ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q5U5Q3 | MPSGSSAALALAAAPAPLPQPPPPPPPPPPPLPPPSGGPELEGDGLLLRERLAALGLDDPSPAEPGAPALRAPAAAAQGQARRAAELSPEERAPPGRPGAPEAAELELEEDEEEGEEAELDGDLLEEEELEEAEEEDRSSLLLLSPPAATASQTQQIPGGSLGSVLLPAARFDAREAAAAAAAAGVLYGGDDAQGMMAAMLSHAYGPGGCGAAAAALNGEQAALLRRKSVNTTECVPVPSSEHVAEIVGRQGCKIKALRAKTNTYIKTPVRGEEPIFVVTGRKEDVAMAKREILSAAEHFSMIRASRNKNGPALGGLSCS... | Function: E3 ubiquitin ligase responsible for the post-transcriptional regulation of common HLA-A allotypes. Binds to the 3' UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation.
Catalytic A... |
Q86XN8 | MPSSLGQPDGGGGGGGGGGGVGAAGEDPGPGPAPPPEGAQEAAPAPRPPPEPDDAAAALRLALDQLSALGLGGAGDTDEEGAAGDGAAAAGGADGGAAPEPVPPDGPEAGAPPTLAPAVAPGSLPLLDPNASPPPPPPPRPSPPDVFAGFAPHPAALGPPTLLADQMSVIGSRKKSVNMTECVPVPSSEHVAEIVGRQGCKIKALRAKTNTYIKTPVRGEEPVFIVTGRKEDVEMAKREILSAAEHFSIIRATRSKAGGLPGAAQGPPNLPGQTTIQVRVPYRVVGLVVGPKGATIKRIQQRTHTYIVTPGRDKEPVFAV... | Function: RNA binding protein, may be involved in post-transcriptional regulatory mechanisms.
PTM: Phosphorylated.
Sequence Mass (Da): 64883
Sequence Length: 651
Domain: Binds RNA through its KH domains.
Subcellular Location: Cytoplasm
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Q3UE17 | MPGSTGQPDAGGAGTGTTAGDPGHPHPALAGAEDAAPRPPPEPDDAAAALRLALDQLSALGLGGARPGDEGMATRSADGATECGEDEPAPPDELEVAVAPPVTASVAPGGLPLLDPDVSPRPSPPDVFASFAPHPAALGPSTLLAEQLNVIGSRKKSVNMTECVPVPSSEHVAEIVGRQGCKIKALRAKTNTYIKTPVRGEEPVFIVTGRKEDVEMAKREILSAEHFSLIRATRSKAGGLSGATPGPPNLPGQTTIQVRVPYRVVGLVVGPKGATIKRIQQRTHTYIVTPGRDKEPVFAVTGMPENVDRAREEIEAHITL... | Function: RNA binding protein, may be involved in post-transcriptional regulatory mechanisms.
Sequence Mass (Da): 65329
Sequence Length: 643
Domain: Binds RNA through its KH domains.
Subcellular Location: Cytoplasm
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Q9XUB2 | MKAASNSVSSAGGSVSPTTTQPPLPPGQSSHPQIYDQQMQYYFAAAMPNQPMATYAAQNGSSQQYAPAAPYYQDANGQYVQVPANGSMAPQQHMMVSGQPYLYMAQPQQGAQQVMQSGQPQLIYYQQSMAPQAAPMYFHPMQAAPMLPEQMGVMPHTQPAIPPQQQPRQVGVEISSTRTAPLTSSTPLPTSLEYETVQRDNRNRNIQFRYHRVMEHDELPIDEISKITLDNHNDDTMSAEKENHFHEHRGEKFGRRGFPIPETDSQQPPNYKTRLCMMHASGIKPCDMGARCKFAHGLKELRATDAPARYPNNKYKTKLC... | Function: Functions with mex-6 to affect embryonic viability, establish soma germline asymmetry in embryos and establish plk-1, pie-1, mex-1, and pos-1 asymmetry in embryos . Also affects formation of intestinal cells . Binds to mRNA in vitro, and inhibits pgl-3-mediated P-granule formation, probably by competing with ... |
P84149 | MSYRGRGGGYNNNRGQFSSGPHQHQQNVDSFVAANQYPIEIMGWNGASSGECINFISRKCKVIVSNYSVDSNSGVLKGYVKNESQANTLLNWSGVKFAGQSLRFSKGVSNISNQMGGGASTGSQSTIETISQFLKARYQPEIKMLNLSNVKQDPTLTAQGFFGSLSVSSKFFPALMKVASDLKLDVDSIDLSNNELQDLQTLTSMAQTFPKLQNLSLQNNNFTKIKVFETWRHKLNFLRELILFNNPIVQTNDPAEIQTIKLELMKSFPRLVVLSGEILRNEQVLIANLSFPFESPETMFFQDEDSRNLATNFIANYLKL... | Function: Involved in the export of mRNA from the nucleus to the cytoplasm.
Sequence Mass (Da): 68257
Sequence Length: 617
Domain: The NTF2 domain heterodimerizes with MTR2. The formation of this heterodimer is essential for mRNA export and binds to all of the nucleoporin-FG-repeats.
Subcellular Location: Nucleus
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Q9Y8G3 | MLRRKRERRNAVKENEMVIDTPLEKRRTPGKPRATREPPISVVITGHSKGSEDDLISFVWRKVKVRLMNISYSPASVTAVVKSQDFSRLNGLNGAAFAGDHLAIRRVDGASNVTQDYRKAKTKRSFRSVSAPSLSALATQAQRNVSKTLPQSTNETIEKLRQFLQTRYQPATKFLDLGNLQQDPLLKQMGILAEASTKSKMFPALMKVASLNFPDVISVSLSDNNLQSVTAVTTLAQTWPKLLNLSLANNRITSLSDLDPWSPKTKLPELQELVLVGNPIVTTFANRAMDYQREMVSRFPKLRLLDGNSINSEIIASQST... | Function: Involved in the export of mRNA from the nucleus to the cytoplasm.
Sequence Mass (Da): 66535
Sequence Length: 596
Domain: The leucine-rich repeats and the NTF2-domain are essential for the export of mRNA from the nucleus.
Subcellular Location: Nucleus
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Q99257 | MSGFHNVGNINMMAQQQMQQNRIKISVRNWQNATMNDLINFISRNARVAVYDAHVEGPLVIGYVNSKAEAESLMKWNGVRFAGSNLKFELLDNNGASAGTSDTISFLRGVLLKRYDPQTKLLNLGALHSDPELIQKGVFSSISTQSKMFPAMMKLASTEKSLIVESVNLADNQLKDISAISTLAQTFPNLKNLCLANNQIFRFRSLEVWKNKFKDLRELLMTNNPITTDKLYRTEMLRLFPKLVVLDNVIVRDEQKLQTVYSLPMKIQQFFFENDALGQSSTDFATNFLNLWDNNREQLLNLYSPQSQFSVSVDSTIPPS... | Function: Involved in the export of mRNA from the nucleus to the cytoplasm.
Sequence Mass (Da): 67352
Sequence Length: 599
Domain: The leucine-rich repeats and the NTF2-domain are essential for the export of mRNA from the nucleus.
Subcellular Location: Nucleus
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P52477 | MQRTPAMRVLVPALLVAISALSGCGKSEAPPPAQTPEVGIVTLEAQTVTLNTELPGRTNAFRIAEVRPQVNGIILKRLFKEGSDVKAGQQLYQIDPATYEADYQSAQANLASTQEQAQRYKLLVADQAVSKQQYADANAAYLQSKAAVEQARINLRYTKVLSPISGRIGRSAVTEGALVTNGQANAMATVQQLDPIYVDVTQPSTALLRLRRELASGQLERAGDNAAKVSLKLEDGSQYPLEGRLEFSEVSVDEGTGSVTIRAVFPNPNNELLPGMFVHAQLQEGVKQKAILAPQQGVTRDLKGQATALVVNAQNKVELR... | Function: The periplasmic linker component of the MexAB-OprM efflux system that confers multidrug resistance . Functions as the major efflux pump for n-hexane and p-xylene efflux . Has been shown in one study to be involved in the active efflux of the autoinducer N-(3-oxododecanoyl) homoserine lactone, thereby playing ... |
B8MYS7 | MKKIYNVYFLCGFATLGGGLFGFDISSMSGVLGTAAYTNYFQVGSGQYKQGSITCAMPFGSLVGALCSSFIADRYSRVRAIQFSSILWIIGSIFMCASNGIPLLVVGRVIAGGCVGIASAMVPVYQAEIAPKEIRGRVISLQQWAITWGILIQYFIQYGASNIDGGPNNPTQSTAAFRIPWGIQIVPGVILFFGMFLFPKSPRWLASKDRWEEALQVLSKLHGQGDVNHPKVLAEYKEIQEALALEREQSATGFQELIKPRIFKRVILGMSLQMWSQLCGMNVMMYYIVYIMQSTGAGSPLLTASIQYILNTALTLPAII... | Function: Probable MFS glucose transporter; part of the gene cluster 27 that mediates the biosynthesis of asparasone A, a sclerotium-specific anthraquinone pigment important for sclerotial survival .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58332
Sequence Length: 529
Subcellular Location: Memb... |
