ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A2N7QEQ4 | PVIIATQMLTSMINSTMPTRADVSDIANAVFEGADALILSDETAIGKYPVEAVKVMIRTIEEAEKAYEYKLEEYKHVSPDFAIAYSSCILAEELGAKAIVVFTKSGSSAKRVAKFRPKPIIIVNVHDEEVLRRMKIVWGVLPYMVLSEKEDSESMVKEFIKKAYAENLIKEDDILVLTMGYPIGKIGSTNLIRVIKRDQILKFISISK | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 208
Sequence Mass (Da): 23247
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A0A7S2ZR90 | LVLAALAASAQGLTIARVPTLRGSRSAAVNVRMADFDGEKLASMIEKKNIDHLMEGNRVFRESMLKQDKDYFSKMAKGQSPKFLWIGCSDARIPANEILGLEPGEIVVHRNVANQVVNTDMSLMAILQFAIEYLEIENIIVAGHFECGGVKASMSMNDHLAPLENWVRQVRDVQRLHKAELDSISDPKARERRLIELNVLEQCNNVYKEAVVQRRRTYTNLRTGFPKPRIFGFTVDPATGELNNLNFDPETSMSPEVRNIYELYDQKAAKEAYADK | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 276
Sequence Mass (Da): 31112
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A0A8C6FA65 | MVGSWLQLGGRPCIPAFPLEVLSSVLPALWHQPAPLRGLAKLLVSPAGPLGGSDIIASARHSPRSRGRGKRAVGRARLRGDMAGLSTDDGGSPKEDVDPFSYDYETVRNGGLIFAALAFIVGLIIILRSPPVDAGGKAVEMGELASSGPGKLQCTWSQAKGGNQPPLDTPSPRSGRFLGLSYISAHLILLATLRDGHQCHHFADEKPGPP | Function: May be involved in forming the receptor site for cardiac glycoside binding or may modulate the transport function of the sodium ATPase.
Subcellular Location: Membrane
Sequence Length: 210
Sequence Mass (Da): 22036
Location Topology: Single-pass type III membrane protein
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A0A397UYR9 | MKKLYYHENSNSKFSKPRSPYLTSLSELSKWKPENDEFNVAKVDLRERPIFRNDATQKENDKRDCQVVVCHDMAGGYIESFFKIGYSIQYWQYIDIFIYFSHHRITIPPPQWTNAAHRNGVKVLGTFITEWVRDMLENELWVRGPHTKAPLDDSENVDRRIVSTVFADKLVSMAMYYNFDGWFINIESPLIGGSLHAHQVITFMNYLTQQMHKHKPGSVVLWYDSITKEGTLAWQDHLNDLNYPFFDVTDGIFVNYTWSEEYPELSAQKAGSRKRNVYTGIDIWGRNTYGDGGFTTYKALKVIQKAKTSCALFAPAWTYE... | 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... |
A0A401TKC0 | MAVFTPVINGVGGNLVAIQASRISTYLHLWSVPGVLPRRMWQNWPNPWTTFFRS | Function: Acts as a magnesium transporter.
Subcellular Location: Membrane
Sequence Length: 54
Sequence Mass (Da): 6171
Location Topology: Multi-pass membrane protein
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A0A397VVQ8 | MTNSTKLFYELDLKQRIDAVAKWSTSQKNSIRQFYKTISYLTCSTFWLNPYDLYPAIGYPGPDPEINGSRFKGRTFPEYEFIEITEDTKDLEFDVVIVGSGAGGSVAAARLARKSGNSVIIIEKGHHYHQSELTLKEKDGYEKLYELGGGMLSEDSSMTVLSGSNFGGGTTIGWSTSTEPSHFVREEWANNFGLNHFMDDEFNDSLKTIQNRLGVNTNNIVQNESNKILCDGCKKIGAPVTTVPQNSASRPHECGWCGLGCRYGEKQSVVMTYLKDAKDYGVKFIQDCFVEKVLIENNKAVGVEATVNNGEKKFRVNTKK... | Function: Long-chain fatty alcohol oxidase involved in the omega-oxidation pathway of lipid degradation.
EC: 1.1.3.20
Catalytic Activity: a long-chain primary fatty alcohol + O2 = a long-chain fatty aldehyde + H2O2
Sequence Length: 584
Sequence Mass (Da): 64607
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A0A8C6AJN7 | MPALARKPGSQVRHGPVRRAGFGTPGSRPRRPGCLRRPAPTPHARCSLRPCRDFIEKRYVELKKANPDLPILIRECSDVQPKLWARYAFGQEKNVSLNNFSADQVTRALENVLRGKA | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
A0A8J8KPZ2 | MTERPKIAPESGHGLERVIFFSDAVIAIALTLLAIELPVPSGEDWVHQLKEYLGSDYVAFLISFAVIATLWFNHHRMFQQIARLTYGMIWLNILGLFAIVLMPFATKVLTGLGDHPAGPVFYACVMVLWAVVWILMAQTATRQQLWSEDAPTTAPSNMVFGASALLVAFGLSIPIAFADPDWATFFWISAWPISTVGMRIRRGRQERAAAQ | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 211
Sequence Mass (Da): 23466
Location Topology: Multi-pass membrane protein
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A0A346RGG8 | MLKSYKILFFNFMIIGTLITISSYSWLSMWMGLEINLLSIIPLFNSMKNQFPAESALKYFLTQSMASTIFLFSILNSLNMESMFLMDNFLNNLIFNSAILIKIGAAPFHFWFPEVMEGLNWINNIILLTWQKLAPSIIISYNIFSSNFFFIIIITSTIIGGLMGMNQISLRKIMAFSSINHISWMLSSMLISNSIWFIYFMIYSLISIILSYMFLKLNIYYIYQLFNFNNQNKYINLMFFMNFFSLGGLP | 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... |
A0A924R4F9 | MQAEIPLQGLSLVVTRPPAQAARTALLLRAAGADIIEFPVLAIASINATLPAPELASASGIIFVSANAVGHGLPLVASAGGAPAGMEIFAIGRATAAALAQAGFKHVVSPQQSIDSEGLLAMPQLLRVEGHHIILVKGCSEFGGRTVLEQTLTARGARVTVLECYRRAPMVPNLAKREALSELLASGGVHAFFALSVETLDSLNNIFSMMQHTPQSQMVLLVPHPRVAMAARARGFDRVAEVPLAEPAMINALTELKPRLLNPQNF | 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... |
W8F212 | MLKRDFLKNGLLTLVGAMVSPALLAAAHEEKLLREARATPMADGPFTLPALPYAFNALEPHIDAKTMEIHHDAHHKTYVSKLNEAVAGKPEEKLSLAQLLASASKQPDAIRNNAGGHWNHSFFWQILSPKGGGQPTAGLAAAINKDFGSYEKFTEEFTKAATGRFGSGWAWLIYDKKAGKLMITSTANQDNPLMDIAGIQRGTPILGLDVWEHAYYLKHQNKRPDYIKTFWNVVNWQEVGSRYDEARKG | Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 249
Sequence Mass (Da): 27626
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M1KG02 | SKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVAGEENQYIAYVPYPLNPFKKGSVTNMFTSIVGYVFGFKDMRPLR | Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 122
Sequence Mass (Da): 13587
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A0A8S0S4U5 | MTIFYNGMVAVFYVSRDKAQDILLLADEGVQKPAESSDSNVTSDQKNILGTLKGDFPIARRQSLQRFLEKRKE | Function: Repressor of jasmonate responses.
Subcellular Location: Nucleus
Sequence Length: 73
Domain: The jas domain is required for interaction with COI1.
