ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A498IZL9 | MENSTATMRSICLRDMGTYMTPTASQKPSRTTTPIRATTPAARNPISSGSSTPTSHCGRRSSTAKRYAEESNACKNLSENLSLDQGTMEEVFTDFKGFRAGLIKALTTDVERFSQQCDPEKENLCLYGFPNEE | 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: 133
Domain: The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence Mass (Da): 14658... |
A0A1F6QLN3 | MSNIRVKICGITSVYDARMVCSFPIHAIGLNFVKRSKRRISLRTAREILAKIPPLIEPVLIFEDERLSEVIYTAATLGISTLQLHGTETVSYCHDLKRFNKHLKIIKALPTREASVNQLNAYKKVCDCFLLDSFDRKNQMGGTGKPSDWNIAQEIVSKTRLPVMLAGGLNPYNVNSVIKRVKPFGIDVNSGVESRVGKKDKSIIERLFEELNS | 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: 213
Sequence Mass (Da): 23947
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A0A2R2WZF8 | MYFLLRHLAFTDLGYSTTVGPKMLVNFVVDQNTISYGFCAIQMAFFLVFIVSEIFILSAMSYDRYVAICNPLLYPVIMSQRICQLLVAIPYLYSTVIALLITIKIFNLSFCGYNVVRHFYCDSLLMLSLLCSNTHEIEMIILILAGFDLISSLLIVLVSYFLILVSILRMNSAGGRH | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Membrane
Sequence Length: 177
Sequence Mass (Da): 20084
Location Topology: Multi-pass membrane protein
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A0A932VW41 | MRVSALILAGGESQRMGQDKRFLKLQGQPLIERTFQAATKVAAEVLILVAKSEDQQKIIELLGSEHRFLIDENPNSGPLGALIGGLQAMSGDYGLLLAVDFPLLTSDFLSKMQEYLQGLQPQPRALIPIDKENLQVTCALYHKSLYSELKDAFESGELSLYRWIEKNPEGIATLTPSVWQRWGIRENFTDVNRPDELQRLLNAIESGHNMSDNSQ | 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... |
A7SR81 | VVELNTFFLKHILYIPTRHWLNWSRIFLISLVVAPSLRQYYSYVTDTRSKRVGTQCWVLIAITLMECLICIKYGLALFKKTEMTLIAMWLLFQLVSLQMLLCMGVLYFMVMTKSKDGKVVKAKIMEKVRFFKKFGRRKELESIPADDPTSKTIHYLVTNGHHMTENGDTANQGASNGHVKSKEAKDLTNGVDYLIPPSPDHGSSRKRKPKQNDGMTTRLRSRKSQAGV | Pathway: Lipid metabolism.
Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) is replaced by L-serine.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine
EC: 2.7.8.29
Subcellula... |
A0A6A2ZDY2 | MMTKQFTRTPSGLPHPQTPHLDRTGRKEKEVTAFDPRANDFDLMYDQVKALKSGIAVEKPICNHVTGLLDPPELIKPPKILVIDGLHPMFDERVRDLLDFSIYLDISNEVKFAWKIQRDMAERGHSLESIKASSESRKPDFDAYIDPQKQYADAVIEVLPTQLIPDDNEGKVLRVRLIMKEGVEHFSPVYLFDEGSTISRIQCGRKLTCSYPGIKFAYGPNSYFGNEVFFLLLRASLNSGVVYFLLTQFDRLDELIYVESHLSNLSTKFNGEVTQQMLKHSDFPGSNNGTGLFQTIVGLKIRDLYEQITTTKTAAPLEET... | 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: 322
Sequence Mass (Da): 36509
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A0A2M7RPT0 | MNIILIGMRGSGKTTIGKMLAEKLNMGFIETDAIIEKKIGESIIDIIEKSGWQKFRKIEHCIIKEVSFLNNCIISTGGGVVLNNKNVKLLKNNGIIIWLDTDVNILINRIGNNYHRPFLTNKKTAKEDITEAYNNRIIFYKNASSVKIVNNDYPIATVNIIINLFLKLDPYVKFKN | 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... |
A0A7R9IQ49 | MFKIRFSLMPLDGHLAISLLKDSSSPTERSHFDLEAVGLHKLPDWDQYRREEKEGEFIQSRHIKRVLEGVATKEEQAHATVSIAQLAKHLLKCNSRPTEKPQYVVPGINLFCGNLGLYSGDEVKKLCLSKIDDMELDLIIKKIKTISAGQLSYWLGAALHDRKECMLLLVDRASHRHKFDNRFKGVVHPHVCRVRTDIADLCLNNYDQVNAFENVVTVAKHLCGAATVALPVLTENWLLLLWHFVVIIDEHGFTPAEFGVLCGIVSWATCGSGRSRSSISSENGLNERYIRLNLTQEDRKDIGRACKLILDFGRLQFLKE... | 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: 346
Sequence Mass (D... |
A0A1Q3RJX6 | MYINRIFIKKGLRILGVFVGLVFALAIIVSLPTIVRGYDMYKNAISSEPIEIKVMTIKSDENYLRLSEIPKEYTEALIDSEDQRFYSHIGIDFQSTFRAVLENIKAKSYVQGGSTITQQLAKNMYFTFEKRLDRKVAELLVAFKLEQTFSKDDILELYCNVTYMGNGCYGINEASRYYFDKAPDELTQEEIEQLVQTIKNPGYRNPNSLSEDGTL | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 2.4.1.129
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [... |
A7S7U8 | MDRITLFDADVLKEIDYSKGDCKMNQYGLSCESPGEDLRLRPLASDDYNKGFMDLLSQLTKIGNVTEEKFLKRFNAMRDHHGTYYIIVVENTKADKILASGSLIVEQKFIHEIALRGRIEDIVVDDSCRGRRIGQLIVETLLLLSEKLGCYKTSLECRDPLLGFYKKFGFQGEKDQNHLIKRFFH | Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Leng... |
A0A6A0H0G8 | MRLPRHLHVPSLQDYHVIFMYQPDERCLVFDLDSDLPFPTYFHKYVTETLRTDHILHPEHHRWFRVLPALVYLQKFASDRRHMRHADGSWLQPPPPHPAIRAQATRNKGANCKTIVPTARQ | Function: Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by t... |
A0A2S1B956 | MKIGKYTVYAPFLAGCDESDLYQQLRSGDRIWLFDRVAPSDENNEMAELMMGTIFPDRCFRMLRLNKNEKSIRIIEFKGHHLSKQQALAWRTAHPVMYPQKAQQNSQEQK | Function: Involved in fatty acylation of protoxin at internal lysine residues, thereby converting it to the active toxin.
EC: 2.3.1.-
Subcellular Location: Cytoplasm
Sequence Length: 110
Sequence Mass (Da): 12937
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A0A6A3C6W6 | MAAENRSDGGINPTPCYLQKFRLYETRSVKLSVSGKDVKLTLIARRSRHYAGTRYLKRGVNEKGKVANDVETEQIVFEDVPEGCPTQISCVVQNRGSIPLFWSQETSRLNLKPDIICRPWLTRCEKKPRETILRTEFAKSIRFINKILSKEKRLRFLHWDLNRHSRKATNVLELLGKVADYALKLTGIFYCQVTPNRIPEGLLNLSCLVQNDEHLVQIHSDKSDDKQNSIENLHAMGFTESQTIDQNSPLAEDLMVVYEKMGDTLALQYGGSAAHNKIFCQRRGQWQAATQSQEFFRSLQRYYSNAYMDAESKVPLICHF... | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + phosphate
Subcellular Location: Vacuole membrane
Sequence Length: 548
Sequence Mass (Da): 62429
Location Topology: Peripheral membrane protein
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A7STD5 | MGQRAHDKTKLILSYSIFCDTHYYSYACDKYCKYTDDKHGHYQCDLHGNKVCLPGWYIPQGNCIKYCVPQNDDIRGHYSCDSKGNKVCRRGWYGPL | Function: Putative Notch ligand involved in the mediation of Notch signaling.
