDISIIDSVANRTYPGAVQLANKAFADNQPSLLVAKRKPLNISIDLPGMRKENTITVPNPTYGNVSGAVDDLVSTWNEKYSTTHTLPARMQYAESMVYSKSQIASALNVNAKYLDNGLNIDFNAIANGEKKVMVAAYKQIFYTVSAELPNNPSDLFDNSVTFSELTRKGVSNAAPPVMVSHVAYGRTIYVKLETTSKSKDV | Function: A cholesterol-dependent toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol is require... |
A0A0D9ZLV1 | MAECAWWGEVGMSEVSASSTAAVGRVGKHWLALRSGANLFMHSLELDELEKSVVKSWRKGANPLPPRCTVVVIRFRGESRVFGEGNGVVTPLHVPASGYPMMSMDEQTSLSFALFKDAAFNASIRRRGVRATRLRPSGGKPCFSTEGTANFYMHPIEGLTVLVDMDTTEVLHVSDRDAGIPIPTTANTDYRHGHSTPSPCSSADTQRELDSRSGGLPLPLLLLLLALPPAAAVELAPAPLVPSSPTHPPARTAMVGDPSPWRGQ | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 264
Sequence Mass (Da): 28289
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K2AWC6 | MQKIAVYTLHTDLKTAAKALAKKLQLPYTKEALYWILLTPEYLGLQKVSEKLAPLYIDFSSGKMAYRQQHASIREETLAKALGLKHGKERYIIDATAGLARDSFIIAALGFKVELIERSPIISALIEDAFKRARNHPHIAPIIERMHLVTGDAITLLANRSERPDIIYLDPMFPLRKKSALPKKDMQIFHDVIGPDEDTDELLKTALACAKDRVVVKRARLSSELGRIKPSFALSGTSSRFDIYLLRPHGHPALFNSICSAP | 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: 262
Sequence Mass (Da): 29367... |
K2B6W9 | MAKILDGKIVRDKIARKLKSEISRLRSKCKLVILQVGDLSESNAYIRQKILFGQKIGCLVEHQKFDEKISQAELISQLSILNSQFDVTGIIVQLPIPIHLDKDAIIDAIDPKKDVDGLTSTNLKLLWENKSEGYLPATTKGILTLCDFYKIPTGAKKVVVVGRSFLVGKPTALAFLNHDATVTVCHKETRNLKAETRNADILVVAVGKPNLITKDHVKPGQVVIDVGINVVNGQHPRGEIKTKPGEHPGGEKGLSKPETEPSNRRIVGDVDFDNVSKIVQAITPVPGGIGPMTVASLFENLLEAYKRQT | Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate +... |
K2AGZ9 | MLTDVHDIAQAREAATVVDVIQIPAFLCRQTDLLLAAGDTGAVVNIKKGQFLAPWDMANVADKVASTGNDNILLTERGVSFGYNTLVADMRSLPIMARSGYPVIMDATHSVQQPG | Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
EC: 2.5.1.55
Subcellular Location: Cytoplasm
Sequence Length: 115
Sequence Mass (Da): 12285
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K2EA30 | MTKNLFYKSSILASKLIGYTSKYLNLGAGTNFPGKIARLIAPDVLSYLVNQSRREIIVVTGTNGKTTTAGFVANILTKDNRKVAHNRKGANMLTGLTTSITQESKLNGQLDVDHCVLEIDEAFFFKAVDEFNPELLLVTNLFRDQLDRYGELDTTAKKIQSAIDKTIKKKPLKVALNADDPMVSALAQDDSIKKVYYGFSEVNFVNQDQTVKSPQEVAACSCGGKYNYSKIFYGHLGHYSCTCGKTRPELDVSTVAYIDVNSSTLTITVKNKESFSVNIKMPGLYNAYNALAAITLCLELNISPVTIIDGLENYSTIFGR... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The MurT subunit catalyzes the ATP-dependent amidation of D-glutamate residue of lipid II, converting it to an isogluta... |
K1XCA8 | MIKILIADDSPFIRKVLRQIYKDSEEFQIVGEASNGSDAIDLVKILRPDILILDLEMPVLNGFEALKVIMKEAPLPVIIFSSFNLKGAEQTIKALEFGAIDYLTKPFASYDKIDVITKDLSAKIKNIVKSFRQSVKNQNSKSDKKSNLIIGNCHNVNSRKIDLIVFGASTGGVQAASNILPQFSGKTCPIVWVQHMPQNFTATFAERLNDISELNVKEAIDNEPLKKGYCYIAPGGKHIEIRNNSGRFSLHTFIGDEICTNKPSINVMFYSVSEHFSNNAIGVVLTGMGNDGAKGILAMHKAGAFTIGQNKETSVIYGMP... | PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate resi... |
K1XAZ4 | MKKLITLFFVLFLNFSVFSNPVAEVETSMGKFKIILYMDKAPKTALNFINLCKKNFYDGIVFHRIIKGFMNQTGDPTGTGMGGPGYSFEDEFHPDLKHSKPGIVSMANSGPNTNGSQFFITSAPTPHLDNRHSVFGEVIEGLDICDKINSVKTDSNDRPVNPVSIIKITLIGTEPPIVDEELLNYFKKVSEPCIKTSLEVSNLKSNNINLRAVHTRNNRYLAIWDITCEDNTKLAFWIKGAKTDAGFIFDELHTNFIKEK | 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: 260
Sequence Mass (Da): 29189
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A0A3L9LT91 | MCLPTCAQEIPRVNHKRDIKVSGAQERVSGLELFVRRLKCLGIIVIEKYAMNKLEIHGRSVQIFAWILGLSDIEYPIGRQRPVISFLYLMFLMGILTYNLKSVIGHIEINISGSTLSEELIRLLFIVGTGISYYILGSVWLFKKDESECLRQLNEVTECIASISSDTDFKDIKRNKMIQIISWITCVYYMAHFFIKYISDSESLSSFSNIFCINYESFLILYINLMFVNYIRIIQLNFAKMNKRLKELTAFTDCSSSISVYEIIKDISRIKQLHIRLTRVSRSFNDFYGIYTLLSITLRFGTMTFHLYNIYCTLYNVQSD... | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 428
Sequence Mass (Da): 49546