Q6NUT3 | MGPGPPAAGAAPSPRPLSLVARLSYAVGHFLNDLCASMWFTYLLLYLHSVRAYSSRGAGLLLLLGQVADGLCTPLVGYEADRAASCCARYGPRKAWHLVGTVCVLLSFPFIFSPCLGCGAATPEWAALLYYGPFIVIFQFGWASTQISHLSLIPELVTNDHEKVELTALRYAFTVVANITVYGAAWLLLHLQGSSRVEPTQDISISDQLGGQDVPVFRNLSLLVVGVGAVFSLLFHLGTRERRRPHAEEPGEHTPLLAPATAQPLLLWKHWLREPAFYQVGILYMTTRLIVNLSQTYMAMYLTYSLHLPKKFIATIPLVM... | Function: Transporter that mediates the import of cysteine into melanosomes, thereby regulating skin pigmentation . In melanosomes, cysteine import is required both for normal levels of cystine, the oxidized dimer of cysteine, and provide cysteine for the production of the cysteinyldopas used in pheomelanin synthesis, ... |
Q3U481 | MSPPSDDAGPGPPRTLSLAARLSFAVGHFLNDLCAGMWFTYLLLFLHSVRGYSSRGAGLLLLLGQVADGLCTPLVGYEADRASCVRCGPRKAWHLAGTVCVLLSFPFIFSPCLGCGEATPEWAALLYYGPFIVVFQFGWAATQIAHLSLIPELVTSDHEKVELTALRYAFTVVANITVYGAAWLLLHLQGSAHGEQDISVGDQLGVQDVPVFRNLALLVVGVGAIFSLLFHLGTKEGHRSQHWGNEPNEHTPLVAPAAQPLLLWKHWLREPAFYQVGMLYMTTRLIVNLSQTYIAMYLTYSLSLPKKFIATIPLVMYLSG... | Function: Transporter that mediates the import of cysteine into melanosomes, thereby regulating skin/hair pigmentation . In melanosomes, cysteine import is required both for normal levels of cystine, the oxidized dimer of cysteine, and provide cysteine for the production of the cysteinyldopas used in pheomelanin synthe... |
A0A4Q4NJ90 | MAHSTAGDRDPEVGSEQHSSIAQLHTESMSDPWGDSNSPENPLNWPAPKKNFHVAIVSIFTLTANLAATMFAPGAPQLAKEFNITNSTVEAMTVSLYVLGFAFGPLLLAPLSELYGRLIIYNACNAVYIAFTVGCAFSTNVSMFLVFRFLCGCAASGPMSIGGGTVADITPQEERGKAMALFAMGPLLGPVLGPIIGGYVSQYTNWRWTFRIILIMSGIIGLATMFFMRETNAAVLLRRKAKRSPKDAEGMELELDKTKKETPSQVLVRAITRPFKMLLFSPIVLLISLYTGVLFGLIFLLFTTFPTVFQGVYGFDEGTS... | Function: MFS-type efflux pump involved in the modulation susceptibility to various compounds including cumyl hydroperoxide, potassium superoxide, many singlet oxygen-generating compounds (eosin Y, rose Bengal, hematoporphyrin, methylene blue, and cercosporin), and the cell wall biosynthesis inhibitor Congo red . Invol... |
G4MWA9 | MSNEGTNTVLKNPGSNQEEADPDSPSSLGDKSKLDELADSTSDGSQANSGRGIAFWAIFISLSVTGFLSSMEGGIMSTALPAVSRAVNAESDYVWIINVYFLTSAAFQPLYGQLADIWGRRWPMLSAVTIFAAGSAICGAANNSGTLIGGRAIQGLGAAGINTLVELILCDLLPLRERGQFMGLLFLFIVVGSVLGPMLGGIIVDKTSWRWIFFINLPICALCFGLLFFALNLKHRRDDNSTSLQKLKKIDFVGVLILCVAVTLLIYALTYGGGAKYAWSHPVIITTLVLGIFGHGLFIAFEASPWCSNPTTPLTLFQNR... | Function: MFS-type efflux transporter; part of the gene cluster that mediates the biosynthesis of a tyrosine-derived cytochalasan acting as a fungal signal recognized by resistant rice plants and leads to avirulence in Pi33 resistant rice cultivars . MFS1 might be involved in the excretion of the signaling tyrosine-der... |
B2KWH5 | MVTLSNVGADVEKNIVPEVNDASKRDSDNASADFQPGVKRVRAVASVWSKKTLWLTFALLYLVAFVDMLLVSVQSTLNPFITSSFEKHGLLASVSIVATILSGCSTLTLAKIVDVWGRIEGFLFMLLVVVVALIMKATCKNMEAYVAAHTLYWTGHIGMIYCVDVMLADMTTLRNRMIMFSINNTPTIASTFAGPKIADLFFSNLNFRWAFGAFAIMLVGVSLPVIVIMLFMERKSVKAGFLVKEKSGRSAWESIKYHLIEFDVVGIVLITASFALILLPFSIVVYAPKGWATGYIIAMEVVGVVCGAIFLAWERFLAPV... | Function: Major facilitator transporter involved in siderophore transport .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60879
Sequence Length: 560
Subcellular Location: Membrane
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D4AXV8 | MTEKDTDGADGLTKAKSNAVSEDYETVNHVTGLKLAVIVTGLCLSVLLVALDNTIIATAIPKITDQFHALEDIGWYGSSYLLTICAFQLIFGKIYTFFPVKWVFLIAITIFEIGSAICGAAPNSTALIIGRAVAGIGSAGIFSGALIIIAYSIPLEKRPAYTGAIGGMYGIASVAGPLMGGAFTDHISWRWCFYINLPIGAVTILSILIFLKHPKQKLDNNQTWKARLLKLDPIGTAFFMPSIICLLLALQWGGTKYPWNNGRIIALFVVFAVLISGFIYFQIRGGDSATVPPRILKKRSIASGAFFLFTIGSAFFIMVY... | Function: MFS-type efflux pump involved in the modulation susceptibility to azoles, including fluconazole, itraconazole, miconazole and voriconazole (Ref.2). Confers also increased resistance chloramphenicol and thiamphenicol, suggesting that it acts as a pleiotropic drug transporter with a broad substrate spectrum (Re... |
M2R8W9 | MDKTASLTSQDAEKHDPDALRKERATDPPDLFEHGALDPVYQAKAHLIASAIQEIGMGKYQWGLFVVAGFGWFSDSVWPLMGSLILSPVVNEFQFNSPFLSLALNAGLLAGAIFWAFGCDIWGRRWSFNLSLLIAGAFGLAAGGTQNFVALACLFAVVGFGVGGNMPVDSAVFLDFVPGSYQYLLTILSIWWSIGQLVASLIAWPLIANFSCPIGSTTCTRADNMGWRYLLFTLGGMTLLLWAIRFFVFPLMESPRFLVGRGRDAEAIAVIQRIAQFNGRPSSLTLEELAMVAEKAAPKDAVATQRRQVLSQSSDFSTDH... | Function: Major facilitator transporter probably involved in siderophore basidioferrin transmembrane transport .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56014
Sequence Length: 521
Subcellular Location: Membrane
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G4N2A8 | MTALAAVPDLQDAAGPSTTTVHSPNYSGSPADISSSPTTRAVSRNTARQTASAPPNHAESSPPGNASPTGPPSPSGNNVSPHGRHQGMSKLRACLVIATLSGVSFLNTMGSGILTVSLPTMARDVRLDDSLLLWPASVYSLAAGCTLLVFGAVGHIIGPKRVWITGACLYAAFTLGVGRSATGSQLIAFRSVLGVSIAMCLPTAVSLTTNGFGAGRWRNMAFAFQGMGQPLGYSTGLILGGIFTDTVGWRFGFYISGGINAVLAICALVVLPSPPRHDEGDGEQREVEEEATDATVAAAAVNRSSRSRPLISRLAHDVDW... | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of pyriculol and pyriculariol, two heptaketides that induce lesion formation upon application on rice leaves but are dispensable for pathogenicity . With the ABC transporter ABC7, is most likely responsible for pyriculol and pyricul... |
A0A0C4VYV1 | MTHSSSNEHEKEDDRRASDDMMDRDDQNAKEEQDVSKDAPPVNPWDPSQFPDGGFKAWSVVAGGFCSLFCSFGWINCIGIFQQYYQSDYLRGYSSSTISWIASLELFILFAGGLVVGRVYDRYGPRYILLFGTFMHVFGLMMASLSTEYYQILLSQGICSPIGISCLFTPAVNCIATWFRKKRGLANGIVAAGSSLGGVIFPIMFDRLIPRVGFPWAMRIGAFLILFLLIIANLTVVSRIPPMPKPITAKQYLAPFQERTYLLTTIAAMIFVLGLFLPINYIQAQAVEFGMDPSLANYLIPILNAASLFGRTVPGFVADK... | Function: MFS-type transporter that mediates the secretion of the 4 major naphthoquinone derivatives produced, erythrostominone (NQ1), deoxyerythrostominone (NQ2), epierythrostominol (NQ4), and deoxyerythrostominol (NQ5), as well as of 3 newly identified naphthoquinone derivatives termed NQ7, NQ8 and NQ9.
