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Q9PBZ3 | MNTPTHTHPHPFGSTATIRCERAAAELRTGRPVLLIDAHTRRHAVMALDSMTAQSFTTFANAVGNTHYLFLTPARSNVLGLEAPQGARIPLATLSYDSLVKLAYLRQPTHPTTWVPGDIMDAAATEITRLALLLPAIVAAPLTHHTEHAFADCQTLDLTDLDTAAAGASTTEYELVTRTPVPLRDLGMSEFIVFRGGIAQRDQVAILIGQPDLSSAVPVRVHSSCLTGDLFGSLKCDCGDQLRHGLATLKALGGGVLLYLDQEGRGNGIAAKIRAYGYQHVGLDTIDADAQLGFGPDERRYTGAVMMLRALGITRIQLLSNNPTKVERLRAAGIIVEQRIPVIGQITEQNEYYLRTKVSRAGHDLDIDALIMTSQRPQDPSETVDGETVKSIPKTGHA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Catalytic Activity: GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H(+) + 2 phosphate
Sequence Mass (Da): 42975
Sequence Length: 398
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.
EC: 3.5.4.25
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Q8ZEF0 | MQLKRVAEAKLPTPWGDFLMVGFEELATGHDHLALIFGDISGDKPVLSRVHSECLTGDALFSLRCDCGFQLEVALTRIAEEGRGVLIYHRQEGRNIGLLNKIRAYALQDLGADTVEANHQLGFAADERDFTLCSDMYKLLGIKAVRLLTNNPKKVEILTQAGINIVERVPLIVGENPKNEHYLATKAAKMGHLLTK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Catalytic Activity: GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H(+) + 2 phosphate
Sequence Mass (Da): 21677
Sequence Length: 196
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.
EC: 3.5.4.25
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O66679 | MSEREEFKFNTVEEAIEDIRQGKMVIVVDDPDRENEGDLVMAAEKVTPEAINFMAKYGRGLICLSLTPERCEQLDLHPMTPMNTDPKGTYFCVSIDAHPKHGTTTGISAYDRALTIKLAISPDAKPSDFVRPGHVFPLKARPGGVLERAGHTEASVDLARLAGLYPAGVICEIMKDDGTMARVPDLMEFAKKHNLKIITIADLIKYRLRRETLVEKVASAHLPTPWGVFKIHAYRHKLTGEEQVALTMGEWKEDEPVLVRVHSECLTGDVFRSFRCDCRPQLEKALEMIAKEGKGVLVYILGHEGRGIGIANKIKAYELQEKGYDTVEANEKLGYPPDLRDYGIGAQILRDLGVRKMKLMTNNPRKIVALEGFGLEVVERVPIKIEPNPYNKIYLQVKKDKLGHMF | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)
Sequence Mass (Da): 45577
Sequence Length: 406
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
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Q8EKF2 | MNQSLLAPFGTAIERVEAGLNALRQGLGVLVVDDEDRENEGDLIFAAESLTNAQMAMLIRECSGIVCLCLPDEKVKALALPPMVENNSSQYGTAFTVSIEAKVGVTTGVSAADRVTTIKTAIADHAKPSDLARPGHVYPLRAQPGGVLTRRGHTEGTIDLMQLAGLKPAGVLCEVTNPDGTMARLPEIIAFGALHNMPVLTIEDIVVYRKSLLANVG | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)
Sequence Mass (Da): 22956
Sequence Length: 217
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
EC: 4.1.99.12
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A8GYS3 | MNQSLLAPYGNPIERVNAALSALRQGKGVLVVDDEDRENEGDLIYSAETLTNQQMALLIRECSGIVCLCLTDERIKQLQLPPMVSDNNSQYGTAFTVSIEAKQGVTTGVSAADRVTTIKAAIADDAKPDDLARPGHVYPLRARPGGVLERRGHTEGTVDLMKLAGLQPFGVLCEVTLPDGTMARLPEIVEFAQQHDMPVLTIEDIVAYRNTQ | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)
Sequence Mass (Da): 23015
Sequence Length: 212
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
EC: 4.1.99.12
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Q979C2 | MIRVMATGVFDILHLGHIHYLKESKKLGDELVVVVARDSTARNNGKIPIFDENSRLALISELKVVDRAILGHEGDMMKTVIEVKPDIITLGYDQKFDEAELQSKINKLGITVKIVRISKYDGQLNSSSSVRKKIMELIGERY | Function: Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme.