Location Topology: Multi-pass membrane protein
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A0A3L9LY67 | MCIVRELKLFLQLTKLFGFTPYSLEKIELPIQKYAVAYSLFCAGFYGFVIYQRSIEVSLGDVDKLFVLMIIRTILANVALWNDILFGIFYRTKLVIAFQKIWRYDLETRTALDKRVVRYSWTVIFFIFFNDVCISFLTYFSETQKPGLVVVLYNMIYVPMSFSIFKFTLIVYAIQRRLQRLNKMVSAGMPTKNFVNFYLLYIFAIGILFFLTGMRSVIAEINIGCPRVSMKDVRWLHSCLISAIKDVNSLYQLPLFLWIVTLTFNITSRIYSIGQNSASLLLILRECNMILFCTVLLITVITICHVTACEANKTGCIMFS... | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 387
Sequence Mass (Da): 44317
Location Topology: Multi-pass membrane protein
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A0A1M7L9L2 | MEAELVYKIKASLGEGPCWDTRNNILYWTDIAGNVIHQFDPVTKRNKTFSIGQMVGAVVVAEDGRLVLAAEHGFYYFDITTNELVEISDPEKGNLDNRFNDGKVDPAGRFWAGTMQKNDTQPRGALYCLFADHHIEEKLSGLRISNGIAWDLEKSRMYFIDTPTGNIYVFHYQKETGVITNQRVAFPFPEEYGSPDGMTIDSEGMLWIAGWGSGQVTRWDPSTGKVLLTIKLAAKNITSCTFGGKDLDTLYITTARIGMTDQELENLPLSGSLFSVKPGVKGVPAYYFANKP | Catalytic Activity: D-glucono-1,5-lactone + H2O = D-gluconate + H(+)
EC: 3.1.1.17
Subcellular Location: Cytoplasm
Sequence Length: 292
Sequence Mass (Da): 32501
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A0A3B9P3M1 | MDYLSFEKPIEELENQLTKALELANETGVDMAKTITDIQQKLDNAKKEIYNNLSAWERVQLSRHPQRPYTMAYINALTQGDFIEMHGDRGVKDDKAMVGGWGTIDGKSYMFIGQQKGVNTKMRQYRNFGMANPEG | Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
EC: 2.1.3.15
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Length: 135
Sequence Mass (Da): 15425
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F7XKQ0 | MMDIEEIDAIDAVIIGGVGFTNFSGSTDIAENIHLREIETPYGTAAAYLFHLDNKYVALIPRHYGKKHIPPHKINYRANIWAVKELGCKRIISTNSVGSMKDHKPGSFVIVNDFIDFTRNRACTFYEEETVHLDMTYPYCDELIKAIEKSCQDLDIEYTEGIYVCTEGPRFETRAEVSMLKQFGDVVGMTGVPEVILAKELNLCYASICTVTNYASGIGEHKLTVDEVLEYLDKSKHELYNILIQTLSHLPEERHCNCKMSMDGAHI | Pathway: Purine metabolism; purine nucleoside salvage.
Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioinosine (MTI) to hypoxanthine and 5-methylthioribose-1-phosphate. Involved in the breakdown of S-methyl-5'-thioadenosine (MTA), a major by-product of polyamine biosynthesis. Catabolism of (MTA) o... |
A0A256LP02 | LDGYPRNLEQAEYLSEITDLDAVIHLDVDEEVLVDRLTGRRVCDDCGANFHVDFQPPEEAGVCDECGGELIQREDDTEETARERLQVFYDNTEPVIEHFRDEGDLVEVDGEAAPDEVFARIREVLDE | Catalytic Activity: AMP + ATP = 2 ADP
EC: 2.7.4.3
Subcellular Location: Cytoplasm
Sequence Length: 127
Sequence Mass (Da): 14470
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A0A924ILP6 | METAAAHTTTYAVLLQNLAFYTLASFSVLSAAGMLLVRNLIHSAYLLVLTFLSVAGTFFLLNAEFLGVAQILIYASAVAIMMIFGLMLTNKPAAPMPNHGILFRYIAMAIGIGIFSYACRLALIAPWVTSTPVLVDTPVVIGRAFFNEFLLPFEVAAVLLLMALVGALSVARKEA | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy i... |
A0A7G9G8C2 | MKENGEEYNKIITIPNMMSFFRLALLPVFACIYLNAKTVRGYQAAALVLFISALTDMLDGRIARKFHMISRLGKALDPIADKLTHIVVVFCLCSRYRQVWILLIILAVKESFMGIMGIIYLRKGRMLDGAHFFGKVCTTVLFAVLLVLVFLPQLSVLWVNVLAAAACAACLVTWALYIPVFWKMKDK | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Function: This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycer... |
A0A2M8UFK8 | MLPVLLLTVVIDLIGFGLILPLLPFYATSFGASPVTIAMLAAVFSIAQFLSATPLGGLSDRMGRRPVFLACMALTVIGYIWLAFADSLLTIFLARTVAGIGSGKISIARAIIADSTPPEQRARGMGLIGGAFGIGMILGPLIGGLLVGPDPQHPNYTLPALAAATSSGIALLLAIFTVRETRPNASHTLAGLALWRNPFAPLRQLNRVVVALIAINFSINFVFSQIEVLFPLFSAARLDWHAYEVGIAFTFIGTIVLSMQGFLIGPLTRLFGERKLLTMGMINLAAGTAMAHWIVSTPTMAFSIVLTATGVAMIGPTINS... | Function: Resistance to tetracycline by an active tetracycline efflux. This is an energy-dependent process that decreases the accumulation of the antibiotic in whole cells. This protein functions as a metal-tetracycline/H(+) antiporter.