Catalytic Act... |
Q3T9M1 | MSVPHGPTPAPVAEPHTQEPGSDKRDGRLSVCTKVCYGIGGVPNQVASSASAFYLQLFLLDVAQIPAAQVSLALFGGKVSGAVADPVAGFFINKSRRTGSGRLMPWALGCMPLIALAYFFLWFLPPFTSLRGLWYTSFYCLFQALATFFQVPYTALTMILTPSPRERDSATAYRMTMEMAGTLMGATVHGLIVSSAHGSQRCEDTVHPRSPAVSPDVARLYCIAAAVVALTYPVCGSLLCLGVKEQPDTSAPASGQGLNFFTGLAITSQHPPYLSLVVSFLFISAAVQVEQSYLVLFCTHASKLQDHVQNLVLIILVSAV... | Function: Lipid transporter that specifically mediates export of sphingosine-1-phosphate in red blood cells and platelets . Sphingosine-1-phosphate is a signaling sphingolipid and its export from red blood cells into in the plasma is required for red blood cell morphology . Sphingosine-1-phosphate export from platelets... |
A4IH46 | MAETSRELPLSTLTASTRRALRIRARQAREAKLSVLSKVCYAIGGAPNQVSGSASAFFLQIYLLDVALISPYQASLVLSLGKTWGGITDPIVGYCISKSKWTRIGRLMPWMLGCTPFLVVSYFLLWFVPTFETGRVLWYLAFFSCFQALSTAYHVPYTTLTMFLSTDQMERDSATAYRMTVEVLGTLIGAAVQGQIVASAHTGSHCNVTNMTGNLTADFLYEPTEYITSARQVYMIAAGIIGCLYLLCISVLFLGVKERDDPYALVAGKVIPFFKGFRETMQFGPYLNLISSFLLISAAVQIQQSNFVLFCTHAADLQDH... | Function: Lipid transporter that specifically mediates export of sphingosine-1-phosphate in red blood cells and platelets. Sphingosine-1-phosphate is a signaling sphingolipid and its export from red blood cells into in the plasma is required for red blood cell morphology. Sphingosine-1-phosphate export from platelets i... |
B2KWH6 | MRSAFLSKLQTHAPVAQPQVISSGLAKEAGDLPQEQEVDAEDQLSADAQDGVRKIQATTQVWSKGHLIFAYVMIWVITFVDTMQQGMSNSLLPYVTSSFRLHSLTASTMIMSNIIGGLIKLPLAKVLDIWGRPQGFLIMVGALTIGLVMMAACNNVKTYAAAQVFYWVGYNGMSYTISIFIADTSALKNRALMFAFVSSPYIATVWVGGPLATVFLNGPGFRWGYGAFAIITPAITCPLYAVFAWNYKKAKDAGLLPEKTHSRTFTQSLKHYFFEFDIIGIILLASGLALFLLPFSLYSYQKDQWRSSLVISMIIVGGLL... | Function: Major facilitator transporter involved in siderophore transport .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64631
Sequence Length: 588
Subcellular Location: Membrane
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A9BJC1 | MKRFLGILVFVVMVLSVFAGPNHLVIFHMNDTHGHVWGTEDGGGFARAATLINQAREEVAKEGGAVLFLHAGDVNTGIPESDQLDAVPDFLALHYMGLDAMSLGNHEFDKPFEVLEKQYEVAQFPFLGANFVNEKRGGPVFEPYIIKDYGDFSVGIIGLVTEQTKVLEPIYLGENTIVDAEETLNMYLPIVQEKADVVIVLAHLGYHADGGRPNLSVEFTTSDELAENVSGVDIIIDGHSHTLLETPVVINNVIVAQAGDNAENIGRIDLWIDDGRIVDWRGEVIPLTSDIPEDPFIKMFTDAFYQLGSEALNEVVGVTK... | Function: Involved in the biosynthesis of the compatible solute mannosylglucosylglycerate through a phosphorylating pathway. Catalyzes the dephosphorylation of mannosylglucosyl-3-phosphoglycerate (MGPG) to mannosylglucosylglycerate (MGG). Can also dephosphorylate UDP-glucose, ADP-glucose, GDP-mannose, glucosyl-3-phosph... |
A9BFS6 | MEIGLVHYRVGETDGVSLEMVKWKQALRNMHLKTYLIAGDMGTSPGFKIPYIAYTDKRSNILKQKSFVNLDEWDENYFKKEMNKYIEDIYNQLYEMMDLDVMIVNNIFSLAHNPAAAVAIYRFCKDNGIKMIGHHHDFYWERDFYKNPTNDYIKEILEEYFPPKDITHVVINSLAQEELKNKKGLDSIVIPNVFDFNQKRWEIDDYNIKIYDKLNISQKDLIFLQATRIVRRKAIELAIDTVAEVKKDLKKYIGKTTFNGKKITQDTNVFLVLPGLSEESDYVEVLKEYASQKDVELKLAFSISDDIRHEEEEIFSLWDF... | Function: Involved in the biosynthesis of the compatible solute mannosylglucosylglycerate through a nonphosphorylating pathway. Catalyzes the synthesis of mannosylglucosylglycerate (MGG) from glucosylglycerate (GG) and GDP-mannose.
Catalytic Activity: (2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + GDP-alpha-D-mannose = ... |
Q9X0V7 | MKIALIHYRGGLMDGVSLEMEKWKKVLTKMGHEVHIVAENKKEGVDLTLKEIGFENPDFERVNRNFFGGIKDFLSEKEFLDFLKEKEEELFHILNEALKDYDLIVPNNIWSLGLFPSLGLALSRLEKNFVAHHHDFWWERKHLIPENRRFREILDKHFPPDLPNVKHVVINTIAQRELKRRRNIDSVVVPNVMDFSSPITSEEMYHRVREELQIAPGTIVALQATRIDRRKTIELSIDVVSLLKETLTSKKEADLYNGERYSGEVILLFSGICEDEEYLKELKEYASSKGVSLLVLSEEVRKNTSLFWKLYNAADFVTYP... | Function: Catalyzes the synthesis of mannosylglucosylglycerate (MGG) from glucosylglycerate (GG) and GDP-mannose.
Catalytic Activity: (2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + GDP-alpha-D-mannose = (2R)-2-O-[alpha-D-mannopyranosyl-(1->2)-alpha-D-glucopyranosyl]-glycerate + GDP + H(+)
Sequence Mass (Da): 49702
Seque... |
D8QTR2 | MAGPVRCLPPVVEATSIPHAPPVISKEVSEIVNNMLSVAIPAAAAASAQDQRFASQFRCGPEFTTMKAQALEACRKILAENDQGGYTIPAKGLYPYQWNWDSALVSLGLAEMEEERAWEELDRLMSAQWEDGMVPHIVFHKPSSTYFPGPEIWGSPDKPRNTTGITQPPVAAISVRRLLEEAKDKALALAMARKLFPKLLAWHRWFYRARDPEGTGLVATIHPWETGMDNSPAWDEALARVPIDDIPPYVRRDLGHVDAKMRPQKAEYDRYLTLLYRFRALDYDEAKLYYETPFRVTDLCTNCILHKANEDLLWLAGATG... | Function: Catalyzes the hydrolysis of alpha-D-mannosyl-glycerate (MG) to D-glycerate and D-mannose . Can also hydrolyze alpha-D-glucopyranosyl-glycerate (GG)with lower efficiency .
Catalytic Activity: (2R)-2-O-(alpha-D-mannosyl)-glycerate + H2O = (R)-glycerate + D-mannose
Sequence Mass (Da): 54528
Sequence Length: 488
... |
Q03649 | MRLKELLPNFLIVHQEVPEDPIAFKSTDKRENENKEITIPELIDTKVPELADGATDTLYGLLVNGHLQTAYGSFRHFDNIYKVQYKRMIIKYPHGGEGTVDFAVNGRSTKRRKVEKEYVPTSQPVFNGNLKRRYSYYSPDDPKLNSDDAKPMLIILHGLTGGSRESYVRAIVHEITTKYDFEACVFNARGCCYSAITTPLLYNGGWTNDIRYCVNDLRKRFPNRKFYMMGFSLGASIMTNYLGEESDRTKIECAISVSNPFDLYNSAYFINSTPMGSRFYSPALGHNLLRMVRNHLSTLEENPDFKDVIEKHLKKIRTVR... | Function: Converts monoacylglycerides (MAG) to free fatty acids and glycerol. Has a preference for palmitoyl-MAG . Does not play a significant role in ethyl ester biosynthesis . Also possesses ester hydrolase and low but persistent TAG lipase activity .
Catalytic Activity: Hydrolyzes glycerol monoesters of long-chain f... |
Q6LK34 | MNQVLLEMRGITKTFPGVKALDNVQLTLKKGRVMALMGENGAGKSTLMKVLFGIYQRDCGTIRYQGEQVNYSGAKEALEAGVSMIHQELSPILHRSIAENIWLGREPLKGPLRLIDHAKMYRDTTELLKKLDLHLDPRTPMSELTVATMQMIEISKAISYNSKIIIMDEPTSALTGKEVDHLFEIIEKLKKQGVSIVYISHKMDEIFRICDDITVFRDGCYIGEREAQNTNHDELVQMMVGRDLGDVFPPPTAKPGKVRLEVKNLSVEGVFDNISFKLHEGEILGIAGLVGAGRTELIETLFGVRKHDVGEIWINGENVE... | Function: Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-galactose(out) + H2O = ADP + D-galactose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55... |
Q896Y2 | MVENNIILEMNGISKNFPGVKALDGVDLKVKKGTVHALMGENGAGKSTLMKCLFGIYRSDDGEIVLGGKKVQFKNAKDALENGISMIHQELHPVPHRSVMENVWLGRFPVKKVFGLGIVDHKKMYEDTKDLLGKLKMNIDPNTLVSKLSVSQVQGLEIAKAVSYNSKIIVMDEPTSSLTENEVTHLFNIISDLKNQGVAIIYISHKMEEILKIADEVTIMRDGKYIGTWEAEGLTTDLIISKMVGRDLTNRFPPKENTPGEVIMKVENLTSANNKSFKDISFELRKGEILGIGGLVGAQRTELVESIFGLRKIETGKIYI... | Function: Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-galactose(out) + H2O = ADP + D-galactose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56... |
P0AAG8 | MVSSTTPSSGEYLLEMSGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGTILFQGKEIDFHSAKEALENGISMVHQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRETKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEVTVLRDGQWIATEPLAGLTMDKIIAMMVGRSLNQRFPDKENKPGEVILEVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTI... | Function: Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import. Responsible for energy coupling to the transport system (Probable).