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Mass (Da): 16009
Sequence Length: 142
Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
EC: 2.7.7.2
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K4REQ6 | MNWLNSEAFVLFDQHIIWSDMVGNILGLITLALGFRRSLWTWPVQFLSGLVLFGAFYGHLTGSAGKQAVVMAVALYGWYQWNRGTDKAADGKVSVRFATWAERGAMIAAAAVGTVAVALLFKAYPSLSWDPWPDAYIFVGTIVAMYAQARGMVEFWFAWLLVDLVGVPLNFANGYAFSGFVYVIYGALVLWGMRDWWLRSRRDSRPVLEGAPA | Function: Transports riboflavin and roseoflavin . Can also transport FMN and FAD . May confer roseoflavin resistance to S.davawensis, which naturally produces this antibiotic during stationary growth phase .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23749
Sequence Length: 213
Subcellular Location: Cell membrane
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A6WUW2 | MVAACSAYAAVNVATQWAGTRTGIPSVIIAFWQYVIALVLTLPLLVRDGTRALRTSHFGLHVMRVALAAAGVQVWIYALTHVPIWQVVALSMTSPFFVILCARLFLQEKVTPARLLTTFTGFIGALIIIAPWSDSYTVYSLLPILAAALWAGYSVMTKYLTRFEKPASISAYMLVLLTPINAALWLASGLSMSAITAPDVEIWSILIVIGAFTALAQYFQTAAYSIADAVYLQPFDDLRLPINVIFGWIVFAAAPSINFWPGAALIIGASLYLMRQDSGTSRTA | Function: Transports riboflavin into the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30844
Sequence Length: 284
Subcellular Location: Cell membrane
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Q1MIM3 | MKDMNQTSLAVEPSRAVVGALWMVLAGIAFSLLNVVTQWLTMKLAFPSASAAFWQYGFAFLFSLPFLKRLGLAAMRTHYPWRHLTRVVLAALGVEAWVAGLAAVPIWQAIALVMTSPFFIILGARLFLGERVGPARWAATAAGFTGAMIILQPWSDGIGWAALLPVLSALLWGASSLITKSLTGIERPETITVWLLVLLTPINGGLALAAGFAVPTGATLALFLLAGLLTAVAQYFLTLAYAAADAAYVQPFDDLKLPLNVLAGWLFFGYAPAGYLWLGAALILSASLFIMRNEMRRERKPA | Function: Transports riboflavin into the cell. Can also transport FMN and FAD. Required for normal nodule development during colonization of pea plant roots.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32511
Sequence Length: 302
Subcellular Location: Cell membrane
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Q9KKU0 | MSIKHHPLQGALWMLTAGLAFAIVNSVAQYASIQFGLPSTTVALVQYAIAIVVILPYLKTLGIRQSLRTQQFGWHLLRVFLAVIGIQLWLWALAYPVPIWQGIALLMTSPLFATIGSGLWLREKVGMARWVATLTGFIGAMIILEPWADDFNLASLLPVGAAFFWASYSLMVKKLSSHDSPSTMVVYLLLLITPFNLLLALPDWQMPNGQTVWLLLIGAGVMTALAQWAIAKAYAVADASFVQPFDHAKLPLNVLAGWLVFGWVPPGRLWLGAAIIVLSVAFITQWETKKSRRERNIA | Function: Transports riboflavin into the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32891
Sequence Length: 298
Subcellular Location: Cell membrane
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Q9STY4 | MALSFRISSSSPLICRATLSNGDNSRNYHTTDAAFIRRAADLSEMSAGLTSPHPNFGCVIATSSGKVAGEGYLYAQGTKPAEALAVEAAGEFSRGATAYLNMEPGDCHGDHTAVSALVQAGIERVVVGIRHPLQHLRGSAIRELRSHGIEVNVLGEDFESKVLEDARKSCLLVNAPLIHRACSRVPFSVLKYAMTLDGKIAASSGHAAWISSKLSRTRVFELRGGSDAVIVGGNTVRQDDPRLTARHGQGHTPTRIVMTQSLDLPEKANLWDVSEVSTIVVTQRGARKSFQKLLASKGVEVVEFDMLNPREVMEYFHLRGYLSILWECGGTLAASAISSSVIHKVVAFVAPKIIGGSKAPSPVGDLGMVEMTQALNLIDVCYEQVGPDMLVSGFLQPIPDLLPVIPSEDATVEIDPSVDPFEPSIIFFYKTWDLYGMWNITIRYHTTVHVKWYLALSKKHNLLILHPKTLKANKFVGVENPKAYDCVEKIRTARSPEEAALIGRSTLRQKPELVRNDWEDVKIEVMYKALKCKFSTYPHLKSMLLSTIGTVLVEASPHDLFWGGGREGEGLNYLGRLLMQLRSEYLGESSVSAEKTSSA | Function: Pyrimidine reductase involved in the riboflavin biosynthesis pathway. Has also a non-functional N-terminal deaminase domain that lacks the catalytically essential zinc-binding residues.