Subcellular Location: Membrane
Sequence Length: 390
Sequence Mass (Da): 41337
Locat... |
A0A2N2F4S3 | MSSNIVCPSAPKRILLKITGKLFTGPDGKTADATAVRALIPQLAVLAKSHCVGIVIGGGNFFRGSQQGTALGITPSVGHQVGMLATLMNGLMLQDLLAQQGLTSTLLSALPCPTVGHCICPQAINQALTRGDIILFGGGTGAPYVTTDTNAVIRGLQMDADQVWKCTDVDGVYSVDPKKNPLAERFATISYEKALALHVGVIDQTALIIAQQNDLPIRLFSIQEPEALLRAAQEPQFGTLISNQE | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
EC: 2.7.4.22
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Length: 245
Sequence Mass (Da): 25815
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A0A1I7YUD0 | MVPLSEGFSSAQSTNIPSPCLLLGAFRQQRPKAMANISAADVEWLCPSLKLPADVVKLDLQDLLKYPECAGMPTFLAGGSLSELDEGIYAMHTRILMTFIFACLSIVGIVGNVLVITVVFKVPGMITPTNCYLVSLALSDCLFFIAATPTELSTLHLPSDYIFGSIGCSLFSYLPYLAINTSSLSIAAFTIERFIGICYPIQARYICTVKRAKMIIAGIWSFCIMYNSPWLYLATVKEDEEGSMCGFKLERDNWTYKTIFFGDFFAFYVFPMFLYMIIYGKIAFTLKKNDIRHQVTKKSHSNN | Function: Receptor for thyrotropin-releasing hormone (TRH). Upon ligand binding, this G-protein-coupled receptor triggers activation of the phosphatidylinositol (IP3)-calcium-protein kinase C (PKC) pathway.
Subcellular Location: Cell membrane
Sequence Length: 303
Sequence Mass (Da): 33824
Location Topology: Multi-pass ... |
A0A1I7YYE3 | MTVTYSLDVSSSTFLGIHKLLFRWKGSIWKSTYPELLLWLFLYTILSMTYRYVLDQEQQTTFEDLAAFFYTYGDYIPITFMLGFYVSAVFARWGEIFNNLGWIDSPALLIATYMRGADDTARMMRRNVLRYLVLTQALVYRDVSTTVRKRFPTLNHLVTAGIMTENELKEFDKIVSPHIKYWQPMQWAFTLIRKARDARIIDNDIIYADLLEKLRQYRVQVLNLTLYDWVPVPLVYTQVVNLAVRSYFIIALMGRQYLITDRNIPNARSIDLKVPIMTILQFLFYVGWIKVAEVLLNPLGEDDDDFETNYIIDRNLQVGY... | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 730
Sequence Mass (Da): 83638
Location Topology: Multi-pass membrane protein
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A0A059WSW0 | MIMSEIIESKIIRPEIVRPEIIGIAAVAANGVIGARNDIPWRIPADWQRFKALTMGNVLIMGRKTYDSIGRPLPGRTTFVITRDRMWRCNGVRAVPSVEEAIDQAILLDSQKIFVAGGGEIYRAAWNRLNGLEITEVDQYPQGDVRFPDISPDDWIETRRERHEGYSFVSYSRRSRRESTL | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tet... |
A0A059X004 | MKKLNVAIVVAMDKNRLIGKSGDLPWNIPEDRKRFKDLTMGHAVIMGRKTFESILKYIHKPLPGRTNIIVTRDQSYTADGCIVCHTLEDALKKATKIEEQNPNPEVHIGGGAELYKQVLPFVDKLYLSIVEGDYQGDAYFPDYSMFKKVVRNEQKTSNGYLYTILDLER | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tet... |
K8Z927 | MRSCGVIVEYNPFHQGHAYHLQKAKEKSGADCCIAVMSGNFVQRGEPAILDKWTRTKLALEAGADLVIELPWFGAVQPADYFGSMAVQLLSALQVDAFCFGTEKENEFSYMDFVKKEKAHQKELDQRIQQLNCEHPEWSYPKKMAEAYREIFPEEYKDMDQSNHLLGLAYARANLQLERPLELLTIERKGSQHREKELTSFASGTAIRKAVQQKDWTELKNYVPIATYQALKEGPCHRWEDYWAQLQGIGLSLSSSQWKQLYEVHDGLEERLQKSFYEANSFSEWKESLSCAHLTQAKIQRLATYILTQTTKEEVTYAWN... | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine... |
K2BTJ6 | MLAGKQFNIPVVGTMAHSWIMAFDDELTAFQEYARLMPDNVILLVDTYDTMTGVDHAITIGKKLKGIRLDSGDLLSLSKMAREKLNQAGLYDTQIFASGDLTEDRLIDLKSCDAPINGWGVGTHLSTAYEQPALDMVYKLGAIEKNARWQYKMKCTDNHIKTSDPGILQVKRFYDGKKWLRDLIYHVDLGIAQSELNLAEKSQDLLIPIFKNGTLIYSRPSLSDSRNFCREQVKAFNASKAVSYSVQRDQQLIILKKQCMDSAQ | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.
EC: 6.3.4.21
Catalytic Activity: 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate
Sequence Length: 264
Sequence Mass (Da): 29763
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A0A1I7YGV5 | MVCLVDLDLSVDIIVTFSWPPSSPMAFIRRRRSHVLAALCFIVLFCFLFMSTHFRGANEGEGGYGVNIRREDLSEDERTEYDKGFKNNAFNQYVSDRISLRRSLSSPPRQCRYEKYPKNLPKTSIIICFHNEAWSTLLRSVHSVLDRSPLHLVSEILLVDDFSDAAHLKKPLDEYMAQFEKVRIIRLGRREGLIRARLVGASRATGTVLTFLDSHIECMEGWLEPLLARIKQSSKNVASPVIDTINSINLEYGFASTSLYGGFDWNLNFKWYKAPDRVLDARERKIDPLPTPTIAGGLFSIDKRFFYTLGAYDPDFETWG... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 573
Sequence Mass (Da): 66156
Location Topology: Single-pass type II membrane protein
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A0A1I7Y928 | MLREEVMLYNDVIETTIPDTYNYTAFKVHAGYNLHVRHCSDVRFVLRADDDIITLPDRFVHFIDTGYFGNEDKAIYGIILKGGKPFREPESKWYIPKEYYSPDDYPPYINGPAYLMTQNSTKAILDKTNETTFFWIEDVLFTGXXXXIYGIILKGGKPFRDPNSKWYIPKEYYSPDDYPPYINGPAYLMTQNSTKAILDKTNETTFFWIEDVLFTGXXXXPSKNCGLDDIVVENNLLSEQLSVDYVFWKSHDKKDERVFVLNQSNKLLISAQISKNWRETVHSRRRTDPAQFEPTHVGTDPARAGSN | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 307
Sequence Mass (Da): 35588
Location Topology: Single-pass type II membrane protein
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A0A0D9ZXR0 | MEEQFILRVPPSVAERIERLMNESAAASSSSNPEDASLDLSFSEDGRNGTFMIGNESFPASLLDLPTVVESYKTYDDSVLIKTADIGQMIMVREEEDPAPEGVEYKHGLTPPMRDARRRRFRREPDLNAELVHRVEKDLISIMHGNASAILRAGEGGDRKKAGPAPATKPNVKQPAANGEEAEAERSDSDESVDPQVYVLDRCLPGFGYPSQIDIYIYIYIYIXGHDPGAYALWHWHLIDVFVYFSHYLVTLPPPCWVNAAHLHGVKVLGTFITEWEKGAEICEEMLATEASAQMYAERLTELAAYLGFDGWLINIEVKL... | Catalytic Activity: an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-[protein]
EC: 3.2.1.96
Sub... |
S4GJB6 | VRIDSGDLCVMARRVRAQLDALGAKNTKITVTNDLDEYALASLQNAPVDSYGIGTMLVTGSGAPTCAMVYKLTEREGADGVMQPVAKKSKNKATVPGRKLAYRSYDFSVDVNGGVASNGVADCEHVISGSESALATFKPQDSWEDLLVDYVQNGEFNTEFMGHDAIMRAQDYCAKALSRLPISAQSLMRGDPAIPTEINVLG | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.