Catalytic Activity: ATP + D-galactose(out) + H2O = ADP + D-galactose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Ma... |
Q8REE1 | MENLKYVLEMENISKEFPGVKALDDVQLKLKPGTVHALMGENGAGKSTLMKCLFGIYEKNSGKILLDGVEVNFKSTKEALENGVSMVHQELNQVLQRNVLDNIWLGRYPMKGFFVDEKKMYNDTINIFKDLDIKVDPRKKVADLPIAERQMIEIAKAVSYKSKVIVMDEPTSSLTEKEVDHLFRIIKKLKESGVGIIYISHKMEEIKMISDEITILRDGKWISTNDVSKISTEQIISMMVGRDLTERFPKKDNKAKEMILEVKNLTALNQPSIQDVSFELYKGEILGIAGLVGSKRTEIVETIFGMRPKKHGEIILNGKT... | Function: Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-galactose(out) + H2O = ADP + D-galactose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56... |
Q8UIV6 | MEGQRCIALIAHDEKKDDMADFARHHQKVLASFRIVATGTTGGRVQEACPGLEVIRLKSGPLGGDQQIGAMIATGEVDMLIFFTDPLTAMPHDVDVKALTRLATVYDIPMALNRATAENLIDFNSAD | Function: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Catalytic Activity: dihydroxyacetone phosphate = methylglyoxal + phosphate
Sequence Mass (Da): 13753
Sequence Length: 127
EC: 4.2.3.3
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Q5WGQ3 | MKIALIAHDKKKQELVDFCVAYEPILKEHELYATGTTGTRIMEATELVVTRFKSGPLGGDQQIGALVAENQFDLILFMRDPLTAQPHEPDVTALIRLCDVQSVPLATNMGTAEILIKGLERGDFAFRDIIHEQEKANPLKEG | Function: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Catalytic Activity: dihydroxyacetone phosphate = methylglyoxal + phosphate
Sequence Mass (Da): 15759
Sequence Length: 142
EC: 4.2.3.3
|
A7GN71 | MKIALIAHDKKKDDMVSFAYAYKPIFEQHELFATGTTGLRVMEATGLAVTRYQSGPLGGDQEIGAMIAKNALDMVIFFRDPLTAQPHEPDVNALLRLCDVYAIPLATNMASAEMLMHALNRGDLDYRKFRK | Function: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Catalytic Activity: dihydroxyacetone phosphate = methylglyoxal + phosphate
Sequence Mass (Da): 14619
Sequence Length: 131
EC: 4.2.3.3
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Q72NU6 | MKEVSVPAIKRIVLIAHDNRKEDLVNWVKTHREILSKHQLYGTGTTGKLISEETELPVYRFLSGPLGGDQQIGAKIAEGDLDIVIFFWDPLTAQPHDPDVKALLRIAVLYNVPMACNRSTADYMISSPQFTKTYKKILLSYNTKVKKD | Function: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Catalytic Activity: dihydroxyacetone phosphate = methylglyoxal + phosphate
Sequence Mass (Da): 16727
Sequence Length: 148
EC: 4.2.3.3
|
C6BZQ4 | MSKVKNIAVVAHDNCKKELLDFVDCNHNILSRHNLVATGTTGGLVEKMIMERVEQKADEGYEFKPVNRMKSGPLGGDQQLGAMISEGKIDVLIFFWDPMQPQPHDVDVKALLRLAVLYNIPTASNRSTAEFLISSPFFEGEFQRKETDFSSYTQRKL | Function: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Catalytic Activity: dihydroxyacetone phosphate = methylglyoxal + phosphate
Sequence Mass (Da): 17720
Sequence Length: 157
EC: 4.2.3.3
|
B2A7A5 | MRIALIAHDNKKDELLHFIKRYEHVLATHTLCATNSTGRLIAENTNLMVHRYQSGPLGGDQQIGSEIATGNVDFVFFLRDPLTAQPHEPDITALLRICDVHNIPVATNFATAEILVESVL | Function: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Catalytic Activity: dihydroxyacetone phosphate = methylglyoxal + phosphate
Sequence Mass (Da): 13329
Sequence Length: 120
EC: 4.2.3.3
|
Q30ZX0 | MKGQRNIGMVAHDERKEDLLDWVQHNLQALIPHRIFATGTTGGLLRQRFGDLTITPMKSGPLGGDQQLGSMIAEGRLDMLFFLIDPMAPHPHDVDIKALLRLAVLYNIPAAYNRSTADFLITSPFMTGEYIPEIKDYTPYVKRLGAK | Function: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Catalytic Activity: dihydroxyacetone phosphate = methylglyoxal + phosphate
Sequence Mass (Da): 16477
Sequence Length: 147
EC: 4.2.3.3
|
Q6D6C8 | MEFTTRTIPAQKHIALVAHDHCKQSLLDWVGTNKQQLTEHTLYATGTTGNLIQSNTGLPVKSMLSGPMGGDQQVGALISEGKIDLMIFFWDPLNAVPHDPDVKALLRLATVWNIPVATNRATADFLINSALFKEPVQIAIPDYQRYLQDRLK | Function: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Catalytic Activity: dihydroxyacetone phosphate = methylglyoxal + phosphate
Sequence Mass (Da): 16878
Sequence Length: 152
EC: 4.2.3.3
|
A0R1T4 | MNSPGAVDVVIVGAGPVGLTLANILGGQGVRTLIIEERETLIDYPRGVGLDDESLRTFQSIGLVDAILPHTVPNQILRFYDANRRLLAEMAPPDARFGWPKRNGFVQPMVDAELLAGLDRFDHVEVMWGRRMQTIAEDADGVTVEVSGPDGPASVHAQYVVGCDGGRSATRHLMGVSFDGTTSSTRWVVIDLANDPLGHPNSEVGADPQRPYASISIAHGIRRFEFMIHADETDEQAEDPEFVAELLRPFVPHPDRVDVIRRRVYTHHSRIAGSFRKGRMLLAGDAAHLMPVWQGQGYNSGIRDAFNLGWKLAAVVRGQA... | Function: Catalyzes the insertion of one atom of molecular oxygen into position 2 of the phenyl ring of 3-(3-hydroxyphenyl)propionate (3-HPP) and hydroxycinnamic acid (3HCI).
Catalytic Activity: 3-(3-hydroxyphenyl)propanoate + H(+) + NADH + O2 = 3-(2,3-dihydroxyphenyl)propanoate + H2O + NAD(+)
Sequence Mass (Da): 61387... |
Q4P8D2 | MLSSKLVACSAGRSVQRISRTFLPAMRGVATKAAAGPSRQSALSSYSIAAVTAIGVGASFYALQSRSSAIQCEPRQAWHDRLKPKEAKGDATLHKDAHTRHAPAEVQDERVEPVEETPVAIEVAVEESEEQTGQQSAYDPETGEINWDCPCLGGMAHGPCGEQFKLAFSCFVYSEAEPKGIDCVDKFKAMQDCFREHPDVYKDEIEDDEAANAQFEKEEANAKSNGLNDAAQEAVEESSGGKEGASA | Cofactor: Cu(2+) or Zn(2+).
Function: Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Forms a redox cycle with ERV1 that involves a disulfide relay system. Precursor proteins to be imported into the IMS are translocated in their reduc... |
Q6PBC3 | MSYCRQEGKDKIIFVTKEDHETPSSAELIADDPNDPYEDHGLILPNGDINWNCPCLGGMASGPCGEQFKSAFSCFHYSQEEIKGSDCLDQFRAMQECMQKYPDIYPQEDDEDEAEKEKQNKEAEAFSTETSDTKEESSS | Function: Central component of a redox-sensitive mitochondrial intermembrane space import machinery which is required for the biogenesis of respiratory chain complexes (By similarity). Functions as chaperone and catalyzes the formation of disulfide bonds in substrate proteins, such as COX17 or MICU1. Required for the i... |
P36046 | MLRNLVVRNACRNRPSIQVARGLCRHQTRRLMASSPQFGRNSNQEKTAGFIMGILSMAGALYFIAPNRKPLFASRKVESDKTAEEELSSGGEQSPENEDDNNSKSDENGDDNDSKNDETEAGPQLGGDKIGASKVAEDGELVVLAEEDNKSSEDKDTDESKVSTKDDEQSNEDNATANNQKDENISSENSEENTSDKTLDNNAGSSEKKDPEHSDDEKSQQGQSDDKTTTEDNNGEEESSKKTVSDSENSAKQSESSDEEKEELRKQEEKQMGPTEEEVQHEGAYNPDTGEINWDCPCLGGMAHGPCGEEFKSAFSCFVY... | Cofactor: Cu(2+) or Zn(2+).