Subcellular Location: Membrane
Sequence Length: 96
Sequence Mass (Da): 11210
Location Topology: Single-pass type I membrane protein
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A0A0G0BS71 | MLIVLTEYNSPMLKYPVIGLSPMDGVTDIVFRRIVDECSYPDVLYTEFVPVDGIILERPRLLKMLEFHKTKTPVFAQLFGNDPDNFYQVTKMLVNKGYAGIDINMGCPDEHVFKKGGGAALILKPEVAKKIILAVRKSIADNTDKKLMVTLKTRTGYDKADTYNWISHLLEVSPDIITIHGRTFFQKYSGLADWEEIRTAVKLAKNTKTKIFGNGDIKNMEMAKKIIKDYGVDGVLIGRASLGNPWIFGSHVSTQEEKLKMMIRHCELYNKYFPEGNFKSLRKHFIWYVKSLPSSSYLKNDLMKANNVDDVKKIVDLYTS... | Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
EC: 1.3.1.-
Catalytic Activity: a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA + H(+) + NADH
Sequence Length: 326
Sequence Mass (Da): ... |
A0A498ITF3 | MKLCSSTLSVVLVLLELFMIDVVSSTKLPVTAASLNVKKPQAKAVRAEDLLSFNHYVKTCPQAEGIIQQKVGDWIQKDFTLAASIIRLHFHDCVVRGCDASILLNHQANERRAFASRTLRGFEVIDDIKAELERQCPKTVSCADILTAATRDATIIAGGPFWEVPFGRKDGKISILKEADMVPQGQENITQLINFFQARGLNMLDLVTLSGAHTMGRSSCHAFKHRLSNFNGTRKPDPSLNSMYLNNFLKKKCKNDLDLVYLDAITPKTFDPMYYSNLNKKLGLLSTDQLLKSDKRTGPFVTALASQPSLFESQFSVSMV... | 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/... |
A0A931PSC7 | MQSSSSKSRAVSAIVLAGGKSSRMETDKALLQIEGEYLIQRIVRQLKAHFSEIIVTTGETRRYTDLLDVPVLEDKIKNCGPMGGLYTGLQAATNEYSFVTACDMPFLNPALVEFLIAQIDGTADVIVPEVGGVRCVTRAIYGKRCLSTIEKLVGQRRLSLQALVDTAPAWVISESELHKIDPNSSSFMGFNIIEEWKEVRRRIERYSNRE | 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... |
A0A2P4W4T0 | MPHIEIFREPVYRTYRSSECSWAAFYIKLINIFRYFLPILIIFLTDGLWKXTNTFREVPDVSVTGDFIVYAFVCSLPETESKSEYSIPNEHSKSIN | 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: ... |
B7SMP4 | MKMNSMKTLLMLMMFMSTMLTISSTNWMGMWMGMEMNLMAFIPYMTVMKNKKSSKAIMIYFMVQSMGSMIMLFGILMNSFITISYLMEKEIVMMTIMLGLILKMGAAPLHFWMVEMAQHMNWSSLMILMSWQKIAPMYVLSNMITMNLFTVIIIIMSAMVGAIGGINNTNLQKIMTFSSINHMSWMLLMMINKTQWMVYLMIYSIMVIMACSFFKKFKANYLNQLNIIPMSMMEKYTLASILLSMGGLPPFLGFLPKWMVIESMINSNLMILITLLMMLSLITLFYYMRMVSSLLMMFNANNKWMVINKNNISMIFIINC... | 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... |
A7RMP9 | MSNKVFTLSSNELVNFELDSDEEDVDKIIERRRRQRQAIVRKYLPPGATPGSLPPSAATSVTSQGASDDSDSDENSTDSEDSDTVEKRATADLESDLAFADQEDGENKSEGKENEQQEGEEETSKNGDMFAKDDMFSEHYSSPANAMMKIDSTKENPNLTDNWDDADGYYRVRIGELLDKRYNVYGFSGSGVFSNVVRARDQARGSQEVVVKIIRNNEMMHKTGLKELEFLKKLNDADPDDKYHCLRLYRHFFHKNHLCLVFESLHMNLREVLRKYGQNVGLHIKAVRSYSQQLFLALKLMKRTGILHADIKPDNILVND... | Function: Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF.
EC: 2.7.11.1
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Length: 502
Sequence Mass (Da): 57484
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A0A261AMR8 | HSTIRPLSYDNVWNRRLSRQSNNVKVDEEWDWILKTRSKTVLISFGSFMLSKDMRLEYKKALARAMATFPEVTFIWKYESDDTTSFAQGIKNIHFPKWIPQTALLGDSRLLAFFTHGGLGSVNEVSYLGKPSVLCPIFADQMRNAKMLARHNESIEISKYELADSNKIEEVFRNILFDKSYRLASETLALQLANQPVKPKELLVRHAEFAARFGRLPSLDPFSRHMSFIEYFLIDIAFVGLISLLLISFVLFLITKRTFTGNEK | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 264
Sequence Mass (Da): 30467
Location Topology: Single-pass membrane protein
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A7SHY0 | MGPGEISHIWRQFSYKQGDLYHNEGPQVFRVRDFAFSCDRDTESSREHKRRDSGEMLRTNLKVFRVAGPSVFLRSGYEFSRRTHAGFEKMLRMNCTLVSQSLERRFTNECVVASYHGSEKETFDAWDRESVEAESGGHVSVVFKRYRNPTRRRYDGHCCEHVFWSRCGTCDTYLKICLTDFANPRSIKHCPLGSVRTKRLGRDDFRFHLRITRAFTRFKGNIGLYVESWDHDTFTADDLVDKLSLTLHLTRPDPNNHVTSLYRRTLQGRRASLSAELNVYCDPHYYGTACATYCRARDDQYGHYTCNLHGEKVCRPTWHG... | Function: Putative Notch ligand involved in the mediation of Notch signaling.
Subcellular Location: Membrane
Sequence Length: 663
Sequence Mass (Da): 75645
Location Topology: Single-pass type I membrane protein
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A0A3M7QER9 | MKLHCQNMDNFTFSWIIFKLNCPEQVPRIQNYFEKNKSIQKKTSINNSIFESSNNTKTKCDISFINPHENVLIKTNFTQNFQPFQTEINYDRTEEDLSFMKNLNIGGQFEPKDCEPVSRVAIVIPYKNREHNLRMFLYNMHPFLQKQRLKYTIFVVEQVNSDKFNKGKVNNAAFIEIIQKSTKNFTLASDFECVVYHDVDLLPTSFLNFYTCPEKRPKHLSIIVGKSDYRIYYPILVGGVIFFRIENYVQVNGYSNRFWGWGAEDDDMFYRLRSTHLGFDRPKNNTVYKMLTHEKQKKNPLRVKLLREGKDKYQNDGLNS... | Pathway: Protein modification; protein glycosylation.
Function: Catalyses the transfer of galactose onto proteins or lipids.
EC: 2.4.1.-
Subcellular Location: Membrane
Sequence Length: 362
Sequence Mass (Da): 42864
Location Topology: Single-pass type II membrane protein
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A0A261AA57 | FRNLQPIMGTKLSVSLEGANSPEVAPRVDRPPTFDPQYGFERPRKATWEEMEQWKLKPAQRDYCAHHLISLMKCQTQNAPFAGHACDGERGAWDKCEYEDHISRIKEFERERRLLQRQARKEAVKMSIDIQKIVQATLVGKPEHDEQTFIDCLKLVGSNRSPKEKELGFALLSRMVIKTSPQSLRLVQTRLANRFAQISDHFQFSGALFVREVLVRNPTAGDLHSVTVFKIILNSIDAGVQSMDPTVRSLAAELFGLRVSNQNLISLGYAPRVDKSNVDKRLSVDRKDIIRVIEMGIRSQSTTRSAAFTALRSLCLNAKY... | 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.
... |
A7RU19 | MSENTPLPIPERAIYGFVLYLGTYLGFALYLVWAFVREEWLQSIGITYLPQRYWLVAGPVYLLVAFLIVVWFYFAHYLKSTPSLDSINTIADEHSRFLVDQEMTDSSMPPLADVPIYQVNKKLYLLDNY | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.