EC: 6.3.4.21
Catalytic Activity: 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate
Sequence Length: 202
Sequence Mass (Da): 21611
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A0A385PPC2 | YARGCQLLLLGVFTIFYVMFTWWRDVILEASFEGQHTLAVQDGLRLGMILFIVSEIMFFFAFFWAFFTSSLAPVFNIGGVCPPMGLDLINPWVFPLLTPILSLSSGGTFTWGHHRIARGWSDPCITAFHLPLILATCQPSFTALACVEAPFSTSESLYGSAVVKATGFPRVQALGGTDFLFVREERP | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
F0V8I8 | MTVISACIMSRQKPLLARQFVEISKVRIEGLMNAFLKLVEHAGADHTYVESDCARYVYQPLDNVYLVLITTKHSNILEDLQTLRVFATIVQDACSGEGLSGGVNVEQVVLENAFSIIFMVDELISFGLREAISLAQIKTFTDMDSHEEKLQRIIQEGKEKEEKERRRQIAQRLDKERAAKAKPPSSGDAPFLASASLFAPTGAPPPSVPSLAAAADYIQMYGGSPEHVSALTSGVLGVGGSGGPDANAGYSSSSGFAGLGASKGMQLGPQRTTPLASLGLDARAPAERQPAVGTTLGAPGTGLVEATRLGAADGADEASA... | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network.
Subcellular Location: Cytoplasm
Sequence Length: 634
Seque... |
B1PJY3 | TLALFNPNMLGDPENFTPANPLATPPHIKPEWYFLFAYAILRSIPNKLGGVLALAASVLVLFLIPLLHVSKQRSMTFRPLSQILFWTLVTDLLILTWVGSQPAEHPFIIIGQLASLAYFTIILILFPIASALENKMLNP | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membra... |
A0A7C5MN51 | MKRILVINGPNLNMLGVREVDIYGKRDLDWINQKMSELAATLGITLDFFQSNCEGEIITKIQEGMNYDGIIINPGGFSHTSVAILDAIRSIDKPVIEVHLTNIFAREDFRNTVITGRGAKGIITGLGYISYLSALYSFYLLFKEEE | 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: 146
Sequenc... |
A0A1I8AKX9 | MSNKFEAVLLLQVSMMLLDIGFNTAEIVLSQHSSILLMLYILQDTNILMTLIVMLISFSSTFVFQAGLISLLLRRFTPTIIVSLLYLALTVAFHIVSLRLDVNKPAGNLWDVGITVLSVLQKLRSFLLLLLQTNVSFALRSPIPSRQCMAAIEDSAFRHDRASRTTIKTLCALSVSVNRNGFQIGETSHSEDVLEDVDVANCPSKNLVLAHLSVHGKRGDHHAKLNNKGCWTQVQLRTLIVPGRKHGSPGCGAFFPGRSVRRQRPTTCQTAW | Function: Required for ciliogenesis.
Subcellular Location: Membrane
Sequence Length: 272
Sequence Mass (Da): 30150
Location Topology: Multi-pass membrane protein
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A0A3L9LU15 | MILLTDIKPLFYINLLFGNPPHVIFNNSFAITKLGSICSLLWSSVFLCYGYKKTLYIVNDANEIRSLILKVFRLFLVLLCIFNNVVVGYYSHKKLCCVTDNLRSYDLATKIGHTGNRRIRYTMWTLVTVRIICCIIVGYTYHLYHEHDFLILFRMIEVACFFLQIDKFMGIVLLLYSRFRHLNELLLTNDVRVNVHVRSDRGLRLQDAWWLHNCLMDAAEILNSTYSMQLLFWITTITVNITSRIYIISEAWSDEYISKFQDKFFTVYDIITLVTLTTICHVTADQANKSGPTIFSSSLAPSRKFGFATENIEVGMYFKL... | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 355
Sequence Mass (Da): 40975
Location Topology: Multi-pass membrane protein
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A0A9E7EVZ2 | MALDPRANNFDLMYQQVKAPEEGVAIEKPIYIHLTGLPEPRELIQPSKLLVLVRRTAPNVSFHCVSFGDNGFELLVLREWSLLDFSIYLDISSKVKFAWRIQRDMAEGGHSLESIKAGIEARKPDSDAYIDPQKQHAGAAIEVLPTQLIAGDSEGSWHTRTLASSSFMAQRLANSSEVVCQESVSEMDGEFDRSDELIYVERHPSNQSTNRW | Pathway: Carbohydrate biosynthesis; Calvin cycle.