Function: Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Forms a redox cycle with ERV1 that involves a disulfide relay system. Precursor proteins to be imported into the IMS are translocated in their reduc... |
Q8A018 | MPTLIVLIGPTGVGKTELSLRLAENFHTSIVSADSRQLYAELKIGTAAPTPDQLKRVPHYLVGTLHLTDYYSAAQYEQEAMEILHQLFTEHEVVVLTGGSMMYVDAICKGIDDIPTVDAETRQVMLQKYEEEGLEQLCAELRLLDPDYYRIVDLKNPKRVIHALEICYMTGKTYTSFRTQQKKERPFRILKIGLTRDREELYDRINRRVDQMMEEGLLDEVRSVLSYRHLNSLNTVGYKELFKYLDGEWELPFAIEKIKQNSRIYSRKQMTWFKRDEEIRWFHPEQETEILEYLRLQNLTHLPSLDTF | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
A5GE43 | MSCNLLVILGPTASGKTQLGVELARRLSGEIISADSRQVYRGMDIGTGKDLAEYGDIPYHIIDIVDPGFEFNVFEFQRCFQRAFAHIVNRGRLPVMVGGTGMYLEAVLNRYRFVEVPENADLRRELSTFSDEELAERLKGANPRLHNTTDLLERGRLVRAIEIAEYEDSREPLPLPELAPLIFGIRWERPVLRQRITDRLKARLEQGMIDEIEQLHRSGIPYETLEFYGLEYRFVAKYLKGELNRNDMFQKLNSAIHDFAKRQDNWFRRMERHGTVIHWLEGDGDPLKEAQEILRLNAIPR | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q2SJX0 | MSIANDNPNARPVVVLGPTACGKTRLAVALARAFAGEVVSADSRQVFRGMDIGTGKDLQDYGDTPYHLIDIVDPGAPFSLFDYLGAMQRTLDDLDAREKRPIIAGGSGLYLDAILRGYRLVEAPVDPLLRERLKHHDQERLNALLASLRPLHNTTDTQDRERTLRAIEIAYAELNEDSPSVQISIDPVVIGLHCDNDRLRARIRERLETRLDEGLIEEVESLRAEGLSWRQLDELGLEYRYVALYLQEQLNRNDMMQKLASAIYLFARQQVKWFRRMERQGVAIHWLEADDAPLDNALALLRR | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
A6L8Q7 | MKSYELITILGPTASGKTTFAAALAAQLDTEIISADSRQIYRSMDIGTGKDLADYNVNGKQIPYHLIDICEPGYKYNVFEYQHDFFRVYEDMKRRGKLPILCGGTGMYIEAVLKGYKLLDVPQNPELRESLRNKTLEELETILASYKILHNKTDVDTAQRAIRAIEIEEYYKTQAPDVNEYNPINSLIIGIHIDRELRREKISRRLRTRLDEGMVDEVRTILATGVKPEDLIYYGLEYKFLTLYIIGELSFEEMVSQLEIAIHQFAKRQMTWFRGMERRGCEIHWIDATLPTEEKIATTMRILNNQL | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
B2RKS4 | MITILGPTACGKTRLAVSLAYRLGTEIISADSRQIYRGMDIGTGKDLADYQVGGTTIPCHLIDIRPAGDKYNLFAYQHDFHQAYASILARGMDPILCGGTGMYIEAVLKGYHLPDVPPNPTLRDRLQGKSLTELTLILAAYGPLHNKTDVDSAQRAIRAIEIAEYIKNNPAESTEFPPIDSLIIGLDLDRDTRRKRITDRLHARMHEGMIEEVKGLLDSGIPADDLIYYGLEYKFVTLYLTGQTDYESMFTGLETAIHQFAKRQMTWFRGMERRGFLIHWIDALLPADEQCEAVMKLYTANG | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q2LTI8 | MMKNLVVILGPTASGKTRLAVRLARDLKSEIVSADSRQVYRGMDIGTGKDLDEYRIDGEEIPCHLIDIVDPDYDFNVFEYQSRFYRCFEEILSRGIVPILVGGTGLYLSAVLENYRMVQVPENLDLRESLKAEPLERLQQILLEITPRIHNTTDLLDRGRLLRAIEIAQHSGRRGLRESPEHPRIEPLVFGVRWNRDLLRKRIALRLKERLSAGLIDEVKELHQSGISWDRLEFFGLEYRYVGLYLQSRMSYREMAEKLTIHICRFAKRQETWFRRMERHGIEIIWIEGDDYEALKEQLKGNLRS | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q056X7 | MNKKKFLFFLMGPTAIGKSSLALEIKKKFPLIELISVDSKLVYKGLNIGTDKPNKSDLKNFSYKLVNIVKPKNIYTVINFYNDVLKEIKNILKSGKIPLLVGGTMLYFKILLNGFANLPPSNSIIRKYIFKNICLKKKKNLFNLLKKIDPISSKKIHINDVQRVLRAVEVFFVSGGFPLSELIKFFHNKLPYKVFQFGLIPDNKEHLYKKIEKRFFFMLKSGFKKEVQNLYNQKFLDPKLPSMNSIGYKQMLLYLKNKYTYFQMIKETIKSTHKLVKHQLTWLKKWPNIIFIKDNKKDLLITKIYKILNRNL | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
A3NYW4 | MSERNAASARTVACLLGPTASGKTAAALALAARRPIEIVSVDSALVYRGMDIGTAKPTRDERAAVPHHLIDIVDPADAYSAAEFRADALRLVAQIAARGRTPLLAGGTMLYYRALTQGLNDLPAADPDVRATLDADAARDGWPALHARLAGIDPATAARLAPNDSQRIQRALEVYLLTGQPMSALLAAPPRDDDAAAGLRFVPVALEPSERAVLHARIAARFDAMLEAGFIDEVERLRRRDDLHLGLPSMRCVGYRQAWEYLDGCTDYRTMRDKGIFATRQLCKRQLTWLRAMPERIVVDCCAPDATVRAVDALERVLDG... | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
B9MJT8 | MEKIPLIVIAGLTATGKTDVAVELAQLVNGEIVSADSMCVYKLMDIGTAKPTKEQREAVRHHVIDVVFPDEDYNVAMFQKDATNAILDIYKRGKVPLLVGGTGFYIKSVVDDIEFPEMGDSKQVRKKLFDELNNKGNMYLYELLKEIDKDAANSVHPNNVKRVIRYLEIYFLTGKKPTEFLDKVRRKGSERYNVLPLCFIMEREALWQRIDQRVEKMFDMGLADEVKMLLDMGYSKDLKSMQGLGYKQVIPYVEGKISLQEAKEELKIRTRQFAKRQRIWFKYQGEFVFLDVTGMRFEEVVKKCFELCKSVV | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q7U323 | MKIIAVLGSSGSGKSALAHRIAMEQNCKIFSLDSLSIYKYLDIASAKPTLLEQSQVCYYALNILEPHQKSNVMIFKDLLLQSIEDIKNNSPHTPLLIVGGSSFFLKSIMEGLSPMPPLEEHEEWVKSLGNISMQYAQLTQIDKTYAQSLSPTDTYRICKALALFKATNTPPSIYFATHKKESLGYDIEIFCLECERDELRERIAKRTKAMIQKGIVEEVQNVLEAYGAQAPALNAIGAKECVNFLQGKVATLQQLEEQIFFHTCQLAKRQRTFNRTQFAQITHLKEKALEAQLIQQIHNNIL | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
O25961 | MIKEGFLIKTPKKLIALLGPSGSGKSALSIELAQELDAEIFSLDSLSIYKDINIASAKPSLKERKNIKHYALDHLNIDEKNNAPLFKTLLEDAMRVSSKEILLIVGGSSFYLKSILEGLSRMPKLSGEEVVKIEREIATLSNPYIFLKSIDPNMAFKIHPNDTYRTHKALEIFYATCTPPSEYFKANPKKPFEHAISLFALSIEKSALHNNIKRRTKNMLHSGLVEEIKALYTQYPKDSQPFKAIGVKESVLFLEKRLTLKELEEAITSNTMKLAKRQNTFNKTQFNNLYVGSAEEVRHAILKHSKSGIKG | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
A9AY15 | MQAPQPLIIAIVGPTAVGKTAFSLDLAQALNGEIVSVDSRLVYRGMDIGTAKPTPAEQALVKHHLIDVVNPDQEYSLATYQAAAYAAIAQIQQQAKQPILVGGTGQYMAALLEGWSIPEVAPNYELRARYEQQAASEGHAALHQQLQTIDPEAAKAIDPTNVRRVIRALEVFHETGQPISQLQQRNPPHYRILTLDLERPRDELYARIDQRVDLMMREGLIAEVWALIRQGYGWELPSMSGLGYAEFRPLWQGQQSAGACISQLKFNTHRFARKQGAWFRRLPKRVSLDARHTDLLAQVQELLAMPEHAPIHTDH | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q31GP3 | MQSMNVAQLIEQKICLAIMGPTASGKSGLTMALAKHLPIEIISVDSALIYRGMDIGTAKPTLDEQVAVPHHLIDILDPTESYSAADFVEDVHELVKEIFARGNLPVLAGGTMMYFNALQQGMAKLPSADEAIRAKIHQAWQANPAAVHAQLKQVDPEAAERIHQNDPQRLIRALEVYEMTGKPLTQLQREGQQEGLTEFKLAKVALIPEDRKKLHEQIAVRFHEMLNNGFLKEAEKVFSLDGLSADLPAIRSVGYRQAWLFFAQEYDYDTFVEKSIVATRQLAKRQITWLRKEQDLLVLDPFKTNVDDRVEAVLDYLSAL... | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
B4U6P0 | MSIDAIIIGGPTASGKTEIAHELAKLLNTEIISADSMCVYKFMNIGTAKPSLEKRKEIKYHMIDVVLPNEYFDTYIYVEKAKSIIKQIKEKGKIPIIVGGTYLYIQALLYGLPETSEPDFRLRKKLESIANKKGLHFLYEKLKVIDKVYAEKIGKNDKKRIIRALEIFINTGKPFSSFHKWHEPTMKVLGFYTNLTQEELNKNIEKRTYYMIEQGLEVECINLLCLGYKEAMTSSQAIGYKEMIPYIEGKSSLKEAIENIIKNTKEYASRQRRWFQKTTFTPIRTIEDIKHHLQSLVL | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q0C511 | MHPAILIHGPTASGKSALAIELARKLGGEVINADSMQVYSDLQVISARPTEEEMAGVPHHLFGYVDAGRRYSTGEWLESARSVLKRLQRQNKHAVIVGGTGLYLLALTQGLSDIPPVPEDIRAEVKAISESEGADGLRLRLAPHDPELAERLGTGDRQRLARAYEVWLATGRQLSEFQNERQPPVLKEGEWVGFALTPPRAALYKKIDRRFEGMLMQGAVAEARALVSRNLDPELPAMKALGMPSIAAFVRGEISAEEAAESAKRESRRYAKRQFTWIGRQFPFWPRIPSPEVSDRMRVIFALYREIDTADTEDYA | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