Subcellular Location: Membrane
Sequence Length: 129
Sequence Mass (Da... |
A0A238F8J1 | MSKTKGTPVLETSMGTISFEMYTDHAPKTCRNFVELCNKGYYSGTVFHRIIGDFMVQGGDPTGTGRGGTSIYGASFEDEIHPELRFTGAGILAMANAGPNSNGSQFFITLGKLQPIRPFL | 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: 120
Sequence Mass (Da): 12961
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A0A6H9WJN8 | MPNTACLSENRIGPPSSLKLIPRWHAARHRRRRQRCGDTLGSGAALMEFSKLREITVVVFTRLRRRVAGFGAELFAMQVALIIVVAAVFTSAAATAQVALVRDDAEDDIRALAISAASLPTVVEGLRSDDPTSTIQPVMDALRLASGVEYITVVDMHGIRVSHPDRSQIGRPVSTDHSQVRLGHEFVGTEEGTLGVTFRAKVPVRDAAGAIIGTLSVGMLESDLARDVADRTWQLVGVALAAVIAGSLLSWVATRMIRRRLYGVDPRELRTLLQTREGMIAGVSDGFVAVDASGRVALANRAAEDMLGVRDILGRDAASA... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 618
Sequence Mass (Da): 64863
Location Topology: Multi-pass membrane protein
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W6KFF3 | MQNFWIKDNYLFHTPEVEFSNRCALRVTTVLGKEYLWTCSENFNEAYLYGDPMGVIPYFSIYQDARDEKGRISEITFTLSIPINNLGDILSEAGQAASSTDPSTDPVFDAVSHVEFLPEFVYRIHHPLVRLNMTAAPLLRFTRPLFHSPTGTASPLASNSGPLCGFTEADLWFHSTVRLPRSTSRKERGHHALERSPFVEDATELAVLYDLPSFARRYTSRAQRVETRMITETSGGLGLFAGGETVRGVWQDSQLLHAFTWRIRLRVQPAQLFYRPSFAEALKSAWVQYFAIAYVIQWVLWWVRGFVVVNGVVDTRAVFT... | 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: ... |
A0A1G2HHX0 | MDKQLDKLNKLEDKRQLETINLIASENYVSPAIREAMSSRLTNKYSEGYPGARYYPGNQYVDEVETLAQKEALKTFNLKNSTWGVNVQPYSGSPANFAVYAAVLEKNDTALGMALSSGGHLTHGFKVSHSGRFFNFFQYGVDKNGLLNYEEVENLAQKYKPRLIVCGASAYSRIINFIKLSKIAKKYNTLLMVDIAHIAGLVATGVHPSPFSAKSGQALADIVTTTTHKTLRGPRGAIIFGRAELMPAINKSIFPGHQGGPHNHQTLAIAQAFIEAQTPKFKQYTVQIIKNTKTLAKELQKLNFNIVSGGTDNHLFLLDL... | Pathway: Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1.
Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of ... |
A0A8T3Z1M5 | MDYKKTLEKFKPLIIIILLFSVVFFLRAEAYNISGAPDQSQDFYKDASGLPYFSEMDSYYNYRLTLNYLEKGMLGDTNINGSDWDLHSYYPPGRAVDYPPLIVYMTSFFYNVANLFGDIPLANVAFWTGAIIGSLCVIPAYLFVRRITNDYGGIAAGILVGTAPTYFAHTYAGFFDTDMFNILLPLLVIWFFVESILAKDIKTRAIFAALSAISLMVFSLAWVGYIFYLSILVMFVIAYLIVARFVLNDTKPVIEYPNKLKWFLDQKELFALGIVLVIGGLFVGIFNGFASILNSLYGLIGVNEIQALAQATSYPNVYVS... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
EC: 2.4.99.21
Subcellular Locat... |
A0A6A3AQ33 | MLVTTLLPTPTKSGSTKSKSHNSPSTSESNGDSNTNLIMAGVGDPYYNRTMQRPWGDHGGKATPPHDDGVVASGAWGTPSPVPPWRTTYSFATPSPTMPLGINTGTFTYEELSAATGGFSEANLLGQGGFGFVHKGVLPSGKEIAVKSLKAGSGQGEREFQAEVEIISRVHHRYLVSLVGYCMGRHQRMLVYEFLPKKTLEYHLHGSAKGLAYLHEDCHPRIIHRDIKSANILLDYSFEAKVSSLKIEPEFLSRHSLTGSHTVCIFVIGGDFGLARLSEDNHTHVSTRVMGTFGYLAPEYASSGKLTEKSDVYSFGVMLL... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 837
Sequence Mass (Da): 91525
Location Topology: Single-pass membrane protein
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A0A8B7N9K8 | MAARPGRRTNAEGSCRKPPAEDEAGLVAVPELLSNSKCHDSRSSCPTERLRGSSQNPPHWDQKLLPARYFLAAFQYYRERFHNCLFIVITEPGEYEWCRQNLARNSTDVIVADDKCHAQQDFALLSTFKHFIYSFGTFGILGIFLSNAKTVVYPHAAMDGKNLRYFFIQI | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 170
Sequence Mass (Da): 19381
Location Topology: Single-pass type II membrane protein
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A7SN85 | QSYVVCELPDKLNFLFSFIRNHLKSKILVFVSSCKQVKFIYEGFRRLRPGIPLMALYGKQKQLKRVAIYDEFCKKTQCVLFATDIAARGLGEC | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 93
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): 10769
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A0A498HFE6 | MHFHDCFVRGCDGSVLLNSTSNSHAEKETIPNQSLRGFHVIDAVKSAVEEKCPGVVSCADILALVARDAVRIINHSH | Cofactor: Binds 2 calcium ions per subunit.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Length: 77
Sequence Mass (Da): 8354
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A0A6A2Z6I1 | MLLYPLQFKLLSLTYLLLAKYLQAGTFDLVGTIIYEIDQQPFQSIFYNGTIEVAEAGGFLSVESVFLVTLGIALLVLLGLWLHGQFQRISKKTKRAPKVEVGTRATEASMDEWLQGTAYTQSASKSKKK | Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facil... |
A0A498IRB9 | MWLHVGVFHVLANMLNLVFIGIRLEQEFGFWYASGFLASCMLSCIQKKKKKGETFMERGQPAAPSSLEIKVVSPRRSDNVVHPAGQPPETTTPRRSFSDYNLLKRWVSWLVSSIVVANIVVFVVTMFVNDCPKNSDACIGRFLGRLSFQPFKENNVKLSLFYLLGCGLWGTAGVAANPFHVRKDGCSRRSESGSLTPGMAADLIGEQRKEFIHRRWGSNFSFRHIRIGFLYLMSGFGGSLLSALFIQYGIYVGASGALFGLLGSMLSELISNWTMYVNKVNKVSVYSTIHLFIVCARRFDLTVSDFYPQLAALLTFLFII... | EC: 3.4.21.-
Subcellular Location: Membrane
Sequence Length: 367
Sequence Mass (Da): 41025
Location Topology: Multi-pass membrane protein
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A0A7X7PCS2 | LTLAAATAATITVGSASAAPTSETFLPAPTGPSPVGVTTLRLVDNDRQDPWTPGELREVPVTVHYPASAVEGYDTASYLPTEPGAAVGALPPELVDAAQTRTNGHYNAPVAAGAHPVVLFSPGYQVPRFLYTIQAESLASRGYVVISMDHPKDGLVSVFPDGRTVPGGVADSYTDAGLKKAIDTRIADAQLAIDAAETLSVGGNPDADSRVLPAGLNGNIDASRVGIYGHSIGGATATEVARIDPRVAVAVNVDGALFYGNDASPVVTDGASTPMLHLVTKIHADDESGKERFWNQYFDTPRGWSKVYALADTGHISFTD... | Catalytic Activity: (ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+)
EC: 3.1.1.101
Subcellular Location: Periplasm
Sequence Length: 389
Sequence Mass (Da): 40716