EC: 2.7.1.19
Catalytic Activity: ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate + H(+)
Sequence Length: 212
Sequence Mass (Da): 23847
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A0A841QXX2 | MSAATEVVGIVAEYNPLHQGHVAQIKAVRKAFGDAPIVIALTGAFVQRGEPAVADPWTRARWALHAGADLVVELPAIFALRSAEHFAAGGVRLLHAVGVTTLVCGAENPDLAALKKLADGPNPTALQTALAQGLSYPAAMEAAFAATDPDIAPLLRTPNNILAAGYLRAIERYAPSLCLAPLLRERSDSAEGIAGISGSAVRARLQEGLVPRDMLPAYTYDDLSEALRAGVFPQPERYELLALQALRLLTPATLAQLGEFSEGLEDRWYAARNAATLAELWNDVKTKRYPQTRLSRLLVQVLLGMRRQDLNDAAKTGPAW... | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine... |
A0A345UJB8 | MHWLLKFFGILIAIIFISGSLFLLIFTRGSFFPHTDAIEPEEGRQPVAELTTVTLGGFEQHLLLRGHDDTKPVLLWLHGGPGTPQMPFAHAFGRELEEHFIVVHWDQRGAGKSNTADFDEASLTFEQQTADALELVHWLRERFGQDRIFLLGHSWGTRVGIALAAEHPELFYAWIGVSQVVDHGRATVMARDWLERRISLEERWTLGEIKIPAMQHDDYRRLAKIVERRGGGTDLPVSELIRIALRAPEYSMRDNLQLLTGMNRGGKPMHAQGIIKPYNLTEQIASLDIPAWFLNGRNDFNTPAALVREFYEQLEAPLKR... | Catalytic Activity: Release of N-terminal proline from a peptide.
EC: 3.4.11.5
Subcellular Location: Cytoplasm
Sequence Length: 359
Sequence Mass (Da): 40882
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A0A3D0PXH2 | MSVLDELVSGAVEDARAREKVVPLDEVKRRAAQAAAPIDASQWLKRPDGIPVIAEIKRASPSKGHLSDIPDPAALAREYEQGGASAISVLTEGRRFLGSLGDFDKVRAAVHIPVLRKDFIV | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 121
Sequence Mass (Da): 13022
|
A0A1L5KW81 | MDDLFAKRKQHIQHYLYDAPCTYSLSVELDITHLLSELKSRGLKLYPALIYGLSRIVNRHEEFRMYLNADQQLCVYHEVHPLYTIFHPESETFSCLWSRNPEDFPAFYQGYLNDLKQYGHCTDFSAKPDAPENVFNISCLPWISFTGFQLNIQGGYTYLLPIFTFGKYHSENGRTLMPLAIQVHHAACDGFHVARLIQELQKWADEFKAPSHI | Function: This enzyme is an effector of chloramphenicol resistance in bacteria.
EC: 2.3.1.28
Catalytic Activity: acetyl-CoA + chloramphenicol = chloramphenicol 3-acetate + CoA
Sequence Length: 213
Sequence Mass (Da): 24840
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A0A6S4QNL8 | MSVEGTEKVSKLLNKALKMELTAVKQYLYNAALLRDWGFDNLAKIEVKEAYEELEHVNKFSDRILFLNKNPKFDGPERIKKVNSVEDIIKCNLSMELDAVKTYKTFIKACLDSKDYGSYKIFLDVLIDEESHVEHLMKQKNLIKTVGIEGFLHAQE | Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
EC: 1.16.3.1
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Le... |
A0A1I5MU33 | MYKNKMSPVNHVLIGLDCLLGRVESAVLGMAILALAAFACANVFGRFVFSESIYFVEELNEFLMVLITFFGLGYVTRNGRHIRMTAIYDQLPAVTKKALMIVIALVTAGIMFALAYFAIEYVAKTASRGRLTPALKVPLYLAYVPVVLGFVITGVQYLLTAWRNLDFTDPDVYVSYRTRDEYEAVELADSSVMDDAGRDKHSPQPCNDARDAVLKEVK | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 218
Sequence Mass (Da): 24268
Location Topology: Multi-pass membrane protein
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A0A345UK64 | MISGLQANGAGSGHSNDLKKQICRHLEKFVTTQRLTRMRQVLDKRTRYVTVVLEDIYQPHNAAAVLRSCECFGVQDVYAVEGRNTFDISSKISRKAHQWLTLHTFKQAEAGDESCFKALKNKGYKIATLTPEAETRLDQLPLNLPLAFVFGTEKEGVSALARNESDFQVQVPMAGFSESFNVSVTVAITLYETMKRLRMPEIESGFPLSLTSAEKEAIWYVWLKNTVKKSQLLEQEFLQNIKRASNPGK | Function: Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA.
EC: 2.1.1.34
Catalytic Activity: guanosine(18) in tRNA + S-adenosyl-L-methionine = 2'-O-methylguanosine(18) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 249
Sequence Mass (Da): 28092
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A0A3G9FT71 | MKTNLKKLSMILLAIILATGFVFISCEDVGLAVEGDGARATTITNSSTGTHDGYDYELWKDNGNVSMTLENGGNFSCQWSNIGNMLCRKGKKFGASQTYSQIGNITIKYDAQFTPGGNSYLCVYGWSKDPLVEYYIIESYGTYKPTGTSKGSVSIDGGTYELYETTRNNQPSIEGTKTFKQFWSVRTSKRTSGTISVTEHFKAWDSKGMKLGKIYEAALTVEGYQSSGNAKITSHTLTVGGSSSGTSTGSTNTSSNNTSSGGTVSSTTTSSGATKVEAENMTKGGKYTGSTSSPFNGVKLYANDDKVSFSQNFANNSHTF... | Pathway: Glycan degradation; xylan degradation.