Catalytic Activity: 5-amino-6-(5-phospho-D-ribitylamino)uracil + NADP(+) = 5-amino-6-(5-phospho-D-ribosylamino)uracil + H(+) + NADPH
Sequence Mass (Da): 65502
Sequence Length: 599
Domain: The C-terminal domain (416-599) is not required for the reductase activity while the non-functional deaminase domain (21-150) is necessary.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 3/4.
Subcellular Location: Plastid
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P94465 | MTIIAGTVVKGKQLGRKLGFPTANVDAKIHGLRNGVYGVLATVNHQFHLGVMNIGVKPTVGSNLEKTLEIFLFDFHRDIYGEKIECSILFKIREERRFDSLESLTKQIKKDISCVAKRFELIGIMAPNKKESLLSHQELNLPDLCFYKKCNNLYGVNRGVYNVIDNWFFEYGITQVAYRRIYILSFLSFLKEDNPKVSSKYIRFGAGGLADKLNRFISSYVEESEENILG | Function: May be directly involved in the regulation of the rib genes. C-terminal part of RibR specifically binds to RFN of the rib leader of the riboflavin biosynthetic operon. The RFN element is a sequence within the rib-leader mRNA reported to serve as a receptor for an FMN-dependent riboswitch. Possibly, RibR produces the comodulator FMN through its own N-terminal flavokinase activity. FMN-activated RibR may stabilize the anti-anti terminator structure of RFN mRNA, causing transcription termination of the rib genes in trans.
Catalytic Activity: ATP + riboflavin = ADP + FMN + H(+)
Sequence Mass (Da): 26229
Sequence Length: 230
EC: 2.7.1.26
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P0CI36 | MSKTRRMVLIAMLAALSTILLLPILQFPLLPGIDFMKVELSIIPVLIGVFTLGLGDGFIILFIRSVLWYLLFNQGPSTWIGVPMNFVALGIFMAIVWFFTKKKFSIKNYTVGIVLATIASVLVMMVLNVFYALPLYRLAAGFDVDKIFAGATHLFNMGSLSVTLNPTYLLTVVLPFNALQYIIFALVFGLIVTVFKKNKVVKFYNA | Function: Mediates riboflavin uptake, may also transport FMN and roseoflavin (By similarity). Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins. Uptake of riboflavin into proteosomes containing EcfA1A2T and RibU has been demonstrated. Uptake requires hydrolyzable Mg-ATP.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22972
Sequence Length: 206
Domain: Riboflavin is stacked with one or more Trp residues in the binding pocket of RibU.
Subcellular Location: Cell membrane
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Q03WN0 | MSIIPVTRVQRTTLIAILSAISFGLMLFPQVPIIPSADFLKLDFSIVPVVIGLYWLNYSASLWVILIRTLLKLILANEGVNTYLGLPVNLLVVLAFITVLKITMPNLEQYSNWQKKILPLISSTFVMTIVAIVINWFVAIPLYARFANFDIAKFIGLKNYFIGMVLPFNLIEGIIWFVVSMIILRAIQPLQRRFHS | Function: Probable riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins and transport it into cells (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22268
Sequence Length: 196
Domain: Riboflavin is stacked with one or more Trp residues in the binding pocket of RibU.