Sequence Mass (Da): 8279
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A0A3Q9XVR6 | MNIILAGPPLTGKTTLGKQVACKFGWPFIDTDMLVEKCYKNEKNIEVSCREIFKREGETQFRAYEQEAVLSLQGYTHSVISLGGGALEKLDNVRILKKIGKIIYIKTSLALLEKRLLDHSLPSYLENEEKPLEAFQKLVRRRSPFYELYADQIIETGSLSASQIVAIIYESYHGQ | 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... |
A0A432QZD7 | MPFRKMFNKMTLRDIPKEELEGKKVFVRVDFNVPIENGVIQNDKRIRAALPTVNYLIDHGAKVVLCSHLDRPKGWDPKLTLKPVAERLSRLLERDVKFIPDCVGEEVEWEVENLKPGEVALLENVRFYKE | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
EC: 2.7.2.3
Subcellular Location: Cytoplasm
Sequence Length: 130
Sequence Mass (Da): 15157
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A0A8S0V0Y3 | MFNSSIIGLINGVAAGWGDMGGGVCQLLMPLLFHMIKVCGATPFTAWRIAFFIPGWLYLIIGVMVLTLGQDLPDGNLSTLQKRGSIHKDKFSKLLKYAVTNYKTWVFAFIYGFFMGVELCMNNIIAEYFYDRYAAIRHVRHSTDALYARFYHFIALDSFTFWVYFKVVFITTRNCQG | Catalytic Activity: NH4(+)(in) = NH4(+)(out)
Subcellular Location: Membrane
Sequence Length: 177
Sequence Mass (Da): 20250
Location Topology: Multi-pass membrane protein
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A0A398TNQ6 | MDKKLIAFLCTLIITGCSNGIGDSPSPPGKNVELVGIPGQGIAVTSNGATPTLGANNTEFPEVSIMSTGGALLTIWARPVRNWLWGYTPFDSVNFGENRNWKVVDGKDAGTVKFVNVAQGTCMEAFKNGVIHNTCDDNSLSQEFQLLPSTNGNVLIRSSALQTCIRADYLSRTILSPFAFTITLEKCPGAKEETQEMLWAISPPVRAAKPNLIKPELRPFRPLPIPPPPHDKPDGMEGV | Function: CDTs are cytotoxins.
Subcellular Location: Cell outer membrane
Sequence Length: 239
Sequence Mass (Da): 25791
Location Topology: Lipid-anchor
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A0A6B9HJC1 | PPLAAGIAHAGASVDLSIFSLHLAGASSILGAVNFITTIINMRAPGMSWDQNPLFVWAVFLTAILLPLSLPVLAGAITMLLTDRNLNTSVFEPAGGGDPILYQHLF | 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... |
A0A7K4M462 | MPFLDLQRRLGIDVDSWLLRQSTAQPHGTAAVCHAFEREWVECGHGLGRTRAVRECALEYEDFMECMNRRKL | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
A0A1M5WR94 | MNIKIITTEKIREKFAKEAINEYSKRLSRYCKLKFVEVKDKKQLQKEITDKTYLVLVSIEGNLISSEELANKISNLALTGKSDITFLIIYGEVKNEIKERADYHLAISNMAMDISVLIIIMYEQIYRAYRIINNEPYHK | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.177
Subcellular Location: Cytoplasm
Sequence Length: 139
S... |
A0A257G1T4 | MPSIPWPQTGCLFAAHAPALAHWHPHIHRHAATANLREWLTDQASLTARLTARCGQFRVQRLQQQIARCLPDESTVMGLPVRANVVERDVLLRCDGVAVVYAHTILPLSATAGHWPLFASLGNKSLGSTLFHDPLVVRGDLHYAQLRATHPLMRRIADLHLVPTPAPRLFARRSLFTRHGSSLLVTEVFLPALCALPLLAHSKSAG | 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... |
A0A7S0BJV5 | LRWSKESTFDQADAERVRTEINKHGRGIVSNVRVSERTRKAPNGLNTVQLLMACSKSLGISPKKTMQVAEKLYTAGYVSYPRTETSQYPQSMSIKSILNDHKDHPDWGKTVDFVSRQNPAVPTGGVSVGDHPPITPTKSATRSELQGGLEWRVYEFIARHFFGSLMGDLKYREINSDIQVGALTLVHRQVIVDRLGFAGSMKWNLGEVYRIDEEFKTRSERDSVRSGQMQKMFPRDPVTFGKVQVIRNETAPPQFLQEHELVSLMDKHGIGTDASMAGHISTIVDRSYVVVCDKEGVPIPVGRKPGSGARKPAGGRYLVP... | 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... |
A0A401RV81 | MGNHPRKSDLGSKELTAIVIGLVSFLCLALLVAVFYKRHTLCAYMKEKKNDKDCVCSIVAETKTLKDHIIDTSAGSGSDTGTWTQLWLVLEYHENGSLFDYLNRYIVTIDGMMKFAISIVSGLAHLHMEMIGTQGKPAIAHCDLKSKNILVRNNGTCVIADFGLAKRHDKATDNINTSPSRRVGTKRYMAPEVINDSINKSDFGSFKYIDIYALGLIYWEIAHRCCAGGFHDEYHLPYYNLVPSDPSIEDMRTVVCEQNLRPTIPNQWQNFQALQMMGKIMQECWNANAAARLTALRIKKTLSKLKVEE | Catalytic Activity: ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]
EC: 2.7.11.30
Subcellular Location: Membrane
Sequence Length: 309
Sequence Mass (Da): 34787
Location Topology: Single-pass type I membrane protein
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A0A142XEA6 | MVRIKICGVTTPEAARGAAEAGADAVGLNFYPQSPRFVTPAQAGAIVRALPAFTTPVGVFVGMPVRQVCAVAFQLGLRGVQTYDDQPPDADTFPFAHVPAFRVKDQAGLEHVRRFVDTARALNRAPAAVLIDSHVPGQMGGTGHVAPWDLLKGFDVGVPIILAGGLTPENVADAIAVVRPWGVDVASGVESAPGVKDPDKVALFVKNVRTASESLFT | 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: 217
Sequence Mass (Da): 22688
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A0A8S0QX28 | MGSSENVDSGNFSVKRSNFSQTCSRLSQYLKENGSFGDLNLGFTQNFESKRTAPTGTMNLLPMIEKSGQNSGADLNMPVKKSEQETAQMTIFYAGEVIVFDDFPADKAKEMMILASNSSAQNHSTTAFPPPLPTPPPSNMVQSPAESATNIVPTPAAPPLASDLPIARKNSISRFLEKRKERSIAKAPYQATEPSKPAKGEPWLGLGHRFPH | Function: Repressor of jasmonate responses.
Subcellular Location: Nucleus
Sequence Length: 212
Domain: The jas domain is required for interaction with COI1.