EC: 3.2.1.8
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Sequence Length: 549
Sequence Mass (Da): 58264
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A0A1Z1N0S2 | GLVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLAAPDMAFPRMNNMSFWLLPPSLTLLISSSIVESGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMKSNGLTFDRMPLFVWSVSITAVLLLLSLRVLAGAITMLLTDRNLNTSFFDPSGGGDPILFQHLF | 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... |
A0A6S4QM32 | MKGPVILIFEDALFEGVRESVQPATSHSNGKKRLRLGEIESAACSLMMRLRPRATTGLVKLVEFGCQFLLIVKNKKRLKAFETELTLHTEQLMGESTSESTGESTSEIALSVKKLLAREGIVFRAILTVEELAAQSFFSKKPLLRSSIQATRFNDPIRFEADILLPETTFLTVFGEESVHWHLHTHNTNNNKNNNNNNNNNANNHTNNNANSNANNNANNNVNSTITANHLDSNSTSIGLGMLEIVQPIEPDIAKTVNDDNDDNNNNNGHWKATSRYILSEKAVTVDTGIDKNNRNVNNSDVNNSNVKDRIQPAEIMKSS... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
EC: 4.2.1.19
Subcellular Location: Cytoplasm
Sequence Length: 547
Sequence Ma... |
A0A059X9M2 | MVGRREWSVWMITLVLAMAENGVIGNKGAIPWRIADDMKRFKALTVGKIVVMGRKTWDSLPRKPLVDRTNIVVTRRTGWSADGAVTASSLDDALNKAANATDVMVIGGGEIYHAALPRADRIELTEVHGAFDGDAHFAFDRASWREDARETHTTPDGLAYSYVTLTRR | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tet... |
A0A1V6DZC7 | MLFHNQVAEMATGEGKTLSAVLAAYLSVLSGRKVHIITANDYLAQRDSIWMKPLFEKLGCSVGLLQTGQPMPERQAAYRCDVLYATASALIFDYLSDNGLIASPEQRLQQGLDFAIVDEADSVLIDEARTPFAISGRKDSDLSLYTTLHKPVREVHKLQADYVGQLEQSVAEMLASGSAEHPELGRKCFLIQQADPNNERLQEWLMESSVRRKLEEFVEKAEGSPLLLAELHNQGFYSINPRDHSIQLSDSCQEQFAKLLGHSLVIPDLPAQIARLEKSAHSDEEKQRRREALSTEMEAIASQLNVINQLIKAYALYRRD... | 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... |
A0A7C3TQ55 | MKQHTFHVIHGPNLNLLGAREPEIYGTLTLEE | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 32
Sequence Mass (Da): 3659
|
A0A127SGS2 | MKLYPAMLYYLATIVNHHPEFRTAINQAGELGIYDEMIPSYTIFHEDTETFSDLWTEYVPNIEEFSRAYENDIQLYGSNHGMIGKPDVPENVFTVSMIPWSTFESFNLNLQKGYSYLIPIFTLGKYYEEDGRIVLPLAVQVHHAVCDGFHICRFVNELQELINS | Function: This enzyme is an effector of chloramphenicol resistance in bacteria.
EC: 2.3.1.28
Catalytic Activity: acetyl-CoA + chloramphenicol = chloramphenicol 3-acetate + CoA
Sequence Length: 164
Sequence Mass (Da): 19043
|
A0A660TG68 | ENIIFRIAVKPTSSISKEQKTVDIQGIEKKIKTEGRHDPCICPRIVPVVEAMTALVVIDMYKRQAALMA | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Length: 69
Sequence Mass (Da): 7723
|
A0A660T305 | MDAFYASVEQEDFPEYRGKPVIIGASPGHRGVVAACSYEARKFGVHSAMPISQAYTRCKAGIYLPVRMKRYLEVSRKIMGVFNDFTPEVTQISVDEAFLNMTGTEKLFGTPEEAAYKIKTRIKATTGLNISIGIAHNRFLAKLASEYKKPNGLYIVSKGEELRFIDSINLGDLWGLGKKTLARLENNNIFTAKDLRAKDKTQLKAVLGNSSGDFLYKIVRGIDPGMYTGEIKNRSVSNEVTFGEDTKDPEVLKLTLMELSYKIIFRTLENEEKGRTVQLKLRYSDFTTITARETQTSPIISAEELYNIANKLLKKKWRKA... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
A0A4D6I7P6 | NCYLSVYALTRNPLVEYHIVESFGTYNPHRGATKKGTVEADHRTYDIFETTRTNAHSIDGTQTFPQYWSVR | Pathway: Glycan degradation; xylan degradation.
EC: 3.2.1.8
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Sequence Length: 71
Sequence Mass (Da): 8226
|
C7S5J0 | GWGQMSFWGATVITNLLSATPYIGPQLVEWIWGGFSVDNATLTRFFTFHFLLPFAIAAAAVLHLMFLHETGSNNPTGLNSNSDKIPFHPFFSYKDLLGALLTTIFLLLLALFMPNLLGDPENFTPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALLFSIMVLMLIPALHTAKQRSLMFRPISQTIFWTTAANIMILTWIGGQPVEDPYITIGQLSSILYFSLLLLLTPTLAILENKLLKL | Cofactor: Binds 2 heme groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a p... |
A0A847YCJ0 | MRCKPLCTVRRFEVRLRVRVCAVVGIGIVGGMLPVPGGMTAAAAEETAETEGIRTAPALTLPFPGFERGDFRWKIGPPVVERPRDDAETTYFSIKDPSVVFFGERWHLFCTVRARPRTHQVEYLSLRDWRDRKPQRTFLDIVDGYYCAPQVFYFRPHRKWYLLYQTVMPDRKPQLQPAFSTNDRVDAPSAWSPPQPLFETSPDNVERWIDFWIICDEERAYLFFTSLDGRFWRASTLLEDFPGGWSRPVIALQADIFEAAHVYRLRQAEAYLAIIEAQGGGRRYYKAFLSDSLDGHWRPLAAERDHPFLGPSNVEFEGEP... | Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
EC: 3.2.1.55
Subcellular Location: Secreted
Sequence Length: 378
Sequence Mass (Da): 43440
|
A0A847YB26 | MMSNILDRIVATKREEIERAKVRVPEAELLRRIENAPPPRDFLGAIRRSESIALIAEVKKASPSKGLIREDFQPVAIAQTYERHGAACISVLTDEPHFQGHLEVLASVREAVSIPLLRKDFILDPYQVLEARAHGADAVLLIAECLDDAMLAALYEAVIHWQMTPLVELYEASNLPRVIALGAPLIGVNNRNLRTFEVDLEHTIRLRAEIPADRSVVGESGIQTHADLRRLAACGVQAVLVGESLMREPDIGAAVDRLLGREPIRPEASPDTSPKASSEASAEA | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 284
Sequence Mass (Da): 31129
|
A0A947VRX5 | MLSFSVTFFITVANLAVLYLVLRKLLWKPLRAFMDDRAERIRRDVDEAASVKRSAEEMRQRYDDLITNADEEAEWVLRDAEDRAAVRSREIVAEAEREAEAALRRAAERSALEVARARDQLAEEIAGIAVAAASVAARKGLDGEAERLAALEFIRELGGTGERSDA | 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: 166
Sequence Mass (Da): 18520
Location Topology: Single-pass membrane protein
|
A0A059WZU7 | MLIIIAAIAANWVIGKDNDLPWYYPEDLEHFKNITTGHPIIMGWNTYVSILSRVHKRTGKAKPLPKRMHFVLTSKKAAVIKIELQKLFPGFDQESFSDQVIFCSSFGEAVQRAEVLDKEVYVIGGEKVFETAIRDANAMEITEIDAEYDGDAFFPKFDKSLWNREVRKRDGFSFVRYTRKKLDA | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tet... |
A0A1I8A9P5 | MSRDDGVVHEEIIVRKYHGASPWAHLFHTLIYVTTLVLPLIIAFLTQGFWRKVELYREQPIVDFDGKSIMLIRGSRENEYVVWSSFHALNEAVESHLSVPLIEKQKFDWDDDGRVDKISIYAEFANVQFPVHSVVWVILLQYRLDQHFLVEVGALVIL | Function: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling.