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A7RIB6 | MAAVSAKYTLETKRQAVEYFNSNNVPKHVEELLNKMFKEKPEDIFGYMSEHFGAIAKSPTITNVSAKEVLSSRGHPSVKLELNCFVNGVKKDREAWTKLNQRIGEKCFVIGNELYRRNPSILATGVTEKLSSVALLSADNANTVTELWEKIRAVSDQGGLVMLSKGQVEDVNTLAVDFVSTVVNIIPVANSWITRIPVVLATNFACPYLCHCILDKWYPCVTWRPYCVCCYASR | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
EC: 4.2.1.11
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Length: 234
Sequence Mass (Da): 26186
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A0A174M369 | MMDKLQKFCVISLTQGGRHADNTVDLQEFMIMPCGAPSFREGLSMCAEIYHTLKQLLKEQGYSTSVGDEGGFAPDLKDSDEALQLIVNAVQKAGYAPGNDVMIAIDAAASELYEESRNVYYFPGESRQCGKTVFRDTAEMVAYYEELIEKYPIVSIEDGLCEDDFEGWKQMTEALGNRVQLVGDDLFVTNVRRLSCGIALGTANAVLIKVNQIGTLSEALDAVEMAQRAGYRAVISHRSGETEDDFLADLAVATGAGQIKTGAPCRSERNAKYNELLRIEERLGEEAKYRNPFPQKGTGVREW | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
EC: 4.2.1.11
Subcellular Location: Cell surface
Sequence Length: 303
Sequence Mass (Da): 33455
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A0A498KI82 | MVMEVEEGGIAPYSPRTVEEVFTDFKGRRAGLIKALTTDVERFYQQCDPEKENLCLYGFPNEEWEVNLPAEEVPPELPEPALGINFARDGMQERDWLSLVAVHSDAWLLSVAFYFGARFGFDKTERKRLFTLMNDLPSIFEVVAGIEKRQSKEKSSVSNNSIHRPKSSSKGRGSESVKYAKAMPKNEDGVLDGEGDDDEHGETVCGACGESYAADEFWICCDICEKWFHGKCVKITPARAEHIKHYKCPSCSNKRIHHLLVLTAYTSNGEGEEEEDVSVIKYMTDAVLLGEIIDGEEADLQSHSVAMVDDAHERALSTDI... | 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: Membrane
Sequence Length: 851
Domain: The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence Mass (Da): 9434... |
A0A498HJY5 | MAFYSHSLFITLLTLVLPFPAATASRAQLTENYYDKTCPKFNEIVHRIVTEKQIATPTTAAAVLRLFFHDCVLEGCDASLLIASNSFNKAERDADINVAIPGDGFDVVTRIKTALELQCPGVVSCADILSAAARNLVNMVGGPHYTLRFGRKDGLISRADRVEGHYARTNMTISEIINLFSSINLSVQDLVALSGAHTIGFSHCNEFAKRLFNFSTTAETDPALNRNYAEGLRKLCANYTTNPGMSAFNDVMTPGKFDNLYFQNLQRGLGLLATDNALVTDPRTKPFVDLYAADQAKFFEDFGQAIQRVSLMKVKTGKHG... | 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/... |
A0A5B7RAS2 | MAWGVAVAATLVAAELLVVRLLERVAPDSAFGALFLFGVLVVSAGWRFRLALATSVVSAVAYAYVHVSESSASLVPAVVVFSLLALLTNVLVGQARLRAEESEQRRCEADLLAELARTVLRTEDPTDVLAIAGERLSAVLALPPPYAVLGLPGARVGPGQRLVELRDGEAVTGSLLVPAELGAADLRRVRRTVPALEALFAAALDREVLHRQAVSLAHQQAALRRTATLVALRGDLEDVHDAVVREIADGFGAEHVSLVRFHDEGSMTVLAARDDGARTPLAAGERVELGGHNVSSAVHATGRAASMDYTGASGPIAERL... | 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... |
A7SWC7 | MAASRSFRIWKPLARFSSSRAAFQNPLFCRAFQTSSVFLQLQGDDSQNIQVHFKSGFPVVTVPLPSRRELCQFTLRPLSESVKDFIENVKEEDGGIERVAVYDPSGSRISGSTKVDVLMKSNFKLVINDVEYDVKVPDTVAIAEDDQRSLAHVKTLIHQLYSSMNIEEHQLQKEEKLLSKLEEIKADLQPMEKLKSELNDKAAKRANFLVWGGLGFMAVQFGLLARLTWWEYSWDIMEPVTYFVGYGTAMACYAYFVITRQEYLYPDARDRQHLLAFHKLSKKKSFDVEKYNHLKDCMAKIEEDLKELRSPYKLHLPTRI... | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cel... |
C9V3L2 | MTRHGYHMVQLSPWPLVASVGAFAGVVGMVNWFHGKGVFVMTVGTVLLAWTMVGWWWDVVVEATFLGRHTSLVYRGLRVGVLCFIMSEVFFFFTFFWSYIYYSKVMGHMWPPEGIIPLYPYGVPLLNTVILVGSGFTVTWSQRCLSSGDREQALVGLFLTVGLGVFFTYVQACEFFATSFTIADTVYGSVFFIMTGFHGIHVIVGTVFLTVCWLRMWRNHFAPSHHFGFTSASWYWHFVDVVWIFLFILVYCMSWHRYVKMMSYY | 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... |
A0A498HV12 | MLSMANKGPDTNGSQFFITTTRTSYLDGKHVAFGKVIKGMCVVRSVEHLNTKDGDLLTEEVVISDCGQLPERADERVCNFFKDCDVYPDWSVDLDTKPDDISWWVTDVGAIKAIGNQQFKKQDYKMALRKYRKALRYVDICWELEEIDEEASSSLRKTKSHIFTNSSACRLKLGDLDGALLDTDFALHDWEDNVKALFRQGQTYMALNDIDATVESFKKALELEPNDGGIKKELLVAKKKDI | 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: 242
Sequence Mass (Da): 27432
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G0WDT0 | MASRVAQLDAVALDQELYTLLGSSILQSNLLNWNSIRNKNTEEIKLIIKSLIFICSTKYSVLEGVTRTYGSQLNGVSFKCRKSSLYLLTILSDYFNKKLSHYFFSSNPASTTLHNQDILRKLYSRLSKIYDIAYLLNLCVFISSSGRTNKNLYLTPIFRLFKIGSITDPIHLSSSSFYQDSIYGGLEYQNRQLLWNAILEVFNNTLLLSHKFYYSRSYIMNNKRKKKVQAKKQQQTGDSGLQCPKCENFPVNPYRMTCCQGIYCYVCVSYVLKRGYCLNCDETNDLSAQYIYHSSSTQPDNVREN | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 305
Sequence Mass (Da): 35140
Location Topology: Multi-pass membrane protein
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A0A6A3D309 | MFGMRTRIALAEKAVKYEYREEDLSNKSDLLLEMNPVYQKVPVLIHNGKGICESLIQLHYIDEVWNDRAPLLPANTYKRANVRFWADFVDKKIYDLGSKLWKTKGEELEAAKKEFLENMKLLEGELGDKLYFGGSTGKDFGYMICFVTFYSWFYTYEQFGNFSIEASAPS | 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: 170
Sequence Mass (Da): 19778
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A0A7R9NXT4 | MCMRTDLKWLVPRFDWFLCAEHSGTVDKVDLSSSLAEQLLRSDIVPKTAENYRALCTGEKGFGYKGSTFHRVIPNFMCQGGDFTNHNGTGGKSIYGNKFEDENFQLKHTGPGIIYIPAS | 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: 119
Sequence Mass (Da): 13312
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A0A6A3BFJ9 | MYDVEHGINCLELPLFQHTQGPDLDRLASVLSAETTFDWIVVTPPEAVSVFLEAWKAAGSPSVRIGVVGAGTASIFKNIRQSLDVAFAPSSGTDLSPHNSILCHLC | 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... |
A0A353HXL4 | LGCHYRVALPGAQVGLPEVKIGLVPGAGGTQRLPRVVGLELGLNMIVSGNPVLSEKLAETKLFDRVFDAGADLVAASVEFANSIADVRPLPKVRDLKIDYPNAEAFLQFSRNTVKAMAGPFPAPLECVECVAAAVTKKIEDGLAFERERFFALAQTSESQALRHAFFAERAASKVPDVPSDTPTRTIERAAVIGAGTMGGGIAMNFANAGIPVTILETKQEALDKGLATIRKNYENTVKKGKLAPEKAQQRIGLITGTLAYDDIGQADIVVEAVFEDMEVKGQVFRKLDEVMKPGAILASNTSTLDLNRIADFTSRPQDV... | Pathway: Lipid metabolism; fatty acid beta-oxidation.