Sequence Mass (Da): 23002
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A0A7V9CHS4 | MNRQSPNAIWRAGWATNKTTCASKVPDVKANHKIHDGEWKRAAPHPDSPYRAWLLDRGSLTGRIQSRCAAFSVRGVHQRFAKPFRDEVRELSLPARELALTREVFLYCKATPVVFAHTVLQRTALRGPWHFLATQGSKPLGATLFSNPKVARLPLHFKKLTDRHELFRRAQRVLKSSTDCLWARRSLFIVEREPLMVTEVFLPGILELPA | 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... |
A0A1F9M1A4 | MRSHETAESLTSHGRYRRFRRTLFLVMLTISLLPLLTTVGLSFHQYRSLLQKEEEAQLAWNAESAKKTIEAFLEELQGMIVFVAADYTPEELTSQRKLDHVLTNLRKRHKGIVDLSVIDSEGVQQGYAGPYNLKGKYYGDRSWFQATIARRAYISNVFLGYRKLPHFVIAAGKELPQGGGYWVVRVSIDSETLDKFIATINSEASDDIFLIDDTGELQTSSRYYGSTRGKTPSFFTPKKTGITLHINPENNNMMASCYIEGTPWILVLSKKGYIYGRNWSAFRNQTILIVISSAILVLLVIIRTTNLLVNRIFETDRRRE... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 570
Sequence Mass (Da): 63738
Location Topology: Multi-pass membrane protein
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A0A521AYP4 | MDYGHQFFYDICAMIYITRKEHFNAAHKLFREEWSNDKNAEMFGKCSNPNWHGHNYDLFVTVKGEVNPETGFVIDLKDLKQIINSRVIDKLDHKNINLDVDFMKGKMASTEMLAMEIFNQLKGEIESKGAALHSIKLFETENNFVEYFG | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.-.-.-
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 149
Sequence Mass (Da): 17392
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A0A172ZWZ4 | TLYFIFGAWSGMVGTSLSMLIRAELGNPGALIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLMSSMVESGAGTGWTVYPPLSSXXAHAGASVDLAIFSLHLAGVSSILGAVNFITTIINMRSIGMTFDRMPLFVWSVGITALLLLLSLPVLAGAITMLLTDRNLN | 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... |
A0A8S0S1N1 | MGFSHRKLFSEDEIRKADKGLDRCNFCYSGCPDECKNTNILFTSSPPSSKHEMPTILITMLCILAAAFMFLVYLTFRRYRWNLRNSRRRNSPTLENANNREDFIEENQGPVGGPPIWYIRTFGLQQSVIDSISVFKYDKVQGLIEGTDCSVCLNEFQEDENLRLLPKCSHAFHLPCIDTWLRSHQNCPVCRAPVVSNANPSPVNSMLTNSNDLGSREEAQIDSELDQRVVETDETREMRVGIENESPTQIEDRKLADLLHKNSVRPSLRNGKLRVLSDLVDNRVKLDEELQPVRRSISMDFSSASMLYNAVVDIQAKKDE... | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Membrane
Sequence Length: ... |
A0A6J1WQL1 | MATLNNDYLRIPRFYAGRSVLITGATGFIGKVLVERLLTTCPDIKKLCLLMRTKKENQPEERLQQLKDSPIFNDLRHRDPRQMDKLCIIPGDMLQPKLGISNKYLVDLQEVSIVFHSAATVKFNEDLRRAIEMNVLSVMRLLAICDNLPNIQAFVYVSTAYSNAELPEIEEKVYSLSTPIEQLLALVNDNTIDSEDLMKQNLILADQKFHHMNTALKFFVLREWRFKNENVRNLRKRLHTSDTKLFNIEPRAVNWDDHYRHFVCGVRKYLLKQNDDDLPQAKLRLRRAYVLHNFVNIIFLVLFLHGLLEKKQRENIKNNI... | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 381
Sequence Mass (Da): 44902
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A0A1Y3S6M9 | MCPYLIFQLPYLGEFVIPSYALFAFVGLFFTMVFLYFRLQKRGMPFYHFLLLMLILVIGVALGSKALFVMTKLPEILQDFTLEKAIYIIWTSGFVFYGGLFGAIIGACLFARIFSIPLKPFLDIIVPGFPLFHFWGRIGCFFAGCCYGKEATWSVAMHMEPDIPRIPVQLFEAACLLLIFGVLLLIDHKANISISPLASYFLLYSVCRFVLEFFRGDDVRGILGVLSTSQWISLGILAFILCKVVAKRLRWVTQTRQSC | Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,... |
A0A6A1V1W8 | MGLRQQGDARFRVFAVSNVGSANTGGYGGSGDGNSGGRGEGSGDGGFDGDGGNNWSLLSWQAVAHFFCLDLSTSYEMEWTETNGGSSLLEALYKALDEVVKLAECEIYSYNPDSDADPFLERGAIFIAAFMTRTFLPRWSFNFFFYSRRLKRVPSFPCFPRALILIFAFDEVISLGHKENVTVAQVKQHCEMESHEEKLHKLVLQSKINETKDYMKRKASKIEKSKIIGGRVENFAEEHEEKNDLWNDCKRVHCVATMKVRV | 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. Coatomer complex is required for budding from Golgi membra... |
A0A6A1VA90 | MPAKDEDDIVDEEEDEEHGETLCGACGENYAADEFWICCDICEKWFHGKKGESLPLWISNEQWEVNLPTEEVPPELPEPALGINFARDGMQEKDWLSLIAVHRDAWLLAVAFYFGARFGFGKAGRETNQSRWVIREDLKKLWSLKIQQRLRYLLWKIMAYALPVRDSIWYTRNMVTHQNGRVELAVGAIIRRRYDEHEQEWNGRNSLQWEPPPCSNIKISFDGAVDKDVIVFAPGTHPLKAEALSAQLAIHLMEEENLVQACLFEGDAQLMINQIQDDAIQPDWLIEEDVLFIKSKLNDHSQWVFKWIPRNANEMAHRIA... | Function: Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.
Subcellular Location: Nucleus
Sequence Length: 454
Domain: The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence Mass (Da): 52030... |
A0A2M7F5Y8 | MFASLFFDYLFVMILTSAVLMITRKHIVHAVLYMLLMFFHIAGLYILLEAEFLAAVQLIVYAGAILVLYLFVIMLVNIRKLETLREQLFGHLPFALVSAGLLCAGVVGILMQETVLKEPSSSVQAATQMSNPELLGQALYTQYLFPFEAASLILLVALVGAVLIASRKI | 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... |
A0A401U1S4 | IHPARATKDELYPYLAKRWHAHLETFGIQAYQGMMEGPPYPKAQPNASRRDAYPPEGGPQGSSLSFMQKQHLDPNNVALGVLNPLATGQGLRNQDLAGAVCAAINDWQIEKWTSKDSRLKGSVVVANEDGASAAAEIRKRAGDSNFVQVLLLSRNVEPLGQRRYWPIYEAAQEVGLPIG | Pathway: Secondary metabolite metabolism; quinolate metabolism.
Function: Converts alpha-amino-beta-carboxymuconate-epsilon-semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS). ACMS can be converted non-enzymatically to quinolate (QA), a key precursor of NAD, and a potent endogenous excitotoxin of neuronal ce... |
A0A2H0IPH7 | MKLKVCGMRESANISELLKLSPDFMGFIFFAKSKRDVADSLDAELLASFPDSTQKVGVFVNAELDFVKGKVEQFGLDMVQLHGDERPEYCFDLKSKGIKVIKVFSVAESFDFNQLEAYKPYVDFFLFDTKGKERGGNGVQFDWLILKGYDQEIQFFLSGGIDLENLEQLSELKGMNLHAIDVNSKFEIEPGLKDVGRLKELKERLLRASQ | 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: 210
Sequence Mass (Da): 23842
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A0A2M4ANQ4 | MSKGRYVNFARKKKFKGHSGHFAEAETNDIDVANGVSRKAKSKKRSAFKFSVKEEEAEIERLQQRYQQQAGSFKPDDVKTFSDFPLSKKTLTGLQEAEYLKPTVIQRDSILAGVLGEDVLAAAKTGSGKTLAFLIPILERLYVQKWTRMDGLGALIITPTRELALQIFETMAKVGKHHDFTTGLIIGGQNLKFERNRLHNLNIIIGTPGRLLQHMDENPLFDATNLKVLVLDEADRCLDMGFASTMNAIIENLPSVRQTLLFSATQTKSVRDLARVKLNNPRYIAPHEHEQSATPVKLQQSYVVVTLPEKLTMLWSFLRT... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 770