Subcellular Location: ... |
A0A0D9YH33 | MVFSCADSRVCPTLTFGLQPGEAFTVRNIASMVPAYDKRGQCSIGSAIEYAVVVLKVECIIVIGHSCCGGIKELLSLKEDRPNTFHFVDDWVKIGLAAKKVERENMLLPFDDQCTVLEKEAVNVSLRNLQSYPFVKERLQKGTLKLLGARYDFVYGSFEMWDL | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 163
Sequence Mass (Da): 18291
|
A0A1I8A3H5 | MNYLLQDLSSSFMKGIFRRFQDLTRRSCVDLRQNLSSWCRVKKTSKQKNRPPDLPKEENPNLDQYSNTSLVNQGSLDWCIASSSCLRPTGASLPSPSPSPPSRDLLPAILWVIPGKWTTPTDVPTSCRRRSGNVXXXXFSVHKEKIHIKKPRNRKTAHRTFLTKKIRISTXXXXKQIRISTNTVIHHSSIREVSIGASLRLLVSVQLELHCLPVIYFQDLSGKRFCGEHAIHDPEDQDRIPCPNDPKHTVAKSELEDHLANRCNARISGDPWIVENINIVSQSTEASEEEFRPSEEELSEVIGLVEKGYESIESTVQTRI... | Function: tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His).
EC: 2.1.1.225
Catalytic Activity: adenosine(4) in tRNA(His) + S-adenosyl-L-methionine = 2'-O-methyladenosine(4) in tRNA(His) + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 639
Sequence Mass (D... |
A0A060CPC5 | VEPLLDSIEGANDRYLVANDFPAYLDAQAEVDDAFRDQERWDRMTICSTIRSGKFSSDRTIAEYASKIWEIEPVFIPEHESDDDDEDRVVAGLVDE | Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
EC: 2.4.1.1
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + phosphate ... |
A0A1I7Y9L7 | MFVFRILHTVPYSNKPIVKDVVASLHSYFTFNMLLGLAILVSYKQFAGRPIECMLPMGFSGAWEQYAENYCYAQDTYFVPFGEAVANVGKDRRQNRQISYYQWISFFLLFEAFCFKLPTFIWKYFATQSGMRVGEILRLASNDANTDPDVKKSNIDALRVHLEGALRFHSRLKEKNLIPHKVIRCLNIKYSRFYVSFIYMISKVAFFVNIVVQLELLNRYLLPDELKNAFGINVVHKFITSNETWKENGLFPRVREMGQRQTHTVQCVLLINLFIEKIFIFLWAWYMSLAAFTVANIFSWLFVLFNFTSTHHFLMNHLEM... | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 490
Sequence Mass (Da): 57454
Location Topology: Multi-pass membrane protein
|
E2BEX1 | MYTHYLLSSLKIDTKSWKKHITQLQMLQFFILAYHISQLLWTDCGYPQWPALVLLPQHVFMLVLFAEFYYNAYIKKEPASAAATTKTETDSVSTEISHAKLEER | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 104
Sequence Mass (Da): 12173
Location Topology: Multi-pass membrane protein
|
A0A1B1YVW1 | MMIFNTRFGRLFFFSTEPQTCSYLPDREAVMLFADPNKVIDTETYARLIDYGFRRSGDNVYRPHCRGCQACVPVRIPVADFAPDRAQRRAWQRNQDLAISTARTEFGTEHLDLYHRYQVARHDGRAVVRDAREQLEFLRSRFINTSSLEYRLDGRLVMVSVIDAMPQGLSAVYTFYEPDDAQLAKRSLGTFGVLRLIEECRTRGLPWLYLGYWIADSDKMAYKSRYQPLHAYQQGRWERLAPTGQEPETDP | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-aspartyl-[protein] = H(+) + N-terminal L-leucyl-L-aspartyl-[protein] + ... |
A0A0K0L8U4 | EMYLIEGLAGGRVATYTKLHHAAIDGVSGAEILTILLDPKPEGRKVAGPEEQWAGEQVPDPKSLFVRSAARLAISPARALRVGYEVARSLPGLKPLKSLPALVGIGGGDDDVVSRPTLIAPRLRLNGAISAHRRWAFGDVDLERVKAIKNAAHTTVNDVVISISAGAVRRWLVEHDDVPERSLQALIPISIRTDEEQGEIGNKVSGMIAPIGTHIEDPLDRLQFVHHTMLVAKETHQATPATLLQDFAQFAPPAIAARAAQVVFRNGRAGRFTPFNLT | 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: 278
Sequence Mass (Da): 29968
|
E2BKG6 | MNHQNPVTGLFPASPNNDHAWIRDNIYCILAVWGLSMAYKKIADADEDRAKTYELEQSCVKLMRGLLMAMMQQKEKVEKFKSSQNPHDALHAKYSSVNCQTVVGDTEWGHLQIDAISLYLLILAQMTASGLQIIFNLDEVAFIQNLVFYIESAYCTPDYGIWERGDKTNHGLPELNASSIGMAKAAMEAMNELDLFGARGGPTSVIHVLGDEAQKCQAVLQSMLPRESNSKELDSGLLSIISFPAFAVDEPNLIHLTRDAIVKKLQGRYGCKRLYYEPWELRMFENIECEWPLFFCYLILDYCFQGNKEGVAIYMKYLED... | Pathway: Glycan biosynthesis; glycogen metabolism.