A6W849 | MGQPNVPLVAVVGPTASGKSDVGVALAHLLEREHGRPGEVVNADAMQLYRGMDVGTAKLTPAEREGVPHHLLDVLDVTETAEVARFQADARAAVEDVTARGGLPLLVGGSGLYVRAAVDDLRFPGTDPEVRARWEAELAVLGPHALHARLAERDPAAAAKILPGNGRRIVRALEVGELTGRPFAASLPEQTYLRPTVQVGLAVPREQLDARIDARVERMWAAGLVAEVRDLEARGLREGRTASRALGYAQVLDAFDGTTTEDEARELTARLTRRFARKQESWFRRDPRVHWLPAPDGSDPLDLARRVLELLPVASAA | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q92HW4 | MLACNDDTSLYLLVKQVTKKEIYSNDLENGNVKRGASMQSLYLIGDPKCCRNNSSKQKSIIILCGPTASGKSYLGHELAKAYNGEIINIDSMQVYKEIPIITASPPKSYKTEILYHLYNFLSMTEDFSVIKYLKLATEKIKEITDRGKLPILIGGTGLYINSLVFGYNNIPDISEDLQEQVRNLHVKIGNIELWSKLEKFDPLAASKINQNDTQRLIRAYEVFMQTGKSIFSFQTLPKEQILSDFNFKIIFLNPERKFLYKTCDERLDKIFKEGAIDEIALIKKQFAPKDYTNLKAVGIKEILAYLNGNLTLDEALNAAQ... | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
A5UYJ2 | MIPLIAIVGPTAVGKTALSIRLAQQFNGEIVSVDSRQVYRGMDIGTAKPTPAERAAVPHHLIDIVDPDEAFSLAVYQDLATAAIADIAARGRLPFLVGGTGQYLAAVLQGWQLPRVAPRPDIRAALERQAAELGAAALYARLAEIDPAAAASIPPNNIRRIIRALEVYEATGKPISEQRSVQPPPYHTVTIWLTLPTPALYARIDARVEAMIAAGLLDEVHRLLERGYHWDLPSMSGLGYREFRPYFEGRITLDEAIARLKYDTHAFARRQPAWFRRLPNVLTLPADASDLQQQAATIVRQWIDA | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q1AW38 | MRSARVVAVCGPTASGKSEVADELSALLTEAEGVWVPTVVVDSMQVYREIPEITNQARSRPAELVGVVPVTREWTVAEHRRRARAAIEGSGAGAAVLDAGTGMYLNATVLDIPLAPKVPREIRALAQRAAAGAANPRREARRLELELYGAPERGSIWEGEPAYELALIYLRPERASLDEAIARRSSRIARRGLADARRLQDLLEAGARVNPSVLGSIGVRELLSHLRGEISLPEAEETISVRTRHLARRQMRWFDKLARTLSGRARLVVSPSPEDPALRKALHSMHDIIGA | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q5LSV5 | MAVGAALPPIPEGAPVLIAGPTASGKSALALEIAERFGGVIVNADASQVYDCWRAISARPSPEEEARAPHLLYGHLPYDAPYSAGHWLREVTPLLDGTARPIIVGGTGLYFTALTEGMADIPATPPDVRAEADTLPLDRLLAGIDPATAAGLDRNNRARVQRAWEVERATGRALHLWQADTPPPPLPLARTVPLVLEVDKLWLWDRIARRFDQMLDQGALDEVAAMAARYDPALPAFKAIGVPELMAHLRGEITLDAARERASIATRQYAKRQRSWFRARMGDWHRLPVGG | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
B8GNC6 | MPQPMSPPAIFLMGPTASGKTDLAVELVRRLPCEIISVDSALVYRGMDIGTAKPGPEILAEAPHRLIDILDPAEAYSAARFREDALAAMAEIAAAGRVPLLVGGTMLYFRALEFGLDRLPEADPEVRAQIEAEAAASGWEAIHARLAAVDPPSAARIHPNDPQRLQRALEVYLLTGRPLSAFHGGADASTLPYRLLRLALIPADRAALRERIARRFDQMLELGLIHEVETLYRREDLNPSLPAIRAVGYRQAWAYLAGEMDFETMRSKAIIATGQLAKRQLTWLRSYPGIEVLEMEQLDPAAVVARVRAHLEAARAGAGP | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
O83644 | MRLETQALVPYPVRFDRSHHDALVVLGATATGKTALAVALAQKYQGEIISADSRQVYRGLDVGTGKDLALYGSVPYHLIDVCDPYEEYNVFRFQQAVYGIVPSILRAHKVPIIVGGTGLYLDAVLRQYALVPVERNQALRASLRGASLSHMRAVYFSLKDSHAVHNKTDLEDPARLMRAIEIAVFHATHPELLQQARETRPMMRAKVYGIQYPRSMLRARIRARLEQRIRGGLIEEVAALHKGGVSWQRLEYFGLEYRFTAQYLQGIIATRDEYVDLLFRAISRFAKRQETWFRRMQRLGVKIHWLVHTENGFVLR | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q820X9 | MLAVAFVGATGTGKSLLSLDAARDFNGHIVNADSMQLYRDMDIGTAKLSHSARQGIPHHQIDVIDPSSEASVARYKLSAQTCIKHIHALNSIPFLVGGSGLYVSSVVHNLQFPPTDGRVRKLLEDEADKSGIGVLHDRLLKLHPGFTVSRGNRRRIIRALEVAYITGRSPNPVLPLQNRANNFIVINLICDKGTLDIRLQKRVESFYDNGLIDEVRLLQEKYVLGRTAAKAIGYKQAIMYLAGEISCADAKDSTLQETIRLANKQIKWFRRYSGQHIVDTTDMSVAYEQIRSILNKSFRIS | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
A1WQM5 | MAAPDSRLPNIALAGPTAAGKTAAALALAAALGRRQAVEIISVDSALVYRGMDIGSAKPTPAERAAVPHHLIDIRDPLQAYSAAEFVQDARRLIGEIRARGALPLLVGGTMLYFKALFDGLDAMPAADPAVRARLNARAAEQGWPALHTELARVDPVTAARLAPGDSQRIQRALEVWQISGQPLSSFHAIEKGAAGAYGACACALFSLEPQDRAWLHERIARRFDAMLAAGFIAEVQALRARGDLHPDLPAMRCVGYRQVWEALDWQARHAGGPPLHGAPLHARGMDAVRERGVAATRQLAKRQITWLRSMPQRHTTACD... | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
A5CW57 | MPIQINKTVIFLMGPTASGKTNLAIKLSQQFKTRLISVDSALIYKGMNIGTAKPDKATLKKYPHYLINICSPESSYSVFDFIRDANKQIKTAFAKNELPILVGGTSFYFHVLEHGLSNLPESSTKSKEKFNQLLRNKGTIKLHQDLKKIDPQAANKIHPNDSQRIIRALEVFNLSGKTISELQGNKKPIIDYPIKKIILMPKRNELHTKIETRFLLMMKNGFLNEVQHLKQNPNLHQNLSSIRCVGYRQAWQYLNGKIDKTEMIEKIIIATRQLCKRQITWLKSEKYALVLNNSNLAKAVTFINS | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q8D318 | MNENKCTDKINNLPKAIFIMGQTAVGKTKIAEILKKKLPVEIISVDSGCIYKGMNIGTDKPNVKKSSSDKYHLIDICEPNDYYSVENFRLDALKIMEKISKKGLIPLLVGGSMFYFKSLLHGLSNLPSYNIENKNLLKKKINEIGWYKSYIFLKKIDPIFASNIHPNDHYRLTRALEIYFSSGNIPTNLFKAKTKKLEYNIRQFSIMISDKKILYKKIKDRFFNMLKNGFKKEVEFLKNKKQINKNMPSMRCIGYKQMLAYLSGEINYKEMILFTISATNKLAKKQSTWLKKWKNINYIYNKDVYISSEEIFNILKKDNF... | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(3... |
Q97I18 | MDKNKLFFIETWGCQMNAEDSEKLAGMLKEMKYEATDNREDADLIIFNTCCVRENAELKVYGNLGTLKKLKDKKPNLIITVCGCMMQQRDMAEHIKKRFPFVDIVMGTHNTQMFPQYLKKVENERTSVVEIWDKEEGIVEGMPIYRSYDMKAFVTIMYGCNNFCTYCIVPYVRGRERSRKPEDIENEIKELVKKGYKEITLLGQNVNSYGKSLDEEMNFALLLRRLNNIEGLLRIRFMTSHPKDLTDDVIAAIADCDKVCEHIHLPVQSGSTTILNKMNRNYTREDYINLVNKIKSGIKNVAITTDIIVGFPGETEEDFE... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
Q895H1 | MLNNIVNTIHSDKNQKGTFFIETWGCQMNEEDSEKLSGMLKNIGYKNAEDKNQADIIIFNTCCVRENAELKVYGNLGALKGLKSKNPNLIIAVCGCMMQQEGMAEAIIKKYPFVDIIFGTHNSYKFPEYLNRAKQEGKSIIEVWDKEEEIVEGIPVDRKSSTKAFVTIMYGCNNFCTYCIVPYVRGRERSREVSDIEKEIKELVKSGYKEITLLGQNVNSYGKDLEPKVSFAELLRHVNEIEGIERVRFMTSHPKDLTEDVIYAIKECDKLCNHIHLPVQSGSSRILKKMNRYYNREDYLNLVNKIKEEIPNVAITTDII... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
B5Y8R7 | MKYYIFTYGCQMNKNDSEMVSGILKSSGWEEAKNVVDSDLVVINTCSVRLHAEERAIGTISALKKLGKKVVVMGCMSEVRGNEIMSRFPHVQAVLGPSYEAHILDVLNGERRILVGDEKVDFEKYSSANRKEKHSVYVSIMKGCDDFCTYCIVPFTRGRVQSRDPESILEEVRVCVDNGAVEITLLGQNVNDYGKDLSGWDFVSLVERVATIDGVRRIRFMSPHPANFKKDDITRLANLPQVAPYYHLPLQSGDDEILRRMNRKYTTGEFAELVGFIRESVPNVAIGTDLIVGFPGESDEHFQNTFKFLEKMQFDVVYMA... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
Q2G9P6 | MSSSAPSSASPKTFRVKSFGCQMNVYDGERMAELLAAQGMSAAGDGDDADLVVLNTCHIREKATEKVYSDIGRLRRADGSAPLIAVAGCVAQAEGEEIMARAPSVKVVVGPQSYHRLPEMVADAAAGKRSTETDMPAEAKFAALPKRRKSAPTAFLTVQEGCDKFCTYCVVPYTRGAEISRPFSDLVEEAKLLVAGGAREITLLGQNVNAWAGEDDKGRPIGLDGLARALAAEPDLKRIRYTTSHPNDMTDGLIAAHGELEKLMPFLHLPVQAGNDRVLKAMNRSHTADSYMALLERIRAARPDIALSGDFIVGFPGETD... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