EC: 1.1.1.35
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH
Sequence Length: 540
Sequence Mass (Da): 58713
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G8CAJ1 | YKVVVTAHAFVMIFFMVMPIMIGGFGNWLLPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYPPLAAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTMDQMPLFVWAV | 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... |
A0A1Y4M7W5 | MLCLKGTTVLRTILYALLAYLSGSVLYAQIFARLFHKPDLIERSNDHNPGTANAFQYGGFWCGVLTLVCDLLKGFIPVFAFLAGPKPDPIACALVLAAPVIGHAFPAFYRFQGGKGIAVTFGCLLGLLPIWQPVATLAMYFILFSVVLQISPHFYRTLVAYLCALVHMIFIVKIPAIWMGFLVISGVVLLRLHMSKEQREQIEVKWVWTR | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl pho... |
A0A0L8QIK2 | MCIRDRPVHRRPTVELLVLGDELLDSGPPHDGRVRDALGPLLPPWLRDRGARVTERRRVSDDFGLLRAALRDSAADVVVTTGSTAAGPVDFLHEALAEAGARLLVDSVAVRPGHPMLLAELP | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 122
Sequence Mass (Da):... |
A0A6A2Z490 | MAGWFGSQSATVATMFVTSTPSADLALTNLAYCSPSDLQSFAVLGSKLFLANIGDAFVLSVVTLSFENLTCRQFLVTNSFPSSTCRFIPLQDFNLALLRVELEFVKKGTKNEQVDAVLLANQLRKRLINQVMTVGQKVTFEYHGNNYIFTISQAQLEGQETSGAPERGMISGDTYFIFDAQNSSGIKVVNQREAAISNIFRHKEFNLQSLGIGGLSAEFADIFRRAFGSRVFPPHVTNKLGIKHVKGMLLYGPSGTGKTLMARQIGKMLNGKEPKMERN | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo p... |
A0A6A5FUF1 | MSCRTAPKNITCWILSAALVFIYFIVIGYVRYFDGYWLYPILTLFAIEHFVISYILAFFGFFLLTKSACLLNNFFHNSSTTPTVVRTKKTKKQH | Catalytic Activity: 12-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 12-hydroxyoctadecanoate + H(+)
Subcellular Location: Membrane
Sequence Length: 94
Sequence Mass (Da): 10973
Location Topology: Multi-pass membrane protein
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A0A2N6U542 | MSSLEVTFVTADRTVWTGRARQVVVPAVDGSMGILPQMQPTLAILGDGLVRIICEEEGVRELSVRGGFVSVDSDVVVIGVDDADHDDEVAKESLTGSAI | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 99
Sequence Mass (Da): 10456
Location Topology: Peripheral membrane protein
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A0A7V0NDD7 | MGEEMVDEATLKALEEKVAELKRLVEQDGLALEEELVLLERRLAELRREYFAKLSDWDRVKLARDPRRPTGIELVEMVFDDFYELRGDRLLRDDPALRGGMAKLSGKPLVVLFH | 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: 114
Sequence Mass (Da): 13239
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A0A6A2WC41 | MIACGLATHYCLNARLAWIEEHLGSLLNDEPSTIKSSLAQYGDIVYTDRSSILHRIETIDKCFCHDTVEEIIDSLETEAAGT | Pathway: Amino-acid degradation; L-valine degradation.
Function: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism.
EC: 3.1.2.4
Catalytic Activity: 3-hydroxy-2-methylpropanoyl-CoA + H... |
A0A6A3B8N6 | MNSLEPRSIFLISAIFRVGLILYGEWQDAHMEVRYTDVDYIVFSDAASLMASGHSPYKRTTYRYSPLLAFLLIPNSFISRSWGKFLFSASDLFVGLFIRIILKQRKVPDHLCTYSMLIWLFNPFTFTIGTRGNCEPIVCAMILWIIICLINADSRSDKKQKMITENAKNETERLTTKLKG | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 180
Sequence Mass (Da): 20749
Location Topology: Multi-pass membrane protein
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A0A1F9E5S0 | MDAFFISVEQRDNPALRGKPAAVCGSLSRSVVTSATYEARPFGIHAGMPVQEAKRKCPGLILVKGDHSKYTSTSARIFSILKDYTPLVEVASIDEAYLDIFQSLLLFNSSLHLAKSIKEKIREKEQLTCSIGVAPNKLLAKLGSRLKKPDGLTIIRKDEVEGILRELPVSKLHGIGPKLTEGLQEMGILTCGQLGKTPVSILTKRFGAIGERLHEMGLGVDESRVIPFDEEEDAKSISHSVTLEEDTSDKDLLRKVLLQLSEKVSRRMRQEGFYGSRVVLTVRYSDFYTFSKQKTLTRWINSGNEIFRHSLEIFESIPHP... | 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'... |
A0A6A2ZLM4 | MSESEGLSNPSPLDLKSDNDSNDRLSPPAPPNSESDLDSNLYSTFSTDDSSNKSSPPTESPPSSSSSPSPTSSPPSPPPPSPKKQSPPPPSPPPPEVQSPSPPLSESSPPPPKQRPPPPEKYPPQATSTLQSSSNASRASSSNNQTQDVTNETHSRYDVIISAAVAGAFFIGIFVALFFILKRRRKKKKQTLHGNYMPPSGKIEVKSDAHGKESPMGYASGGQTGQFCISQKSGFITGSKTFFTYEELMEMTDGFARDNVIGEGGFGYVYKGRLSNGSPVAVKQLKVGSGQGDREFRAEVEIISRIHHRHLVSLVGYCIS... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 636
Sequence Mass (Da): 69791
Location Topology: Single-pass membrane protein
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A0A260ZQR0 | MFSIFMRIPDTAQVDAVFSEAYASIEQGLCYDEVGDWENTLAMYEKGMNLIKEGEKMKHAKKSEMWKMLQEAKTSVEHRIKVLKKEGPKAPSSEKVKEAEQSVEDEKEAIRMQLDSFGSQEADLIYFLPEGVQLFTIDGEKTTAPTAPTSLQILRFPQPLDDGSTSDTLAFMQVGPWAYPLMGSKTPVLRNEFGAYIVANPTPENPNMTVAILLSSDIEPRLVEELHIVLRQFTDFKEQTEPSTELSKDEKKKISTQIANFLIRGGQKIAWGVETTTVRVISRVEENGETYRTTLVATDKPMQVSPVVRGMDKIGDMGVS... | Function: Required for peroxisome inheritance.
Subcellular Location: Membrane
Sequence Length: 639
Sequence Mass (Da): 71600
Location Topology: Peripheral membrane protein
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A0A2R8BTL4 | MPDFSLTLLRHRLSARTQSRRPSMARRARPEGRLMWLHLGENFDPTGVCIAVERLRERHRDLRVLITGDQADGGLIDAPPSDTVPSVRAFLDHWRPDIALFAGNDVFPMLWSEALARGIPLIAVEVDTTRHAAAMIRQMRGFDAILALEPDLRLDPVIEVTGPLSTTPLLPHADRAEIERMHEAFGNRPVWLALGAMADETEAILQAHALASRMTHRLLLVLDVDDATATSRLRDGGWRWVDRDADGVPIDAQVLLTEFGTEDGLWLRLAPVTFMGGTLSGDGPSLDPLAMASLGTALLAGPQGADVASMSRLTAVGAVR... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A8B3RZK6 | MKRSRLIDVRNLSFEYERGSIRGTTGALSDINLQVNSGEFVVITGPSGCGKSTLCKCLNGLIPHAIGGMMDGEVTVCGMNTTEHEVFEFAPHLCMVFQDPDNQLFSNDVESEIAFGPENLGIGRHEVAERISLAISSIGIEHLRDRLISELSGGEKQRVAIASAIAMKPDILVFDEPTSELDPTGAFLLMDALKRLNKEFGITVILVEHRIERLLGVMKRLIVLKKGKITCDGTPEEVFQTGLENMGVFIPPLVQFSKKFGFPLHQYRSVDDLNPCCGWRSTFNGHGGNGGSGGSRSREPAVSLKNIFYRYPGTKNQSAL... | Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system.