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): 86638
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A0A962B649 | MRTIARFFDTIVGGISLAAAAIAAFLLLAMFVVVQYEVVMRYWFGRPTHWTHEVTTFAIAWVGFLSAGYLLRQGRQLEIDIVTSRLSAGARRLLGTFTDIIGAAFCGYTVLLGYRFVSTAHMMGATNASELDTPLWIPYSAIPIGFTILGLEFLARILNRWGLTPERSDDPHSSTAI | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 177
Sequence Mass (Da): 19581
Location Topology: Multi-pass membrane protein
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A0A401RKT9 | MPSDQDAETVGKLLHSKTPASPSICSQGQQEFRTRAKSPRPTFFRNVSVPDPRLSAQEGVLVEKPGVFQRQNSVSKTIRRGTAEWFGLGTDCDLDQHHWQRKSWRHCSQRYGKLKAQYQRNMGIPNLESDPFSTVDSPKVLKGHVLRYTDTVDQPGIPHPADLPLKSLGSFQNSQSGYVGMIRRKRESVVRMSLRAASAVVTGRPLLRPSPHRRTRGSFVYPSNFVEDVTDGPERLDSSFFSKIDAPDESYSMPDDVFESPPLSDSWPMRDVHLVERLQSPLYVLRNKGVFESVQHMQQENFWIGPNSVALIHLGAKFSP... | Function: Regulates ADAM17 protease, a sheddase of the epidermal growth factor (EGF) receptor ligands and TNF, thereby plays a role in sleep, cell survival, proliferation, migration and inflammation. Does not exhibit any protease activity on its own.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length:... |
A0A3N5EQW9 | MATARAALAGRRVLVAGLGESGLAIARWAAFRGAEVTVADSRDAPPQLAALRAACPGVRFVGGALDAALLDGIELVGWSQGLSPITGEAAPLFAAAREAGLPVWGELEFFAREIARLRAAGHEGRVVAITGTNGKTTTTRLVGHLCRQAGLRVAVCGNISPAALEALREAIEHDDLPQVWVLELASYQLRLAESFVPDCGTVLNVTQDHLDWHGTMADYLEAKQRVYAPGTVCVFNRDDPLSVPGATLPVQADAAPEPADDTAGGSKAERLAARRAAARAERAAAEARAAIEAARRTVSFGLDAPSAAPGYGLVRDGGLV... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-... |
A0A432QTK0 | MRKPWLLSFSLLLASCFSKPQGTVSYTPPPPPKLNFQTAPLSEGSLWNGNARFKYMYGDLKARDVGDLVTILIVEKTSAQSQTETSLKKSSKLQGGVSALFGINQSTLNKTNVSMQGSAEHGGKGTTVRGSTLTGTITAQVIGKQPNGNLIIQAQKSIVVNGEAQVLTITGLVRPEDINDDNTVTSDRIFNLQITYTGEGVLTDVQEPGLIWKIVAKLWPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Subcellular Location: Cell outer membrane
Sequence Length: 221
Sequence Mass (Da): 23853
Location Topology: Lipid-anchor
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A0A7G9QFL4 | MQNETTKIALLVAVSTLVFLLMPVFLILYIRSYNRHKKNHFLEKQNMQQRFESEILQTRIEVQDQTMQSIATELHDNVGQLLSLTTLTLNSVNLNDAEKAKKKIENSLSLVNKSIKELRELAKLLHGEQLVENGIGHAIDQEISWLNKAGTYELKTKNQLIDSTLISPDKDLIILRLLQEIINNVIKHAQATHIQIDSYLENDALHLKVIENGIGFDPDEINAKKAGMGLNSIYKRIEMINGKLALNSAPGKGTSITIEIPYP | 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... |
A0A5C7LXS7 | MEHDDRSLNEPAPVFDNIEINVAEILLALGRGNDEGTRETPKRVRKFYLDWTTAGEPTFKLTDFDAESFDQMVIQRRIPFFSMCEHHLLPFFGLATVAYIPNGKILGLSKLARIVDWFSRRPQNQERLTQQIGNFISKTLKPKGVGVSLTGRHMCMEMRGIRTYGTMTTTNVLMGIIRTAPDAREEFLRSTTYEQL | Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Length: 196
Sequence Mass (Da): 22460
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A0A949FPW5 | MDAPPQASRHPLDLPANLLASLGTVWIFVIMCLVVADVIGRDFLDAPITGVAEFSARSVASIVFLQLAAAICSSRMTRSDFLLNIIGKRSTAAVKALDVFNALVGAALFSALAMI | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 115
Sequence Mass (Da): 12103
Location Topology: Multi-pass membrane protein
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A0A961Z2R0 | MRDAARYRGMTMAAVLSGGAASRFGSDKTQEMLDGQSLLDRTIAFAGTQAASVVIADGGQGHALPDGLTRLVDADFGAGPARGLCAALAHAAGLKTPPRYLLTLPCDVPFYPHDLAGRLIGAVVHDPQMPALAVSGSRLHPAIAVWPVARASAIIARVKAGENALHALLGPAQERGEVRFSGPVIDGIEIDPFFNVNTPEELEIAREVLQALAEG | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
A0A6A1WFF0 | MCSLTTTFVVAAIFFTTTLYESNAQLTATFYASTCPNVSSIVSNAVQQALQSDSRIGASLIRLHFHDCFVNGCDASILLDDSANIQSEKNAGPNTNSTRGFDVVDNIKTALENSCPGVVSCADLLALAAEASVSLVSLFCFPRAEKRT | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/... |
A0A832XI81 | MSDFYTIDDFNFKDKTVFVRVDLNCPIDQKSREFLDDRRIVEHAKTVKELSDKGAKVVVLAHQGRPGDEAEFTTLQKHAERLGKYVGKKVKYVPDILGPTAQSELESLKSGDIILLENVRFLAEENLNRTPAEQAQTLFIKFLAPFVDYFVLDAFATVHRSQPSLVGFTEIKPSLAGRVLEEEIKMLSKAVEAKKHPAVFVTGGAKIKDSLKTIEQFLNRKIVDEVLTCGLVGNIFLAAKGYPVSGIEYIEDYVKLLEKSKKLLGLFPDKILIPVDVAVDKYGQREEIPVSKLPQPYRLADIGAKTIEHYKSIISKAQII... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
EC: 2.7.2.3
Subcellular Location: Cytoplasm
Sequence Length: 408
Sequence Mass (Da): 44883
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A0A1E3BSJ0 | MDNWTPSSWKSKPIKQDVVYSDLDGVQSALDKLQKLPPLVTTQEIHNLKKHLKNVALGKAFVLQGGDCAELFDYCNQDMIEAKVKLLLQMSLVLIWGANKPVVRIGRIAGQFAKPRSSPMETINGIEMPSFRGDNINGFAATPEARTPDPSRLVSAYFHSSATLNYLRASLSSGIADLHSPLDWGLGHVITPSIKEKYERIVTRVKDALRFMHTVGIDTDRGVETVEVFTSHEGLLLEYEQSLPRLQRNPSSSSPSDSSHYATSAHFIWIGDRTRQLDGAHVEFFRGIANPIGLKIGPSISPEDLVKLLDTVNPTREIGK... | Cofactor: Binds 1 divalent cation per subunit. The enzyme is active with manganese, cobalt or cadmium ions.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
EC: 2.5.1.54
Catalytic Activity: D-erythrose 4-phosphate + H2O + p... |
A0A1Y2T710 | MGRAVLVFDGAMGTMLQARGLAPGACPDVWNLERPEEVIAVHRAYVEAGAQIIETNTFGSTPLRLRHYGLQDRCREITVAGVRCAREAAAGRAWVAGSMGPLGALVEPLGELTFDEAYAQFAAQARAFAEAQPDFIIIETIADLNELRAAILACKDHAPGIRIIAQITLDPSGRAFTGTDPETAALVLQSLGADVIGLNCSVGPDVLVDAVARMARVARVPISVQPNAGLPVLQPDGTTRFPMGPEEFAAYGPKLVEAGAALVGGCCGTTPEHIRRLRAAVEGLKPKGQPGPLASALGLASRTRSLFFVEQNLPVVIGER... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.