Q30YS1 | MHERTFHIMTFGCQMNVNDSDWLARALEARGFTQVPEHEAAIYIINTCSVRDKPEQKVYSLLGRIRRETKNRRNVTVCVGGCVAQQIGKGFFKRFSQVRLVFGTDGAASAPQAIERLVQEPHARISLLDFSEEFPERDAGWENGEVPVSAYVNIMQGCNNFCAYCIVPYTRGRQKSRSSAAVLDECRTLVGNGAREITLLGQNVNSYGLDPHGDGTTFARLLHDVAAIPGLERLRFMTPHPKDIAGEVIEAFGALKNLCPRVHLPLQSGSDRVLKAMGRKYDMARYMDIVTRLKAVRPDIQITSDLIVGFPGETEADFEQ... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
B1ZVI7 | MNRVHIKTYGCQMNERDSEAVAAMLRARGYRIVADENDCDILLLNTCSVRDAAEQKAIGKAGYLQQRKKKQPDFVLGILGCMAQNRGASLLDQLPDVDLIVGTQKFHQVPGYLDNLRAARDAGVPIGETIVDIGEEAGSQNTIKDHLLPQDSDSDSQPSTLNSQLRGAAAPPPQITAFVSIQQGCNMDCAFCIVPKTRGDERSRPMDDIVRECEQLAARGVREVTLLGQIVTSYGRRDYTHTNGISPFVQLLERVHALDGIERIRFTSPHPRGFKDDLVAAYGRLPKLCGYVHLPLQSGSNRILRAMNRPYTRERYREIV... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
B3CV38 | MNKMLYIKTYGCQMNVYDSNRMVDLLETQGYNIVANMADASVIILNTCHIREKASEKMYSELGRIKKLQQSRLKAGKSKAKIIVAGCVGQAEGEEIFIREPAVNIIVGPQSYYNLPTMLEKLDSGTENHLIDLDFVEAAKFNKLPEVLKSPTVSGLVSVQEGCDKFCTFCVVPYTRGAEFSRPLEQVYREVLNIAQQGAKEVVLVGQNVSAYHGKDENGKECSLADLIKYVAKIDKIKRIRYITSHPNDMTDQLLSLHATEEKLMPFLHLPVQSGSNKILKLMNRRHSRERYLEIIQQLRELRPDIVISSDIIVGFPGED... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
Q0AYB7 | MGDKEKKPLKYRILTYGCQMNVRDSETIAGLLEGSGFNQAEDLSEADLIVFNTCSVRHSAENKVYGKLGEIASLKKKRPELLIAFGGCMAQLPEVRQKLKKRGVDVVFGTHNIHELPYLIARAKEKRSPVFEVWEKEGSIVEPLPSCRKPGLSAFVNIMFGCNNFCSYCIVPYTRGRERSRKADDIIRELEELAAAGYKEVTLLGQNVNSYGRGLGEKIEFADLLYRANSVAGIERIRFTTSHPKDVSDRLLQAIAECEKLCEHIHAPLQAGSNRILQRMNRNYSREHYLKLVERMRHYVPGVSITSDLIVGFPGETEED... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
Q9WZC1 | MRFYIKTFGCQMNENDSEAMAGLLVKEGFTPASSPEEADVVIINTCAVRRKSEEKAYSELGQVLKLKKKKKIVVGVAGCVAEKEREKFLEKGADFVLGTRAVPRVTEAVKKALEGEKVALFEDHLDEYTHELPRIRTSRHHAWVTIIHGCDRFCTYCIVPYTRGRERSRPMADILEEVKKLAEQGYREVTFLGQNVDAYGKDLKDGSSLAKLLEEASKIEGIERIWFLTSYPTDFSDELIEVIAKNPKVAKSVHLPVQSGSNRILKLMNRRYTKEEYLALLEKIRSKVPEVAISSDIIVGFPTETEEDFMETVDLVEKAQ... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
B5YKW2 | MKGRAVYIKTFGCQMNEHDSERMLGILGTKGFIEVDEPKKADIVIFNTCAIRHKAEQKFFSSLGRVKHLKKKNPQLKIIVAGCSAQLQGEKLLNKLPYIDYIIGPDNLHVIENIIENQVSHRIFTDENPEVANINLPVKRKDCVKAWVNIIYGCNNYCTYCVVPYTRGKERSRPVDDIIKEISLLAEQGYKEVTLLGQNVNSYKDGNTNFPLLLEKVEKIEGIKRIRFITSHPKDLSKELVDVMKDYKKICEHIHLPLQAGSNKILKLMNRKYTYEEYFEKICWLREAIPDIAITSDIIVGFPQEQHEDFEKTINALKEI... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
Q73MD3 | MTYFFETYGCQMNQAESSSMEQILLEKGWTNSSDAEHCDLLIINTCSVRITAENRVLGRLGHFSGLKKKRKFFVLLIGCMAERLYTEIQKEFPLIDYVVGMFERNLLPQIFDEIKARLKNDNYMAEFTHDNIEEKPVSGYYFAPLSHSPKSFQSYVPIMNGCNNFCTYCIVPYVRGREVSRPVNEILQEITELSSRGVREITLLGQNVNSYKGEDGEGRLIDFPKLLTLIAREADKTDMIRWIRFMSSHPKDMSDALIDTIAAEKRLCKLVHLPVQHGSDTILKRMNRVYTIEHYKNRIKRLKETIPDIALSTDILMGFP... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
O83735 | MTYFFETYGCQMNVAESASVEQLLLARGWTKAVDAQTCDVLIINTCSVRITAETRVFGRLGLFSSLKKKRAFFIILMGCMAQRLHDKIQQQFPRIDYVVGTFAHARFESIFQEIEQKLTQKDYRFEFISERYREHPVSGYRFFASSYSEGSFQSFIPIMNGCNNFCSFCIVPYVRGREISRDLDAILQEVDVLSEKGVREITLLGQNVNSYRGRDREGNIVTFPQLLRHLVRRCEVKDQIKWIRFVSSHPKDLSDDLIATIAQESRLCRLVHLPVQHGANGVLKRMRRSYTREQYLSLVGKLKASVPNVALSTDILIGFP... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
B3E424 | MNHKKLYIDTVGCQMNVNDSERIVTMLQPLGYTQTSRRHEAALILFNTCTVRAGAEECLLQNIANLKNLKRKKPGTLIGVAGCVAQQMGAELLQKFPWVDLVFGTHNLHLVPEMVKDAEAGRRRAETDFLDSSERLDLFPPIEGRKRVSAFVTVMQGCDNFCSYCIVPYVRGREISRRFAEILQEVQDLAAQGLREVVLLGQNVNSYGLKGEEQPSFAELVRAVAAVSGIDRVRFVTSHPKDMSDDLIACFADLAKLCGSLHLPAQAGNNRILKAMNRGYSREHYLETIYKLRQARPEIKITGDMIVGFPGETEAEFEET... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
Q8YT18 | MNLFKPRILVLFAATALISGIAIVAQTSVADSGDKITATSSLKTPIVNRAITESEVLAAQKAWGEALVAISTTYDAKGKASAKALAEKVIDDAYGYQFGPVLFKPTLAISPRTFRTTRAGALAYFVGDDKAFPEDKGFALSSWRKVEIKNAAIFITGNTATTMGNVIITDKQGKATTVDKTWQFLKDDHGKLRIITHHSSLPYEQ | Cofactor: Does not require a metal cofactor.
Function: Catalyzes the hydration of carbon dioxide (CO2) to bicarbonate (HCO3(-)) . Has only very low bicarbonate dehydration activity . May function even in metal-poor environments .
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 22111
Sequenc... |
Q09T02 | MNDILETETPVMVSPRWDMLLDAGEDTSPSVQTQIDAEFRRVVSPYMSSSGWLCTLTIECGTIICACR | Function: Lanthionine-containing peptide antibiotic (lantibiotic) active against S.michiganensis subspecies sepedonicus strain 2136 (MIC=30 pmol/ml). The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane por... |
Q5B7T4 | MVGSVVEAHRQSVGCLRNLSQLLAWASNTSGGLIFYSREDDVLTSTRISYAELLADAGEKARLIGQITGLSSESIILLHFDTQREVIEWFWAATLAGYLPAISTPFVDDTARRKAHLLHLHAQLNQPVVLTSKRLVPEFLGLEELRLHDVESLLSSAAKDGLIQYLGVQKLAEDVAVLMLTSGSTGSAKAVPLRHGQLLTAIQGKSTHHGTLPGDVFYNWVGLDHVASLTEIHLHALILGSDQVHTAASELLRNSLQFVRLLDTHKVAYTFAPNFFLTKVLDSLRENPTFTADLSSLKALISGGESNVVVTCDKLTRELR... | Function: Microperfuranone synthase is the only protein required for the biosynthesis of the secondary metabolite microperfuranone from phenylpyruvic acid (PPA) . Several steps for the microperfuranione biosynthesis have been proposed . These steps include the activation of PPA, by the micA adenylation (A) domain to AM... |
Q29983 | MGLGPVFLLLAGIFPFAPPGAAAEPHSLRYNLTVLSWDGSVQSGFLTEVHLDGQPFLRCDRQKCRAKPQGQWAEDVLGNKTWDRETRDLTGNGKDLRMTLAHIKDQKEGLHSLQEIRVCEIHEDNSTRSSQHFYYDGELFLSQNLETKEWTMPQSSRAQTLAMNVRNFLKEDAMKTKTHYHAMHADCLQELRRYLKSGVVLRRTVPPMVNVTRSEASEGNITVTCRASGFYPWNITLSWRQDGVSLSHDTQQWGDVLPDGNGTYQTWVATRICQGEEQRFTCYMEHSGNHSTHPVPSGKVLVLQSHWQTFHVSAVAAAAI... | Function: Seems to have no role in antigen presentation. Acts as a stress-induced self-antigen that is recognized by gamma delta T-cells. Ligand for the KLRK1/NKG2D receptor. Binding to KLRK1 leads to cell lysis.