Subcellular Location: Cell membrane
Sequence Length: 568
Sequence Mass (Da): 61463
Location Topology: Peripheral membrane protein
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A0A7S0MVL8 | NLPGVKVDLPTLTEKDVSDLVDFGVKHDVDFVAASFVRKASDVDTIRQVLDKAGGQSIRIISKVENHEGLVNFDDILERSDGIMVARGDLGMEIPLTKIFWVQKMMIRKCNMAAKPVVTATQMLDSMIAAPRPTRAEATDVANAVL | 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: 146
Sequence Mass (Da): 15965
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A0A1C4D6P7 | MLSLLNQYSQSRFAWFLLFFSTLSFEITALYFQHGLGLAPCTLCIYQRCAIFGIMLASIIGLIAPKNILARLAAVLIWLFSAYKGFALATFHAHLQFEPNLSDTCSLSPQFPAWLPLDSWLPSLFNAYGSCADKIWTFLTIEMSQWMIIIFACYLIVGLAILVSQLFSAPKSSMWSK | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Subcellular Location: Cell inner membrane
Sequence Length: 177
Sequence Mass (Da): 19944
Location Topology: Multi-pass membrane protein
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A0A1S9C896 | MYNEIEITHDYVTQYIRALTLPKSGVMLEIEKEIRLGNAYYPIIKPEVVELITVLLAMNNPKKILEIGTNVGYSAIHMAKVSGARIETIEREDHLVELATANIKKECLEDRIRILNGDALEILGKLEEQKYDVVFMDCAKGQYINLLKDCKRVLRSGGILITDNVLHEGIVAKSRYNIGRKNRTIQRRLKEFLWAITHDSQLKTSIIPIGDGLSVSYKK | Function: Catalyzes the methylation of 5-hydroxyuridine (ho5U) to form 5-methoxyuridine (mo5U) at position 34 in tRNAs.
EC: 2.1.1.-
Catalytic Activity: 5-hydroxyuridine(34) in tRNA + S-adenosyl-L-methionine = 5-methoxyuridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 219
Sequence Mass (Da): 24939
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A0A8B7NUM1 | MSVRFTKTMLLYILLIVQVIQITYYLHSNLLYSTNIQCTPEHPTAVHNISDETEAPFMLGNSSLWSGLRSHIKKKYSGLQLPWSSPTVFVVTPTYRRPTQMADLTRLSQTLMNLDFIFWLVVEDGETTQLPVAQLLQRSGLPHRYMAAATPARYRNDPDVGRGVFNRRAALDWLRAHEKRGVLYFADDDNSYDIRLFQQIRSTQKVSVFPVGMILEYGISSPIVRQHKVVGFHDAFQALRKFAVDMAGFAVNLEFLYRKPNATIPLLVSYLEDGFLRALGTSLDDLEPLAHDCTEVLVWHTRTQTPFSPNVAHLPPHSND... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP
EC: 2.4.1.135
Subcellular ... |
A0A3M7SEN5 | MSKLSFTSKIPEDLDETKIDKWDWNALKNALDDAGRKFLTNQKDCQETHSLMNGRLIISTIAVLFSLYAIGYDYLYPFPESKLVIIVCVASYFVTVGILTLYTSFIEKGCFAQVVQKLDNKTFYWKFLSKQKPHKENFYVLTIELQHGNKVIKKTVEKSVAKYFDENGVLVVKNYYSDLEKFCSQTFNDKRE | Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the tr... |
A0A498HG71 | MLPYLITPYGLIICLFFFSGAHTIGISHCSSFSNRLYNFTGVGDQDPDLKTEYAAKLKAKCKTPTDNTTFVEMDPGSFRTFDLSYYTHLLKRRGLFQSDAALKTSPKAYNYINQLLKGPLQNFFYEFGKSMEKMGRANVKTGSAGEIRKQCSVVNS | Cofactor: Binds 2 calcium ions per subunit.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Length: 156
Sequence Mass (Da): 17544
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A0A498KN47 | MERHLSAAEKLPVLPVSVRHLSAAQKVQPAAINGLRGNSFTGTKLVVKPTARASEPKTSVNASCLLFLSGAVVAKYGDKSVYFDLEDLGNTTRKWDLYGSDVMMIQMLMNILVIFLVV | Function: Possible role could be the docking of the LHC I antenna complex to the core complex.
Subcellular Location: Plastid
Sequence Length: 118
Sequence Mass (Da): 12851
Location Topology: Single-pass membrane protein
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A0A6A2XKP3 | MAFPKVFLLGFHAMVCAVDGYGGGWTNAHATFYGGSDASGTMGGACGYGNLYSQGYGTNTAALSTALFNNGLSCGSCYEIKCVNDAKWCLPGSILVTATNFCPPNSALPNNAGGWCNLPCITLTFLSLFSNTLNNTGLELCLLLTEGLHVEEREESGSQSMATPTSTYSSSPTLAVPVMYTPWPSRALGPVGSPCLGTGARTGKATATSTVKASHLRSPPVMAVPWCPTTLPQPVGPLGRPSLVPNSARGGRLIKIQYIFKAVFNGKTFEIMFWKKLIHGIKYSQD | 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: 286
Sequence Mass (Da): 30156
Location Topology: Peripheral membrane protein
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A0A8B7P2E6 | MTLQFPVTNMTNPAIKTCEVDTKLAGVGFKFFKLAVVTLMTLLLMWSYTTQHLETDDRRHRQYKPIAINMPNDKARTMSDKVNISDHTEEYHSSNCPGSLNYTENLVVNDTAAQIVALVLRLTSIKRADVIALLDSTLRNAAPQLAFLLDVLQDFDTQHACEACHDTRPPPRPVLDARIRLDHNVSWMGLSLPALAMNPLGRLGNQMGEYATLFAFKKIYNTTVVLIPTESALDASFAGLSIPHLKKFNHSAWRPVYRDDAGLYTYHATHLAAAGLLGPHLFLLMDYPFEAAVFGAYKTELIKEFSFNETVMRQAEARLE... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 479
Sequence Mass (Da): 53505
Location Topology: Single-pass type II membrane protein
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A0A7H5P4M7 | MCVEKDLFFMKQALDEARKAYERDEVPVGCVIVHEDVIIARGHNSVEQLQDPTAHAEMICISAAAEYLQNWRLKDTSLYCTLEPCLMCAGAIQLARITRIVWGAPDLRLGAGGSWVNVFLEKHPFHQVECCAGVCHQESEWLMKNFFLEKRKAKNEK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).
EC: 3.5.4.33
Catalytic Activity: adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+)
Sequence Length: 157
Sequence Mass (Da): 17882
|
A0A1W1VJ97 | MNTKILTRIGLLAAFGLVLQIFSFPLPFFPEFLRYDAAELPALIAAFALGPWYGVLVDFLKNILSLFVGMAPAGIIGITANFIAGATFSLVAGTIYFTKKTKARAFIGIVLGVVLTTIVMVVANYFWLLPLWGIPKSGVLELLAISIIPFNIIKGLMTGTLTFVLYKKVKSIFEPVFKSKKKQVLNKLG | Function: Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex.