Subcellular Location: Cell membrane
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Q8Y5W0 | MKNYSMKVFVSVAVLGTLAFILMMLQFPLLPSAPFLKLDFSDIPALIGGLLFGPLAVILVELIKNVLLYIVSGSPVGVPVGELANFISGLFYVLPIYYLFHWLRSTKGMVLSTAVGTVLMTGAMAVFNYFVLLPFYIKLGGLPANTDVAWLITYAIVPFNLLKGVIVSAVFLLLYSRLKKWIAKNQTMKERRKFEKRQQEISH | Function: Substrate-binding (S) component of an energy-coupling factor (ECF) ABC-transporter complex (By similarity). Mediates uptake of riboflavin . Can also transport roseoflavin (RoF), and probably 8-demethyl-8-aminoriboflavin (AF), toxic riboflavin analogs . In addition, during intracellular growth, binds and imports FMN and FAD directly from the cytosol of host cells . Essential for virulence and intracellular growth .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22654
Sequence Length: 203
Subcellular Location: Cell membrane
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E5QVT2 | MNGRRKLNMQQNKRLITISMLSAIAFVLTFIKFPIPFLPPYLTLDFSDVPSLLATFTFGPVAGIIVALVKNLLNYLFSMGDPVGPFANFLAGASFLLTAYAIYKNKRSTKSLITGLIIATIVMTIVLSILNYFVLLPLYGMIFNLADIANNLKVIIVSGIIPFNIIKGIVISIVFILLYRRLANFLKRI | Function: Mediates riboflavin uptake, may also transport FMN and roseoflavin. Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21009
Sequence Length: 189
Subcellular Location: Cell membrane
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Q5M614 | MRSLFFGIGKSIGNFFQIVKIWRNFFMTNTRKLAYIAILSAVSFLLLYFSFPLIPAADFLKVDFSILPVLIALVIFDFKSAIGVLLLRSLLKLLLNNGGPGSMIGLPMNFVALGVFVWGLSYFWKKNQTSKNYILGSVLGTILLTVAMVVLNYIYAVPLYAKFANFDIAQFIGLYKYLFAMVVPFNLLEGLIFSVAFALIYAPLKSILVKL | Function: Substrate-binding (S) component of an energy-coupling factor (ECF) ABC-transporter complex. Mediates riboflavin uptake, may also transport FMN and roseoflavin. Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins (Probable). Expression of the complex plus RibU in E.coli allows riboflavin uptake.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23644
Sequence Length: 211
Subcellular Location: Cell membrane
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Q9X1G6 | MSSIKKISFVGIFSALATLVMFLEFPIFPQASFLKYDPSEIPALIVSFLLGPGVGMFVVLVKDILFFLMKSGDPVGIAMNAVLGMSFVGIAGLIYHRNKSRATAIKGMIVATLFATAFALGLNALIVPLYFEAPFELYLKFFPFILAFNLVKFGIDSVVTFFVYKKVSSILKLETVEGRSNNG | Function: Substrate-binding (S) component of an energy-coupling factor (ECF) ABC-transporter complex. Mediates riboflavin uptake, may also transport FMN and roseoflavin. Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins (Probable). Expression of the complex plus RibU in E.coli allows riboflavin uptake; uptake does not occur in the absence of RibU or the EcfA1A2T complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20015
Sequence Length: 183
Subcellular Location: Cell inner membrane
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Q6F0N9 | MDKKYKLWNYKYDFSEINLKNWKEVLKDTFKLNTRKIALLSMLFAIEILMTIISKVIMGLAIPMIVGVYTIEISFFVILIIYLCSNYIYASILSITAIWFRLLLGSEPVGLLSMMISDTAFLTIFAVLFFILKKFIFLKFKFKNQIKILIALICFAGLISMIGSGFISMLCNDKFIFEMYYLSDDGSGYWKMLLWVGFGVTLAKYSINILLFASTLKVLLILIKQSRV | Function: Probably transports riboflavin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26329