Function: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor u... |
C7MB20 | MDSPLPRQAFVDATAGIAGDMLLAALVDAGADLERVQQVLDALVPGSVRFVRSQVDRGGQRAVKIDVEVLVEDPPHRTWASLRALLEQARGRDDVPERTVDLSLEVFGRLAEAEGATHGIPAEEVHFHEVGALDSLADVIGACEAWRQLGITEATGSVLAVGSGRIRAAHGDIPVPVPAVARLALGWPTVAGELLPARGHRHSHDHDHDHDHDHDSHHAHLPAHAQGGPHEHGGRRVPAGVAPGIGELATPTGVALLRGLAGSAGPQPALTTEALGVGAGTKDTPGRPNVVRVLVGRPLGPARAASPDAHDTPTAAWQLE... | Function: Involved in the biosynthesis of a nickel-pincer cofactor ((SCS)Ni(II) pincer complex). Binds Ni(2+), and functions in nickel delivery to pyridinium-3,5-bisthiocarboxylic acid mononucleotide (P2TMN), to form the mature cofactor. Is thus probably required for the activation of nickel-pincer cofactor-dependent e... |
A0A7S3A6E2 | MRRDMGQDQVGFVAGGVGACSFTGSAAPLRLAAERKCQSKVQMTIAPEQKILKTPVPGLSVNNDGNVWVPQRARPRRNRKTEGMRSLVRENIVGPQNLVYPLFVHTKDYNEDIESMPGCERHSVDSVMKEVKFAHSLGVNQFILFPKIPEGLKSNTADECYNPDGLVPQLVSRLKHSFPDISVWTDVALDPYSDQGHDGIVSSDNRGDGGKGRILNDETIEQLCRQSICQARAGSDVLGPSDMMDGRVGAIRDALDAEGFTDVSICSYTAKYASAFYGPFRDALDSAPRESSNAPQNKKTYQMDPANSRYESMRMLDRAD | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Function: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensat... |
A0A7S0BIF9 | SKICKAFMASVLPFPEKAEDQRKMYARVITEIGDLKGIIDSTKRQRRELLADLIPKFASWNDFVMREKAVYHSLNMVKTEQKLFVATGWVPTVAIDSVRTAAEKGKKRSHSQAQTMIETQHVPASTEPPTYFRTNRFTSVFQGIVESYAVAQYKEMNPAPFAVVSFPFLFAVMFGDVG | Function: Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Subcellular Location: Membrane
Sequence Length: 178
Sequence Mass (Da): 20133
Location Topology: Multi-pass memb... |
A0A2T0BBB4 | MKGKKKLTKVLIIIISIFVAFFLVRFIICQVTLRNSTNRNEISELQQVKLDNKMQTVLLEGVTKDLPIMITVHGGPGSPIPFNVGCRGIFPELTSKYIMVYWDQYGCAKNYEKLNYDVTIDSYENMLSDLVLEMKKQFPNKKIYLFGMSWGTVLTCKVANRLPNDINGVIAYGQIIRDVAKDKDTYNQLVQCNLTVDERKVLKHVMESDNCDMKSRLEVYALISKYTNGFFYKDKDESNSRFYKIILKTFFSPDYSLKNAYGTIVDGNQNVQTNSNVLEEMFNINLTKELLQLKVPYLILQGKDDIVASTSIAKQVVKNS... | Catalytic Activity: Release of N-terminal proline from a peptide.
EC: 3.4.11.5
Subcellular Location: Cytoplasm
Sequence Length: 355
Sequence Mass (Da): 40627
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R7Q612 | MAKDSRKLKKKRRVSFSLPEAEEKHEDSPKVQVSIHDEASYDDEVETMDVEGSNGLAKTDSSDESSDEAASHESEAESDAEMTAPREANGRPKQSESDSESASDSDDCASNSDENVSSSDSADESTSEDENDEADTPQNDPEAGQAPPSVSSFGEMSLDPRVERAIERVGWRKPTPVQSAVVPAALSGRDVLVSAPTGSGKTGAYAIPIVQHICRAKSLERSGTKVVVLVPTRELVHQVTGVLKALCRYIGGVQVAAVMSRKKGNTKKNQGAKGGPAKQAHGQQASEALTFTQSADIMVGTPASIVNAAGTEQKSALSEV... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 742
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): 80873
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A0A0S1I642 | VIVTAHAFXMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLMSSMVESGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHXAGISSILGAVNFISTIINMRTAGMTFDRMPLFVWSVAITALLLLLS | 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... |
A0A401T125 | NNTGKGPSWAREGAMSLPGSCGLLPAGDRAPKLGSSYGSPRSVNRPIDIVHKRRRFDVENGLSPGRSPLDPQTSPSSGLVLQANFSHSQRRESFLYRSDSDYDLSPKNVSRNSSIASDIHTEDMIVTPFAQVLASLRTVRNNFATLTNLQDPPNNKRKTGCTSGICRSLISEESKLAAETLEELDWCLDQLETLHTRHSVSEMASNKFKRMLNRELTQLSEMSRSGNQVSEFISTMFLDKQHDLDISQSSTREKLEPMKQISALKYSTSVVSVDVPRFGVSSNQESELEQELSSINSWGLDIFKVGEYSNHRPLTVAMYA... | Cofactor: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
Pathway: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.
EC: 3.1.4.-
Catalytic Activity: 3',5'-cyclic AMP + H2O = AMP +... |
G2FMV9 | MNKIATLGPTGTFSELASKKYIETINENTEVIFYPSIKKVFNAIGTECELGIIPIENTLDGYVQLTLDLLAQTDLQIIYEIVLPIQFSLVGNIQDISDIRYQISEKFTSNLKLKDNVLIF | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Length: 120
Sequence Mass (Da): 13519
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A0A2T0XJV6 | MVNRQLSEHGWQVFEIPLLTVEPTMLKVDQVLAQPKDFDLVIFASRTAVQGYSRQLGPAFQWPDGCMIATVGSATASAVKNVFVTTQPIICPGGGQADSESLWAELDRLETPLKRVLLVRGQDGRDWLIDKLTAVGIETAVHASYQRLPVELDVQARSYLREWVGAEQSVVWLLTSTQSIDVLLAQELPQNVLSWLSNCTFVLTHEKFQSHLQQRFSVLNVKLNRQNMAICRPDDSSIVQCFLTRLHTPKITIAP | 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... |
A0A7C6LZH4 | MIKITYDNKFNTKLVLDLEGKAKSKELELLLEKKLFSAKQGEIFVNVNLNREGTVYLALEKGLDGCHDKIRTAGFNLAKKLVQEKVSKINLDCKEEDPKLVSTLIQGILYSNYNFDKYKTTKLDKEEIEVSLLNAPKALKDKIKELEVVINGVNIARDFVNTRAIDLYPESYANEIVKLFKGSKVKVEVYDKKQIEELGMHALLAVGSGSDKEPRFVVMKYFGNSETDKHITFVGKGLTYDSGGYDLKPGKSMFDMYDDMAGSAAVVGAIKAISDMKLKANVVAVTGLVENLISGHAYKNGDIISSMKGSTIEIGSTDAE... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
EC: 3.4.11.1
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xa... |
A0A7V9CHM5 | MIVNILRFLVVFMSVTGIVQAANPQVKIETTQGDFTVELYPEKAPKTVENFLQYVREGFYEDTIFHRVIQGFMVQGGGISKDLKEKKTRAKINSEANNGLKNQLGTIAMARTADPDSATAQFYINLNDNRFLDFKGLTPNEYGYTVFGKVTEGLDKVVRIGAQPTGANAMFSSDSPKEAVVIKGISIIEPKVTRSSPTK | 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: 199
Sequence Mass (Da): 21961
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A0A172VNL3 | VVVTAHAFIMIFFMVMPIMIGXFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSLTLLLSSSLVEAGAGTGWTVYPPLSSSIAHAGASVDLAIFSLHLAGISSILGAVNFITTIINMRAPGITFDRLPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNLNT | 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... |
A0A8C6BYR0 | MAKRWAPPSSGRLTRSPADVRTHNPGSSSADTSRARDAGPPAGVREPAMGHPRTAPWTVWWPHALEKAGRGRNQVARWEHKTRKLSGAFGSPHLACCTLGGAILLLNVLRSHCFTQAMRSQPRMQSLDNPLAYRTGLALLGVGGVFVLSSFLALGFTGTFLGDYFGILKETRVTTFPFSILDNPMYWGSTANYLGWAIMLLTRCWNVWAGRLPAHGQAAGIRALWMRPHADLRLRRRLWVPASGPPSRRLAQGITPLAPQSSSDLSIFWMRTSSIESCFCRKCSA | Pathway: Lipid metabolism.