Subcellular Location: Cell membrane
Sequence Length: 189
Sequence Mass (Da): 20649
Location Topology: Multi-pass membrane protein
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A0A7J3XHJ8 | MRELQVVVVVADGLGDRPVPELGMRTPLELADFSPVADVLAGSSVGLWDPIEPGVRPGSDTAHLALFGVNPVGNYPGRGPFEALGAGASLRPGDVAFRGNFATVGEGMVVVDRRAGRFIPEAKRLAEYLNERLGTIDGVEVRLYHATEHRVAVVFRGDNLSDAVSDTDPHVEGVRVSRCVPRSGDPAAARMAEVVNRFTEIVHKLLEECPVNAGRRSRGLPPVNAVLLRGAGRMVRYPPVTERQVISLARAAAISATALVKGVCSLLGFEVYTPPGATGDVRSDLLSKAREAVDLYRRGYDFVYVHIKGTDSA | Pathway: Carbohydrate degradation.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 313
Sequence Mass (Da): 33483
|
A0A059GCA7 | MPKVNRNQSVPSRSRRRPATIVDESTGEEIRVSSILFGLVMLIAIIVATAAWMGGSLSQIETRFGGFMDDTARMAGVSVNDVSVLGLEQNPALADDVRAAAMIEPGENMFRADPKLIRHRVEGTRKVLNVRVHRLWPGQIVIIADAAEPVALWHDGKEWTVVDGLGRILPDANADDHKTLVRLAGRGAPLAAPALVKALKEAPDVAARLAIATRVADRRWDVRLVNGATVRLPEDTGMESALARLTKLQTRTALLQRPVTMIDLRNKGRVYLSPALEGGAIKVAEAARS | Function: Essential cell division protein.
Subcellular Location: Cell inner membrane
Sequence Length: 289
Sequence Mass (Da): 31315
Location Topology: Single-pass type II membrane protein
|
A0A3M7T4S2 | MALLIRNVSKLSPLGSIRSYSEVVNVFGRRNVDTKGAEERKPIATIPENAESVKEISCHPEEHVSGRMATIYVPPKNAMQSGTFGTRRWRVEFDNRERWENPLVGWGSSGDPLSSLQPEFATKEDAMVYCQRMGIRYQVEEERELKRRIKSYGANYSWNKRTRVSTK | 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.
... |
A7RX59 | MVPWTYGERNPKFREKLNGRPSVLLLNKMDLVEPGKRQEVLKKFESQGIRTVFTDCKAQHHYSAKRIVPAVLDAVKDAEYEGSYIRKDPDKPYHLLVCGLPNTGKSSLINALRRTHLRKGKGTRVGKLPGMTTAIQEKNMINDEPKMYIFDTPGIMAPHIPTAEIGMKLASIGCFKDHMIGEDLIADFILYTLNKRKKLEYVQKLGLENPSDSIDFVLRHMATAQQYLIKGDRPDYLRASIQLISSYRKGEYGCFMLDG | Function: Plays a role in the regulation of the mitochondrial ribosome assembly and of translational activity. Displays mitochondrial GTPase activity.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 259
Sequence Mass (Da): 29448
Location Topology: Peripheral membrane protein
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A7SA08 | MADSLFFTGLATLLAISVGILLLIDFKQSQPYLDEIFHIPQAQQYCEYKFSEWDPKITTLPGLYLVSLAILRVAAFFSSTELIDVCSVLWLRFTNVFFVIGNAWLLREVLIQLNLQNSRKSFPMFIFSSAKPL | Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodoli... |
A0A7C1BU48 | MNNKVVIVRGSVISGIGVGHKYVSIPYYKNLLSSLLDGEEPYPGTLNIRVNLTYKELSNLCKPNEVPSKVIEGKRYGGFIYWKGKIKTVPSIGSSKQVIVPKVLILRPHLSRHEDNVLEIVSHVHLRSKLSLRDGDTLEIVIMCK | Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1.
EC: 2.7.1.161
Catalytic Activity: CTP + riboflavin = CDP + FMN + H(+)
Sequence Length: 145
Sequence Mass (Da): 16235
|
A0A7J2UZQ4 | MACLVKLAIPKGSLEKTVYDFLERAGYTLIGKERSYRPIIASDPDICVKILRPQEIPIYVYEGLYDIGITGIDWVLEQGVEDKVRP | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
EC: 2.4.2.17
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
Sequence Length: 86
Sequence Mass (Da): 9743
|
K9SIE1 | MLKSSLKNIVFKLVALVLVATIALTCTSSAYAARNTYTLGSGNPLTTKELREKVNAGLTGNYVDDTKKLIESLKYTLSLAKDADDRSEAQAETRARINAYSARYRADNSKTGLVSFTTMRTVINSLASYYNGTTKRSVPQRVADRAISQISRAESALEAGR | Function: Plays a role in the repair and/or biogenesis of the calcium-manganese-oxide cluster on the lumenal face of the thylakoid membrane. Its presence in a photosystem II (PSII) preparation prevents binding of some small extrinsic subunits and thus assembly of calcium-manganese-oxide cluster.
Subcellular Location: C... |
A0A7R9IJ80 | MNDPIKNTSYEITQPPSTRESFTPVSAWPVRLVGDRRPEWADRFPKGARGRYTKIQTPDVLSSIMSLTFRQRDYRRSSQVLILVDLRLDLNWKYILGNGGGCYLSTVAITKIPQQRNAAMAEAHSAVAFQFSITHEGWDVNFDREVLHLVWQSGIRSWKKRLARFKNSIKNGVYPASLQSLWAMVAIIAALHFTGVGVAHKYVNTITNYLPAPTLQWQVVSCTVLGIALWLTVIYFIRYTLKLLFIYKGWMYEERGKGRVISNRTKLWVVMVKALSGASSPLLYSFQGSLPRLPLPSVQETMKRYLRSVRPLLDNEKYTR... | Pathway: Lipid metabolism; fatty acid beta-oxidation.
EC: 2.3.1.21
Subcellular Location: Membrane
Sequence Length: 940
Sequence Mass (Da): 107796
Location Topology: Multi-pass membrane protein
|
A0A4R2PQG4 | MTGLVQQEEAAPGIRRVVLGNGAANLLTSDMLAALDGALAAALAAPGVRAVLIASAGRVFSMGLGPEGAAGAGALAAICARLDRAGVPVVALVGGMAMGGGCELALAAHYRVALPMAQFGLPEIAIGLPPGAGSTQRLPRMVAPAVALELMLSGQPFSAAKAQRVGLVDALVDGNLEAAGLRFAQGLIAERAGPRPAPGRVLPPFGRLHAAVAERRAGLPVDGPLAAPGRVLDCVDAAAMLPYEAALDYEAAAYEDCRDSPVHRALSHLALGEAGLRRRVERWQGEARAVTSVGIWGWGTGAAALAAALLSGGVAVRMAA... | Pathway: Lipid metabolism; fatty acid beta-oxidation.