PTM: N-glycosylated. Glycosylation is not essential for interaction with KLRK1/NKG2D but enhances complex f... |
Q22638 | MMVSPPQEDTVFNTDSDPVYEQATDDMTFNDTTTDGNGQESVPLEALTVVEIEKTSKGFGFNIVGGTDNPHFVGDIGIYVSSVNSESKSYGVVRTGDKILSFDGIDMTYKTHDEAVEVFRSVKIGHVAKMLIDREYLHLQEDRTQTPTASVSITPQVTPQTRSTQNNTDTPKSMSHSESKSRLTSHGLSAVIERIRGKVYEEEDAQSVTSYAPSTHSIIDDVPRTPRKPLSLLDPRNNSWLTEALYVSIGLGALTISGYLAYRFIRGRR | Function: Plays a role in the regulation of lifespan in a partially daf-16-mediated manner, and may be involved in regulating the levels of reactive oxygen species production in response to heat stress.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 29730
Sequence Length: 269
Subcellular Location: ... |
Q95PZ2 | MLHCSFLRVIPIKNASKRLIIVRSLTSAPAKTSEAEKQQDSLKNIDAGEKYTALGNIRQKKDVFHYTDRASGVGYSHYSSSVYQHRPYIWPPLRKLYHWNYALVIAGMVILMSDFEWLKDQIKSASLPFRPEASQKEEVTESNGEVEEVKEKPKKKKLGFRERRIIEYEDRLRLYSTPDKIFRYFATLKIIDPNEDSGRFEVFMTPEDFLRSFTPGVMQPRRWGLDSFKNYNPEKHKRHKFSDPDSIFYKLGENGLINFSDYLFLMTLLSTSHADFALAFKIFDVDGNGALDKEEFTKVQQLIMSQTTVGQRHRDHITPN... | Function: Key regulator of mitochondrial calcium uniporter (MCU). Modulates the activity of the mitochondrial calcium uniporter protein mcu-1 depending on the level of intracellular calcium in PLM touch receptor neurons following axonal injury .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 62120
... |
P0AEZ5 | MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFVNVIQGDATLNQALIKDKRTENLYILPASQTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDRILGILASKSRRAENGEEPIKEHLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRASNQGEPVILDINADAGKAYADTVERLLGEERPFRFIEEEKKGFLKRLFGG | Function: ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they matu... |
O25098 | MAIVVTITSGKGGVGKSTTTANLAIGLAESGKKVVAVDFDIGLRNLDMILGLENRIVYDVVDVMEKNCNLSQALITDKKTKNLSFLAASQSKDKNILDKEKVAILINALRADFDYILIDSPAGIESGFEHAILHADMALVVVTPEVSSLRDSDRVVGIIDAKSNRAKKGMEVHKHLIINRLKPELVANGEMISIEEVLKILCLPLIGIIPEDHHIISATNKGEPVIRTDCESAKAYQRITRRILGEEVEYVEFKAKRGFFSALKGIFS | Function: ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they matu... |
Q7DDS7 | MAKIIVVTSGKGGVGKTTTSASIATGLALRGYKTAVIDFDVGLRNLDLIMGCERRVVYDLINVIQGEATLNQALIKDKNCENLFILPASQTRDKDALTREGVEKVMQELSGKKMGFEYIICDSPAGIEQGALMALYFADEAIVTTNPEVSSVRDSDRILGILQSKSHKAEQGGSVKEHLLITRYSPERVAKGEMLSVQDICDILHIPLLGVIPESQNVLQASNSGEPVIHQDSVAASEAYKDVIARLLGENREMRFLEAEKKSFFKRLFGG | Function: ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they matu... |
Q55900 | MNRIIVVTSGKGGVGKTTTTANLGAALARLGKKVVLIDADFGLRNLDLLLGLEQRIVYTAIDVLADECTIDKALVKDKRLPNLVLLPAAQNRSKDAINAEQMQSLVEQLKDKFDYIIIDCPAGIEAGFRNAVAPAQEAIIVTTPEMSAVRDADRVIGLLEAEDIGKISLIVNRLRPEMVQLNQMISVEDILDLLAVPLIGILPDDQKIIISTNKGEPLVMEEKLSVPGLAFQNIARRLEGQDIPFLDFMAAHNTLLNRIRRRLLGG | Function: ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they matu... |
Q9X2I3 | MGNVIVVTSGKGGVGKTTITANLGCALAKLGEKVCLIDADIGLKNLDIVLGLENRIVYTMIDVVNGKVSPQEALVKHKMLKNLYLLPASQIATKEMISPNDMKAIVKELIPHFDYIIIDSPAGIERGFRNAVAPAERVLVVTTPELPAISDADRVIGLLENFGFSDEKINVIINRFKPHMVKKGEMLTTDDIKHTLSLEIIAVIPDSEDIIVASNTGIPVSLNGNSRISKNFENLARRIRGEGVPLENDFVTVSKGLIDTLKDFFSKLKRG | Function: ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they matu... |
Q8L799 | MTILIDRHSDQNDAGDEIVEKNQGNGKEEETELVLDAGFEAPHTNSFGRTFRDYDAESERRRGVEEFYRVNHIGQTVDFVRKMREEYEKLNRTEMSIWECCELLNEFIDESDPDLDEPQIEHLLQTAEAIRKDYPDEDWLHLTGLIHDLGKVLLHSSFGELPQWAVVGDTFPVGCAFDESIVHHKYFKENPDYDNPSYNSKYGIYTEGCGLDNVLMSWGHDDYMYLVAKENQTTLPSAGLFIIRYHSFYALHKSEAYKHLMNNEDRENMKWLKVFNKYDLYSKSKVRVNVEEVKPYYLSLTNKYFPSKLKW | Cofactor: Binds 2 iron ions per subunit.
Function: Catalyzes the oxygenative cleavage of myo-inositol to D-glucuronate. Involved in the biosynthesis of UDP-glucuronic acid (UDP-GlcA), providing nucleotide sugars for cell-wall polymers. May be also involved in plant ascorbate biosynthesis.
Catalytic Activity: myo-inosit... |
O82200 | MTILVEHFVPDSRVDEKKVIEERDNELVLDGGFVVPKSKETDAFDAPDMNFLGHSFRDYENGESERQQGVEEFYRMQHIHQTYDFVKKMRKEYGKLNKMEMSIWECCELLNNVVDESDPDLDEPQIQHLLQTAEAIRRDYPDEDWLHLTALIHDLGKVLLLPEFGGLPQWAVVGDTFPVGCTFDSANIHHKYFKGNHDINNPKYNTKNGVYTEGCGLDNVLMSWGHDDYMYLVAKKNGTTLPHAGLFIIRYHSFYPLHKAGAYTHLMNDEDRDDLKWLHVFNKYDLYSKSKVLVDVEQVKPYYISLINKYFPAKLKW | Cofactor: Binds 2 iron ions per subunit.
Function: Involved in the biosynthesis of UDP-glucuronic acid (UDP-GlcA), providing nucleotide sugars for cell-wall polymers. May be also involved in plant ascorbate biosynthesis.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
Sequence Mass (Da): 37048
Sequen... |
Q8H1S0 | MTISVEKPIFEEVSAFEKSGDNIGELKLDGGFSMPKMDTNDDEAFLAPEMNAFGRQFRDYDVESERQKGVEEFYRLQHINQTVDFVKKMRAEYGKLDKMVMSIWECCELLNEVVDESDPDLDEPQIQHLLQSAEAIRKDYPNEDWLHLTALIHDLGKVITLPQFGGLPQWAVVGDTFPVGCAFDESNVHHKYFVENPDFHNETYNTKNGIYSEGCGLNNVMMSWGHDDYMYLVAKENGSTLPSAGQFIIRYHSFYPLHTAGEYTHLMNEEDKENLKWLHVFNKYDLYSKSKVHVDVEKVKPYYMSLIKKYFPENLRW | Cofactor: Binds 2 iron ions per subunit.
Function: Catalyzes the oxygenative cleavage of myo-inositol to D-glucuronate. Involved in the biosynthesis of UDP-glucuronic acid (UDP-GlcA), providing nucleotide sugars for cell-wall polymers. May be also involved in plant ascorbate biosynthesis.
Catalytic Activity: myo-inosit... |
Q9FJU4 | MNISVENPVFVHEDSTTQKTGELRLDSDIPMSKISSDDEVFLAPEMNAFGRQFRDYTDTNSERQKSVEHFYATQHTNQTLDFVQKMRSEYGKLDKMVMNIWECCELSKEVVDESDPDLDEPQIQHLLQSAEAIRKDYPNEDWLHLTALIHDLGKVLTLPQFGGLPQWAVVGDTFPVGCAFDESNVHHKYFMENPDFNNPKYNTKAGIYSEGCGLENVLMSWGHDDYMYLVAKENGSTLPSPGLFIIRYHSFYPLHKAGAYTHLMNEEDKENLKWLHVFNKYDLYSKSKVHVNVEKVKPYYMSLIKKYFPENLRW | Cofactor: Binds 2 iron ions per subunit.
Function: Involved in the biosynthesis of UDP-glucuronic acid (UDP-GlcA), providing nucleotide sugars for cell-wall polymers. May be also involved in plant ascorbate biosynthesis.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
Sequence Mass (Da): 36544
Sequen... |
Q4V8T0 | MGPDPSLAYRPECHEKDKTEFRNFENGDLFDRVFNTYKLMHTHQTLDFVKQKHQVWSNCSHFSLSMMDSIDSLDELVDESDPDVDFPNSFHAFQTAEGIRREHPDKDWFQLVGLIHDVGKVMALYSEPQWAVVGDTYPVGCKFQNSIVFRNSTFEGNPDGKNPAPNTEFGIYEPQCGLDKVLMSWGHDEYLYRVMKFNKCTIPEEGLYMIRFHSFYPWHSNGDYMHLCNEKDQQMLPWVKEFNKFDLYTKSTELPDVERLKPYYQSLIDKYCPGVLQW | Cofactor: Binds 2 iron ions per subunit.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
Sequence Mass (Da): 32735
Sequence Length: 278
Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.13.99.1
|
Q54GH4 | MIETRTTTSTSEIKHDNSLKTGFEITKEVEEFRNYENSEDRVSEAYRNSHTYQTYDYATEKKKQYSQLDTSIKMGLWEAAELLNTIIDESDPDSNIPQINHCLQTAEAIRKVYPDSKYDWFHLTGFIHDLGKVLLSKKFKEQPQWATVGDTFPLGCKFDESNIFYEFFKMNPDYNDSKYNSECGIYKKNIGLENVTMSWGHDEYFYLVCVGNKCLLPKESLYMIRFHSFYPWHRHNKYTHLTNEEDEKMLNWVKEFNKFDLYSKDSEPVDVESLKPYYQSLISKYFPNELHW | Cofactor: Binds 2 iron ions per subunit.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
Sequence Mass (Da): 34801
Sequence Length: 292
Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.13.99.1
|
Q9UGB7 | MKVTVGPDPSLVYRPDVDPEVAKDKASFRNYTSGPLLDRVFTTYKLMHTHQTVDFVRSKHAQFGGFSYKKMTVMEAVDLLDGLVDESDPDVDFPNSFHAFQTAEGIRKAHPDKDWFHLVGLLHDLGKVLALFGEPQWAVVGDTFPVGCRPQASVVFCDSTFQDNPDLQDPRYSTELGMYQPHCGLDRVLMSWGHDEYMYQVMKFNKFSLPPEAFYMIRFHSFYPWHTGRDYQQLCSQQDLAMLPWVREFNKFDLYTKCPDLPDVDKLRPYYQGLIDKYCPGILSW | Cofactor: Binds 2 iron ions per subunit.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
Sequence Mass (Da): 33010
Sequence Length: 285
Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.13.99.1
|
Q9QXN5 | MKVDVGPDPSLVYRPDVDPEMAKSKDSFRNYTSGPLLDRVFTTYKLMHTHQTVDFVSRKRIQYGSFSYKKMTIMEAVGMLDDLVDESDPDVDFPNSFHAFQTAEGIRKAHPDKDWFHLVGLLHDLGKIMALWGEPQWAVVGDTFPVGCRPQASVVFCDSTFQDNPDLQDPRYSTELGMYQPHCGLENVLMSWGHDEYLYQMMKFNKFSLPSEAFYMIRFHSFYPWHTGGDYRQLCSQQDLDMLPWVQEFNKFDLYTKCPDLPDVESLRPYYQGLIDKYCPGTLSW | Cofactor: Binds 2 iron ions per subunit.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
Sequence Mass (Da): 33164
Sequence Length: 285
Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.13.99.1
|
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