Function: Catalyzes the three sequential steps of the methylation pathway for the biosynthesis of phosphatidylcholine, a critical and essential component for membrane structure. Uses S-adenosylmethionine (S-adenosyl-L-methionine, SAM or AdoMet) as the methyl group donor for the methylation of... |
A0A4U1F9P4 | MLGLYFTLLQASEYYEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLIICFIRQIKFHFTSSHHFALTILNSHFTLASMIPIILLVFAAREAAIGLALLVIISNTYGTDYPQLLPNVLLRPPLHTTPNPNNITPSLDTNSKPIPPSQRTTRLKKALHYSTDYITNTPNYNIHRHRTNPILHRNRTERLNAGLYFLFYTLIGSINMPTKYNRISKFSITTTLNPTAIHFLIQHPHITSLTYGLPFPHAFLVRNNQNQLYLFTSNRPKVTHRILFSQPDSTRYRSHPYPTPLKLHRSYRSNNRPWPHSLYTLLPGKLELST... | 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... |
A0A3A0F6Z2 | MRYIAGSSLSDVRCCMVSVVGGKPEDENAFLEALGRRVRERREEAHLTRKRLAELSGLSERYLAQLEAGDGNISILLIRRVAEALACPIEQLIGDRSFDPEIVAALELLRGLRPEQRHEAVIQLQQRFGESSRERSRRIALVGLRGAGKSTLGAQLAARLRVPFHELDQQIEHELGASLGSIFSMYGQDTFREAEARVLDRLTRAHKRCVIATGGSLVLEPRTYELLRERCFTVWLRASPEDHMDRVVAQGDLRPIRGREHAMAELRTILKQRERLYALADAVVDTSGTDEAQSLERLLGLVDSTPSHLPQERAG | 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... |
D1MXC7 | FNNESFNWTGVTQNGTSSACIRRSNNSFFSRLNWLTHLKFKYPALNVTMPNNENFDKLYIWGVHHPGTDNDQIFLYAQASGRITVSTKRSQQTVIPNIGSRPRVRNIPSRISIYWTIVKPGDILLINSTGNLIAPRGYFKIRSGKSSIMRSDAPIGKCNSECITPNGSIPNDKT | Function: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-i... |
A0A0G0R1F1 | MSPQTFIFIGRSGCGKGTQAELLQKRVKEKDQSSEIFYLETGAYFREFLRGEKYSNKLANEIYKKGERQPDFLAVHIWSHILIGDFKGTEHAFFDGICRSLPEATTFTTALEFYGRKAIVIYLNVSREWSEERLLLRGRADDKSKEEIKKRLDWFDKDSYPAVEYFNMHKQYTLLDINGEQSIEKVHADIVGKLGW | Catalytic Activity: AMP + ATP = 2 ADP
EC: 2.7.4.3
Subcellular Location: Cytoplasm
Sequence Length: 196
Sequence Mass (Da): 22850
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A0A8S0VD87 | MANMSAVSPVPLFSLCLYIYGTYGDYGGWLSGHATFYGNKFFVPPNPSLPNNNGGWCNRPVQHFDLAEPAFLQIAHYRAGIVPVSFRRVSCTKKEGIRFTINGHFYFNLVLITNAVVLEVSILRQPKDQEHDGNKCQEIGVKIGRATRISKVKPSCFKSPLVMDHYNVAPLNGERVRVSILVVAGN | Function: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found.
Subcellular Location: Secreted
Sequence Length: 186
Sequence Mass (Da): 20672
Location Topology: Peripheral membrane protein
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A0A6A1WDH9 | MASFSALKATSKVTENCYEKNYGRWPGTLPLSNFWVGALHEYIDETWQGHPLLPKDPYEIAHARFWTKFIDEQCSPGIFKAIQAKEKEREKAVEEVSEQSKAARQGARRKEVF | Function: Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
EC: 2.5.1.18
Subcellular Location: Cytoplasm
Sequence Length: 113
Sequence Mass (Da): 13035
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A0A077KY20 | KQXXAXXAYPLDLFEEGSVTNLFTSXVGNVXGFKAXRXLRXEDIXVPPAYXKTXIGPPHGIQVERDKVNKYGRPXXGCXIKPKLGXXAKNYGRAVYECLRGGLDFTKDDENVNSPG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in... |
A0A496PJ67 | MIETAPRRGLCPALWLDPTCISLCVAWRTVRLNRDPARTRGRSSLSPVAPIPGSQEETVPESKPSRPSESADSDLEKIGNPAKRASAAEERELQRRKAAKAQEYRPVPVWYKAIMFGLMILGLLWIITFYVASLVGVQIPIPGIGNANIFVGFGIALVGFIMMMGWRD | Function: Involved in cell division.
Subcellular Location: Cell membrane
Sequence Length: 168
Sequence Mass (Da): 18536
Location Topology: Multi-pass membrane protein
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A0A8H3IXJ0 | MPLVDYSDSDCSESVISTAKSTRKRKREQESSTDLPPLPDSFHDLYASTVRTSTQDDPRMHGGRQRQTPHVEGNWPTHVYVEFLTCIRNNSPSEKTRVHSLLKSDLGANMPLHISLSRSIVLTTDQRRPFLDALEQGIANSRLAPFTLTLNGLNWVPNYEGNRWFLVLRVNQPECDTLNKLLHVSNAAAAAFQQPLLYANAQNMRSEIHAQGRRRELSDNGRATKVAAVGLHSNTGEDLCSCFHISIAWTLDKPSAPMQQSLEDLVKDKDEFHLQLDVDAIKTKIGNTVTSNSLIIAPSSINEDYLA | Function: Phosphodiesterase responsible for the U6 snRNA 3' end processing. Acts as an exoribonuclease (RNase) responsible for trimming the poly(U) tract of the last nucleotides in the pre-U6 snRNA molecule, leading to the formation of mature U6 snRNA.