EC: 1.1.1.35
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH
Sequence Length: 704
Sequence Mass (Da): 71452
|
A0A3M7RAI3 | MLIQKFNSNFYVNTESIEYRSEPFMLFLLIKKCLLLCNESSNLCNISFSYPFHLRYHAPSDNYLYQRFKIISPRFLVSDCSQDLKDQNEFIFKSDQIIDKGLIKKFYIGNCYWNEIDFNFSKDKFEFVVPVGQAKLAHITNIKLMIDIFKIFLIEFKDLTYEDNLR | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Essential component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum mem... |
A0A7C2MRM2 | MGFLSDMRDRWRRIEVFTIDSSREGTACSGESLLESILRWRRGAGAAIIAEYKRASPSGIIDMELDIRDYYYQLADLVAGFSVVVEREWFMGSERYIEILRMLGWRGPIIAKGFVFYREQVYRYREAGASAILLIADILDRDELLDLYKYSEEKDLDPLVEIGGNIDPGRIIGIVSPKIIGVNSRNLETLEIQPERMLKTIRSIKREYPDIVVVAESGMRSLDDIARAIEAGADACLIGTELMRNPRRASMLSELYRVLGVEKRYNLESLAPLGGEEVRSP | 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: 281
Sequence Mass (Da): 31923
|
D7CR66 | MVQRAFPAAPPYLALVFGVPILVGVLAWIAHHFHWIMPWYYLLPSLLFLLTFTVMPIGLTIFLAFTDYAGNRNTQLNPTTETTIVQAAGTQVETADLTSLRCEVLFEGCLGVRVRLYTAGTLEVQGVNLENNVLTVSPAPPEGRTVSAAELELTEFGIRAQFPVVAIDGDHLTLGRTPPGEVNLERVALEVAGEVLERRIVAIQGTTLTLDAPLPEGFTYTSLARYNDFRVVGWANFRTILGQANRALLPVFAWNLTFATLTVLINIAVGVFLAVMLNDPELRFRNLYRTLLIVPWALPAIITIQIWRGLLNYNFGAINR... | Function: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 489
Sequence Mass (Da): 53385
Location Topology: Multi-pass membrane protein
|
A0A0E9NS61 | MDNGTKGMSRAGRGGSRGFSRGGARGGARKVSQAGVAPPEKRPRMDIATPESMSQFSTAPTTPAEPSSATPLFQDLADQGVLKPNLLQAIHNNLKYKTMTEVQAATMGSILEGKDCLAQAKTGTGKTLAFLIPAIQTLMGRPPTKKSIRAIIVSPTRELAKQITDEARLLMTGFNFRSHTSIGGLSTSKDQKAVLTCPDLLIATPGRLHDHLSNPSLKACFTEVQFFVLDEADQLLDQGFSVALNKIMALLPPTPKRQTLLFSATVPNTIKQLAGKLLRPGYALINTINETDVGTHERIPQFLIHVPSVNTVLPSLLALI... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 553
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): 59915
|
U1P2L0 | MDIRVGVDEAGKGPVFGPMVVAAVRAPVEAIPEGVADSKALAAGRRTELADXXXXXXXXPHQMRPDQ | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 67
Sequence Mass (Da): 7042
|
A0A3M7R631 | MMSKAIISRRHMYNLFEDALQSQNVTNFEIRCQNSSAKNLTKADFIQLLLEDKQLTKKLSLIKHGTFKFCNLTFLRKQFRTKSVYFLNKFKFLTSSFKSSINNFKEVQPGGYFNQSLFCIHEYLYFIYLKTGLLPNNETEVPLYNSKLIEKFKKDQNLMTFIIIPYLNRESNLKDFLFNMHKFFQNQHLNSYQIVVAEQNVDDPEKRLMFNKGRLYNAAYKYILSKYSKSRIKCLIFHDVDLLPESEFNFYECDHWGDAPRHLSFFIRSENSENQKGREEYEKNPYEMLVGGVLLIKPHVFELINGFSNRYWNWGGEDDA... | Pathway: Protein modification; protein glycosylation.
Function: Catalyses the transfer of galactose onto proteins or lipids.
EC: 2.4.1.-
Subcellular Location: Membrane
Sequence Length: 403
Sequence Mass (Da): 47638
Location Topology: Single-pass type II membrane protein
|
A0A433ZWU3 | YPPTLLLIGILIVTRIHQLGLKGLLNSTNVVWEGTLGFLGHITLSDALVVRLSNVFGTPAAADYKTLYVPALIPFFLVVLIGIFLFRLKRTQVKTMFVQTAQQTNKPFIALFGALIMVNLMMQGGENAPVYIIGRSLAGATGESWIYFASYLGALGSFFSGSNTVSNLTFGGIQQSIAQTTGLNVNLTLALQSVGGAMGNMVCLNNIIAVCTILGITNAEGSIIKKTVIPMFIYGVIAAVMALILTL | Function: Uptake of L-lactate across the membrane. Can also transport D-lactate and glycolate.
Catalytic Activity: (R)-lactate(in) + H(+)(in) = (R)-lactate(out) + H(+)(out)
Subcellular Location: Cell inner membrane
Sequence Length: 247
Sequence Mass (Da): 26306
Location Topology: Multi-pass membrane protein
|
A7RKK4 | MLAKNAMILVLVILLGTSITETKRKKTSSNHARGTKNRGAQPFAIKSRLQTFQPIIGILAQEATGRITREISGQYIKASYAKMIETAGARVVPVLYPSIYDNMGRINQSPQQIQNIFNSINGLLLPGGHVKLQKSGYGRVGKMLYEMAVQSNRQGQPFPIWAECLGLELIALLASGRGLARGQYDTELLDRTDSKIYSKPLNISKDYKQSQLLGSADSTMIQYMMRDLKAYNNHDKSLTPEKYNKYPSLKSAFRIVSTNKDRKGKEYISTMEGRKFPFFLFHWHPNKARFEQLENHPVHHPSHESFLIAQYLTKLFVDIA... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
EC: 3.4.19.9
Subcellular Location: Secreted
Sequence Length: 357
Sequence Mass (Da): 40690
|
A0A0D3HRW4 | MQQQLPVTETAVAAASNFRHRLRKKRSSNVICNSALILFPSQEGRLGLLVTAPGLGQYISGAILFEETLYQYAVDGRRIVDVLAEQGIVPGIKVDKGPRPAGRSDPESWCQGLDGLALREAAYYPQGARFAKWRTVVSIPNGPSALAEDRLVPIVEPEILVSNLLH | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Length: 166
Sequence Mass (Da): 18089
|
A0A6I1EB64 | MIPECFSGCFLHVMTYFDIEGACAVARYYAPSSAAAPEPALRGQAEWLASRESSRNQKIRLMPDAHPGKIGPIGLAMTVGDSLLPGLVGIDMGCGVTLAKLRMKRRPDFGALSAFAREQIPSGFAVREKPLPEALRFNFERFRVLRHINLEGAQKSLGTLGGGNHFLEIDRDQEGAFWLVVHSGSRRLGVEVAGRYMQLASAQAAGTPDGKVPFEEAPLSGGLLTDYLLDLEGASSYAEASRRAMLRLICDGMRWKMESLLSIVHNYVDCSGTVPILRKGAISAKAGEPVAIPINMRDGILLGVGLGNAEWNESAPHGAG... | 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: 394
Sequence Mass (Da): 42448
|
Q8LZR4 | ATIHGTQLNYSPSMIWSLGFIFLFTMGGLTGVILANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGISMNQKFLKIQFLIMFIGVNMTFFPQHFLGLGGMPRRYSDYPDAYMTWNIISSIGSLISLISISLFLFIIWESMISMRKTIIALNLPTSIEWYQKFPPAEHSYMELPMLVK | 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... |
A0A834JWK8 | MVVNYQAFGKRIIESNMGGHGHGHDTIKIPSSDCYKIENSPALVKFQERLASEGLEDPWLRNEAWRYHPNYKTRTQRVLTFCLRGWKIGIPAFLITVGIEQLLSLNKKDDHDHGDHH | 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.
... |
A0A6A5GEM3 | MHAIGIRKTITATSCVFYDAVVDAIGEPVDFSYVPGQMSASGDEMSMTEKVENYRMSTALQKLNIFIWDRETRIYNKYLGPQIPDWRDLMADASLHFVNSVPYVDYPRLVTQKTVPIGGISVDIPSIKSSVLPKDWSDVLDKRSYNIC | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 148
Sequence Mass (Da): 16716
Location Topology: Single-pass membrane protein
|
A0A8J2QU61 | MNKLQKHQESNGLPSPYQYKFAKYQGIMKYILIWTMFNDTENKIGEGQKPFIDRDCRYVNCYLTTKKDFLNDDITNFNAIVFDINKIKMWKKTFFPKQRSDEQKYIFYSDVSSDEVPICNINMDNYFNWTWTYKINSDIVSPFIEVKDLKGNVVAPRSVVNWNSNMTILNEEEKKHLKQKKKAMAWVVTKCHTRNNRLLLARRLRRGFEQNGLIFDIYGCGHKNCPKGGCMEAIEREYYFYFVPEDSFDEDYVTDEVLTAYHHHAVPVVLGGANYRR | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 277
Sequence Mass (Da): 32844
Location Topology: Single-pass type II membrane protein
|
A9YNS1 | ILILSGFGMISHIISQESSKKESFGVLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISFNPSSLWSLGFIFLFTMGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAILAGIVQWFPLFTGLTLNNKYLKTQFLVMFIGVNLTFFPQHFS | 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... |
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