Function: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I.
Subcellular Location: Cell membrane
Sequence Length: 574
Sequence Mass (Da): 64915
Location Topology: Lipid-anchor
|
A0A3D3XQV2 | MVQFTGYNWYAFGITHKHAAAQERQNFALSETQLEAYFREIFPQNECAGFIINTCNRTSFFLFGKHPENIEKKFVQESGHIDISEIGDRYIGKQAITYLFEVMAGLDSQILGDFEIVGQMKTAFDKSKTYGTALGIIEKVVNQAIYSSRRIKNETGLSGGTSSTSYAAVQFLKSTLPNFSCAKILVFGMGQIGKRTLDNLVAEKGNKNIFVANRSFSKSQKQAALHCVQALRWDEALNQIGQFDAIVSAVSAPQPVFTAEILANANTKCIVDLSIPFSVGENVQKELDIELANVDQLSIAISEQMEQRKKWVPRAYEIIR... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tR... |
A0A291C3N6 | IDFLMFSLHLAGVSSILSSINFICTVQTAVFYTVNHEMISVIVWTYMFTSVLLLLSLPVLAAGITMLLFDRNFGSAFFDPMGGGDPILFQHMFXFXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFASFAIVCLGCVVWAHHMFTVGMDIKSTVFFSSVT | 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... |
A0A1M5DEI7 | MTSGPAEQVHDAVRDLVAAWLPTQRWFPGKGRQADIEVRRLTELLHSPQVTIWTARADYGDGEVETYQLPLVSRGEPVDNLEHVLLGTVETEAGNRWVYDALHDKDTTRAWLAGLVDQPAGDVRFTRYVAAEDVPVDEASLVMSGEQSNTSLVYGDAAIMKVFRRLQPGVNPDIEIGGELSRVGAHNVATLLGSVEADVDGAPTSLAMVQEFLTSATDGWVLATASVRDLMAEADLHADEAGGDFAGEAERLGGAVAQTHADLVTAFGTREATADEMVARSQAMQQRLDHALGVVGELADVADGLRAIFAAVAELEGGVT... | Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.7.1.175
Catalytic Activity: ATP + D-maltose = ADP + alpha-maltose 1-phosphate + H(+)
Sequence Length: 464
Sequence Mass (Da): 50268
|
A0A5C9D0F2 | VAEIQRLLKVGFEAARGRRRKLCVVDKANVLESSRLWRETAKRIAPDYPEVELDFMYVDNCAMQLIRAPGRFDVIATSNIFGDILSDEASVLTGSIGMLPSASLGSVLNSSGLPRGLYEPIHGSAPDIAGKNLANPLGTILSAAMLLRHSFGLVEEAAAVEAAVFSALGAGYRTADLASASTPVEMRVGTKEMGVLVLASLLRPVPKTA | Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
EC: 1.1.1.85
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH
Sequence Length: 209
Sequence Mass (Da): 22166
|
H9CTS0 | FVASHPWEVIVGTVTLTICMMSMNMFTGNDKICGWNYECPKFEEDVLSSDIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTGLNEALPFFLLLIDLSRASALAKFALSSNSQDEVRENIARGMALLGPTFTLDALVECLVIGVGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADP | Function: Catalyzes the conversion of (3S)-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonic acid, the rate-limiting step in the synthesis of cholesterol and other isoprenoids, thus plays a critical role in cellular cholesterol homeostasis.
Catalytic Activity: (R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylg... |
A0A256IMF6 | GYGIESDLARCEDEGRRPDARPEYVSQKAMDRGRNQMGSLGSGNHFLEVQRVTDVFREGVAEEYGLREDGIVVLIHCGSRGLGHQTCNDYLRRIEKEHGDLLADLPDKELAAAPAGSELAEEYYGAMGACINFAWVNRQLITHQARETFGEVFDADPIEDLGMELLYDVAHNIAKKETHEVGVDADGRPAVGDEAVDRTERELYVHRKGATRAFPAGHDDVPEVYRDAGQPVIIPGSMGAGSYVLRGGDESMSVSFGSTAHGAGRLMSRTQAKQEFWGGDVQDDLEAGQQIYVKAQSGATIAEEAPGVYKDIDEVIRVSD... | Cofactor: Binds 2 manganese ions per subunit.
EC: 6.5.1.8
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP + H(+)
Sequence Length: 339
Sequence Mass (Da): 36916
|
A0A1I8APH9 | MMRHPHAWMGLLLWSLFTPAHAAWTVNMAPGATEVSNAVFDLHMTIFWICVVIGIVVFGAMFWSMMVHRRSTGQQPAHFHEHTWVEIMWTVVPFLILVAMATDRKSGSAG | Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 110
Sequence Mass (Da): 12449
Location Topology: Multi-pass membrane protein
|
S5XAS3 | TLYFIFGIWAGMVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTAHAFIMIFFMMMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMRINGLSFDQMPLFVWAVGLTALLLLLSL | 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... |
A0A1I6IJ21 | MGARVVVVGSINVDSVVRVVEHPAPGETVLGLGVELLPGGKGANLAAGAAASGADVLLIGRVGDDDLGRRYVERLAEHGVDTSAVSADAKQPTGQAFITVAESGENSIVVIAGANGDLAPDAAARAIPDDAAVVVTQLELGPEVAEAVLRRGRTLGATTVLNASPVSPAASALLELADVVIVNEHEWAALGSPADACVTLGAAGARWGDADAAPDPVEVVDTTGAGDAFAGALVAQFAAGASRADALRAAVAAGARATTYAGAQPWGFAAATG | Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step ... |
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