EC: 3.1.4.-
Subcellular Location: Nucleus
Sequence Length: 307
Sequ... |
A0A6A1W9J0 | MQKKKDPHIHRLRVTQTEPFSVLRSNMLVKTGMTMTEKILAGASEKSQLSPGENVWVNVDVLMTHDVCGPGAIGIFKKEFGENAKLCPRFCKDSYFSGTKVWDREKIVIIPERYIFTSDERANRNVDILRDFCMEQNIKYFYDIKDLNYKGVCHIALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATAIGNTDAGFVLGAGKLLLNVPPTLRFVMDGEMPDYLLAKDLILQIIGEISVSGATYKSMEFVGTTIEKLTMEERMTLCNMVIEAGAKNGVVPADSTTYKYLEIMSEAMGYGKIKGSSIFLAEYRFDVSKLEPL... | Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Length: 482
Sequence Mass (Da): 53087
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A0A2U8QWN0 | MRITKHFTIYFLLLTSLLIAQNKEEGLFAEIKTNQGTILLSLDFKKTPVTVANFVSLAEGKNDFVDEKLKGKPFYDGLKFHRVIANFMIQGGDPDGTGAGGPGYNFTDEITDLTHEGPGILSMANAGANTNGSQFFITHKETPWLDGKHTVFGHVVEGQDVVDKIKQGDVIEKITIIKKGKEAKKFKAEKVFKAYMKDKEAEDKRIAALNDKSRENFAKVQEEKRKKQVALEEQRKKNKKLRSVPFVQKNRFTSLI | 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: 256
Sequence Mass (Da): 28823
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A0A2B7WIQ0 | MVVRTVLCVAEKPSIAKAIANHLGDRVITHNIQGNPYVKNYEFDYTFPQWGHCSVTMTSVLGHLLSHEFEPQYKSWTSCDPSALFDARIEVFVGSNSKPIADNIKRHARRADVLFIWTDCDREGEHIGTEIRSVAAQSNQALGRAGGTVRAHFSNIERTHIIHAAHRPAELDEAQANAVASRIELDLRVGASFTRHLTLSLRPVLQRGNLSEASQLISYGSCQFPTLGFIVERYWRVRNFIPEPFWSIKLYRRAKIQRIDYVGTMLFVGSATSLLIPVTWGGVMYSWISWRTLVPMLIGAVGLIAFILYEMYMAVDPLIP... | 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... |
A0A7I6HH47 | MMLVIYGLFMLIPIFMMFGLWISLFYYLWLLFFFLILFYFVIFHLLLDIQWVLICFLLMMIFLSFWIIYLMLVNVNKYLYFEDLYFMLLLLLFCLFMTFISLNLFYFYVFFEFSLIPVFLIIFGWGYQPERLSSGFYLIFYTLFVSLPVLIVIFFIFHDYGCLFMEVMNCNNFYFYVFFVMFFMVKMPMFMIHFWLPKAHVEAPIFGSMILAGVLLKLGGYGLFRVIKFMFFFEFSYFIYSLSLIGIIYMAVSCLYQSDMKSMIAYSSIVHMGLVICGIMSYNYFSWFGCLILMLGHGYCSSMLFYLAYLVYCRSFSRNF... | 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... |
C7MC10 | MRLRDTGAVDITELTGKILGRREKDCDPLRIVQAGHPALRRRAVRARERLEDGRLEVALLLELAEAMTVTMRAAPGVGLAAPQVGLPLSFYVIEDRYADEPGEDEVGDLLERRPLPLRALLDPVLEPLGTQRVYAFEGCLSVDGWQSIVPRSRRVLLRATELLGDGSLREVEEEHVGWTARILQHETDHLAGTLCHDLCVPRSYIDARYGSRYDDLGEAVRRLGLSGEIAELGPGEVMTS | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic ... |
A0A1X7KAU7 | MRSILFSAILFLFVFEGCEPKGKEIEPDNDFEISVPSYFGSFNERIPENNPITTKGFELGRMLFYEKKLSGDNSMSCASCHQQNKAFTDGKAVSPGIDGISGEFSSMSLVNLLWAEHFTWNGKMESVEVQSTEPIRNPIEMHENFDDAIRELEEEGYQRLFQEAFETEVITEELIGRALAQFQRALISSNSKYDQYLRGEYEPTPSERRGEQLFFTHPIPGQLRGGNCGDCHLGPLTSGAIDEFQGFHNNGLDNDENMKDGLMRVTGNPADKGRFKTPSLRNIALTAPYMHDGRFETLEEVIEHYDNGIHQSSTLDILII... | PTM: Binds 2 heme groups per subunit.
Cofactor: Binds 2 heme groups.
Subcellular Location: Periplasm
Sequence Length: 372
Sequence Mass (Da): 42150
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A0A1I6M477 | MTFKRKHIIALIATLATVSALVAAAAFPALERHYMRQQAERDAVPLKLAVESLRATLDRYAPLPALIAERPALVELLSQPENARLADAVNEDLRQTAATVRASDVYLMDITGRTIAAASYREPASFLGRNFSYQSYFTQALNGFLSSFSVYGTTTGERGYFYAAPVEDGERIVGVLAIKFNISAFESIWRGTDSEIMVWDRNDFVFMSSRPDWHFRAIRPLSEATRRVIAQNLQYPIDRIDLLPITTTRLGEDAQLIEFEGDTNGSYVLTSQRLSDLDWTMASLTPRLPVTLQALNTLVIAGLIVVLGLVGLLAFLLRQA... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 592
Sequence Mass (Da): 65208
Location Topology: Multi-pass membrane protein
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A0A397U3D5 | YIILCFMTILGAMLRLWCFKILKEFFTFTIEIKRNHKLITTGPYRLLIHPSYTGIFLLLPINIYMIDQIQPYVHLYFPYFINYILYNEWIRIIGYVFAIWMFWNRVRTEERMLKNHFKEEWDDYASKRKRFIPWI | Catalytic Activity: [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S-adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + S-adenosyl-L-homocysteine
EC: 2.1.1.100
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 135
Sequence Mass (Da): 16892
Location To... |
A0A397UL03 | MYYFITQYPSRTLVFVNSIDAIRQLIPIMRLLNIEVFGLYAQMQQRQRLKNLDRFKQNLNAVMVASDVAARGLDIPLVEHMIHY | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 84
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): 9915
|
A0A3N5MF07 | MLTQIYEVSSPAEAEAISNIGVDHVGVLVGDGRFPGEQPIIAAEKVAAAIIPPSKLSALFLTHDISLIGEWARRLRPPIVHLGAAPELLPPSQVVKLKESLPESLIMRSVPVSGEESIVIAKSYGGVADFLLLDSYRPADQQIGALGITHDWTISRRIVELSSVPVILAGGLGPDNVADAIRKVGPAGVDSKTKTDRDGSHAKDLQRVRRFHESARAIRCDPTGDARTPE | 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: 230
Sequence Mass (Da): 24551
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A0A8S0R4N6 | MMFRMKINSSLESNTLSRHELILQRLARLGVPKENLCQGPRGLVAYVKTDKSQIAEFVSAILPTDEEAAEAVSETRGGSIKEADEDVFCESMIWLQWLMFDGDPSLALEHLAKMNANQRGVCGAVWGNDDLAYRCRTCEHDSTCAICVP | Pathway: Protein modification; protein ubiquitination.
Function: Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
... |
A0A4Q3TKN0 | MSVVMISTMVLCFALTISVAVSIGLSAVLGIQASNANMLISVKEMFNSINKFPLAAIPFFILAGNLMETG | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 70
Sequence Mass (Da): 7353
Location Topology: Multi-pass membrane protein
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A0A7V5K1L5 | EIYQFDKSKPLVSFFPGSREREITRHIPMFLKIFENLKKLNPHIQGIMVKAPGLKDSFLWDKAKSQIKVIENTQYEVLKYSTVALLASGTITLEAALLETPAIVTYSLPSWMYFIAKKLVKVPYISLANLILQKEIYPEVIKGKDKIGVITHKIKELIDNEEARMEIKKELSTIKKLISPPGASWRIAEDMIKYILSLKKG | 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... |
A0A6J1WEL8 | MPKRLPTDLKYILKWTQAFSHYDSPIFKNGQEALLKYNCTYRNCYFTGDKSLLPDIRYFDAILFDVENYWDYNPILRSPHQKYIFVGLESADNFPVILPKYDAYYNLTWTYKLDSDIFGAYLIVLDKKGNIVGPKVNMEWINPMLPTSDNIRKKLLVKRKAAAWFVSNCKTKGRREVVAKNLSKELLKYGLSIDIYGWCGRLICSKDHMYDCLEDLENDYYFYLAFENSLAEDYVTEKILYPLLHYTVPIVYGGANYSRFLPPGSYIDAGKLNASQVASLISQAIVNPKLYAEYFRIGRRPKLGEAKTLRLCIRTSPLIG... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 328
Sequence Mass (Da): 38046
Location Topology: Single-pass type II membrane protein
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A0A224XEZ8 | MSLKLAYRHLFVVGVLLLPCSAFLIQDTREISSVEGRGRLLSRTLRSTGKVPKTWPGGVVPFVVDKTLIVYPAYRRVIQKAMNNIEKKSCVRFKYRTKEKDYIRLVLSKRCSSNIGKKGGRQILRLHVSCVNIGIVLHELMHALGFNHEHTRYDRDKYLIVHKNNLPEDVHRKYEARPSNTFQTMTGYSYNSIMHYSRKDESLNGKDTLVPIKPGIKLIPAYKKTSLSPIDVKRINILYPCTNLS | Cofactor: Binds 1 zinc ion per subunit.
Function: Zinc metalloprotease. Provoques deadhesion of endothelial cells from cell cultures, and also degradation of fibronectin, fibrinogen and gelatin in vitro. Its role in the venom is not fully understood but it might act as a spreading factor that facilitates diffusion of o... |
A0A6J1W888 | MSNNKVEPKKKAPEENEENVVKPRTNISDLINTIQLALIFEHCFGIYRFHTVDNGLQPTNGKMKLVGILITSAHIVIFYCFLKLPSAITGTGNLVDTMDEVPSIVILLQYVTSAIMTSFLLSGANINIFTTFANLDSMLHINTNQDFYKASRSRTFKYIIVLAVYHIFVSISDLMTSDEISLSKIMVLPIFFEENLEILIFCLIISMLRSRLIVINKYLINFMNDKENSKNSVFVVGERKPTPKENFNLIGRMSSKNMKIRDLAVTYDIIGETCCLINQVFNFQIFMTLVSTFTYIIITIWTSLFYYRTPKATFSSLITI... | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 417
Sequence Mass (Da): 47889
Location Topology: Multi-pass membrane protein
|
A0A7X9AF00 | MTPPQTLLFAANSPGEIAGWLRPLVREARRRWPATRLVVILLPCTFASGSEGRVALDLVGVDEVLPASRFLRLLAWEGDRFRGATLVHLGGDLMYSALLSWRWGLRAWSYLWGRWWWDRAFRGYFVKDPAGLTWLTRRRISAAKAHLVGDLVADAVQASLEESPPTPPPSGRRLSFLPGSRGHEVENLAPFFLEVAEGLAQGRPDLEFQMLLSPFLERELAEQALQAPPHPQVGGRQGRLQGDMLVSPSGVGVRIVREGNLSALAKSTLALTIPGTKTAEAACLGVPHLMLLPLNRPELLPFVGLLGLLDWLPGGNRLKG... | 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... |
A0A8C6C146 | MDRWYLGGSPKEDVDPFSYDYETVRNGGLIFAALAFIVGLIIILRSPPVDAGGKAVEMGELASSGPGKLQCTWSQAKGGNQPPLDTPSPRSGRFLGLSYISAHLILLATLRDGHQCHHFADEKPGPP | Function: May be involved in forming the receptor site for cardiac glycoside binding or may modulate the transport function of the sodium ATPase.
Subcellular Location: Membrane
Sequence Length: 127
Sequence Mass (Da): 13617
Location Topology: Single-pass type III membrane protein
|
A0A7K4LJB8 | MGEPSDLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVGGDVPETNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKVGAAH | Catalytic Activity: H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Cytoplasm
Sequence Length: 147
Sequence Mass (Da): 16849
|
A0A7S0G4G3 | MRMGSPRSWTYGFVRTVHVSRASMAEEKRAAVNEIDKRTFVLRVKTHAVRVQPKLTETARLLLDPELLRVPKLRYLVKRTESSFLLLLKYVNSIEGDPSLPLGNVVLAGEKTKEQVLASLRQTVEEQKHSIKKRITELPESALNAVSSLTVEDLDEHEIEVGYDYWNWSVVLKKSLPDEFLCPSSYEQVGHIIHLNLRDDQLPHRYLIGNVLMEKIKGTRTVVNKVEPTGGAFRLFQMERLAGEDDFLAQVKENGCVYEMDFSKLYWNSRLEGEHRRIVEMLTEKDILADAFAGVGPFVIPAAKLKNVKSYGNDLNPASV... | Function: Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs an... |
A0A6A1VHW3 | MASKRNVQYSRLPTDEDYDNDGISRRQYDPRFDYTPKALDKIPWKSIVLALFLLFLGSLLLFLSYFILSGHMGGERSQAYGLLALGILSFLPGMLKHFSFITAKMVNQRLYVDH | Function: Involved in trafficking and recycling of synaptic vesicles.
Subcellular Location: Cytoplasmic vesicle
Sequence Length: 114
Sequence Mass (Da): 13124
Location Topology: Multi-pass membrane protein
|
A0A961ZA07 | NEQRAFALNRDGARLLARVAAERGVPIVHMSTVNVFDGTKPTPYVEDDAVAPLSVYGRSKLAGEVDVRVANTRHVILRTSWIYSTTPGTFLPNVLARARAGEILRIIADQHGSPTYAPDLAAAVLEIAAKAYAARTDASSSLWGTYHIANSGPPASWYALTEAACHAAELHEPARQIIAITSADMPTRAPRPLNAALDTGRLLKMHGLELRDWREAVAEAARSLVPSA | Cofactor: Binds 1 Mg(2+) ion per monomer.
Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Seque... |
A0A7J5BCN4 | MTIIASADGSALGNPGPAGWAWYVDDDHWAAGGWEHSTNNRGELQAVLELLNATADRDEPLRILCDSQYVINSVTKWMPGWKRKGWKKSDGKPVLNRDQLEQIDAALQGRDVQFEWVKGHAGHHMNEAADERAHGAALAIQAGRAVDAGPGFAASAAPSFADTAAASTADTLADTPADTPSDTPADAAPSSSAASDALAAERLLADARGARDIATGRSLLDEGCRIIGSRALLPAAGDQLRSAAASAVTDDVTIVTYETRSPTVAAHSSVWVRREGHWLLSLHHVSSGGLA | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subcellular Location: Cytoplasm
Sequence... |
A0A8C6B8E1 | MAQLGAVLALAASFLCASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFLVPHAGVPAIAPRPPRKVHPLFQRMSCLCRKIKDWWELVPQPLTSPSGAVFIPLQAVRVTKPNIPEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKRISEIEDAAFLAREKAKADAECYTAMKIAEANKLKLTPEYLQLMKYKAIASSSKIYFGKDIPDMFVDSAGSLGKHLEALADKPSFGLEEEPSEADTE... | Function: Mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs). Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 322
Sequence Mass (Da)... |
A0A3N5M3D5 | MVDEARVRPLIAGNWKMNGSMASLAEALAVRDRLREPQFAPGVDVMISPPAPFLAVLVREATGGRLLFAGQDCHAAPRGAHTGDISAEMLKDVGASAVIVGHSERRADHAERDRDVRAKVEAAHRAQLTAI | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 131
Sequence Mass (Da): 14012
|
A0A159IMB0 | TLYFLFGIWSGMLGSSLSMLIRLELSSISNLIGNDQIYNVIVTAXXXIMIFFTVMPILIGGFGNWLIPIMLGAPDMAFPRMNNMSFWLLPPSISLLLISSMVETGTGTGWTVYPPLSSIIAHTGTSVDFSIFSLHMAGISSILGAINFISTMLNMKIKFMKFDQISLFIWS | 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... |
A0A4U1FVD1 | MSGVAGTKGGERETGQGQMLGRLQGPAVQSRGWQDRGWTRRGNGPPPHPGLQPLMRSPLGSGGLGALLGPTVQAPGSESGPGRLVRRPPPPPQTTGVALRTSRGGTWRHFELLGSPHLPPPLLPGRFTGYRFLAPSTPGNRLSPTVFLGKSRRHRLPLGSPDVRPPVPAPLETELGGQRGLSGGPRAATPPGAVWDMSAVAPQGPTAGQPRAGWPRGLKAGSGSAPARGGCDLEGAGLLGSAALSGPLTLRRDVGLWLCDPKPAPPALWNLVSCGSTEHEATMRFWATCPSLSTIYFLFVTFAGSTIFHCLQRLARVPAP... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: ganglioside GM1 + GDP-beta-L-fucose = ganglioside Fuc-GM1 + GDP + H(+)
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 607
Sequence Mass (Da): 65856
Location Topology: Single-pass type II membrane protein
|
A0A142XFT9 | MHASTDPSRLFFGHPCEILHKEAIVARTTGEGMSVTPVQTPGGIEPAFDLTAYYPILIYAVVCVLFAVGAIAGTHLFPFKPRKPTKIKQMPYESGMDPIGSARMQFDIKFYLIAILFLVFDVELLFLYPWAVIAYGEGGDQTWRTVFGTVVFLEIMVFLVTFVIAYVYAWKKGVFQWR | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
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