Sequence Length: 228
Subcellular Location: Cell membrane
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Q7MGG3 | MHFVSYSLCYDVRSNIMEQPIYFYEPDENHGFLANFYPCSITVSGTCWPSSEHYYQAQKFDDVRLQEKVLRAEDAAQAFRLSREYQQWQRHDWYDIRVEVMRFIVREKFLQNTPLAHQLLATGDTELKEHSHKDAFWGDGGDGHGRNELGRILMMVREELQEHAPYNLVQFIDSAKLPTQWGTFQMYGFIEKATGKEHLALVYGDIEQQAAPLIRLHSECLTGDALFSARCDCGFQLAKALQNIVAEGAGVLLYLRQEGRGIGLINKIRAYHLQDDGADTVEANEQLGFGADMRDYAFCRGILSFLGIERVRLMTNNPRKVKALQLANIEVTERVPLQEGNNPHNHQYLRTKADKLGHMFDRNFVKP | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the hydrolysis of the N-glycosidic bond in the first two intermediates of riboflavin biosynthesis, which are highly reactive metabolites, yielding relatively innocuous products. Thus, can divert a surplus of harmful intermediates into relatively harmless products and pre-empt the damage these intermediates would otherwise do. Has no activity against GTP, nucleoside monophosphates or ADP-ribose.
Catalytic Activity: 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H2O = 2,5,6-triamino-4-hydroxypyrimidine + D-ribose 5-phosphate
Sequence Mass (Da): 42270
Sequence Length: 367
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.
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Q8A947 | MIKNIVFDFGGVIVDIDRDKAVQAFIKLGLADADTRLDKYHQTGIFQELEEGKLSADEFRKQLGDLCGRELTMEETKQAWLGFFNEVDLRKLDYILGLRKSYHVYLLSNTNPFVMSWACSPEFSSEGKPLNDYCDKLYLSYQLGHTKPAPEIFDFMIKDSHVIPSETLFVDDGSSNIHIGKELGFETFQPENGADWRQELTVILNS | Function: Catalyzes the dephosphorylation of D-ribitol-5-phosphate and D-ribitol-1-phosphate. Is also able to dephosphorylate 5-amino-6-(5-phospho-D-ribitylamino)uracil, and thus could be involved in the riboflavin biosynthesis pathway.
Catalytic Activity: D-ribitol 1-phosphate + H2O = phosphate + ribitol
Sequence Mass (Da): 23545
Sequence Length: 206
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 4/4.
EC: 3.1.3.-
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A9WGD1 | MQQTLPVTRVSPRVRSLQRFEWPALGLPVTLMLLLVFWQAGVTLSGYPAFILPSPALVAGRFWQALSSGLLWQHTLATLSAALGGFTLALIIALILGYTLAHIRWLEQALAPVLAASQAIPVVAVAPLIILWFGAGLTSKVLVAALITFLPILINTVVAIRSIPRELIEMAYISGANRWQLLRYVEAPLALPVLFGGVRTGLALATTGAVVGEFVAGRVGLGALINIARGLFDTPLIFVALATLALITLTLYVLAGLLERLLVRWEAS | Function: Part of an ABC transporter complex that transports riboflavin into the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28685
Sequence Length: 268
Subcellular Location: Cell membrane
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P38615 | MNIQSNNSPNLSNNIVSKQVYYAHPPPTIDPNDPVQISFPTTEVVGHGSFGVVFATVIQETNEKVAIKKVLQDKRFKNRELEIMKMLSHINIIDLKYFFYERDSQDEIYLNLILEYMPQSLYQRLRHFVHQRTPMSRLEIKYYMFQLFKSLNYLHHFANVCHRDIKPQNLLVDPETWSLKLCDFGSAKQLKPTEPNVSYICSRYYRAPELIFGATNYTNQIDIWSSGCVMAELLLGQPMFPGESGIDQLVEIIKILGTPSKQEICSMNPNYMEHKFPQIKPIPLSRVFKKEDDQTVEFLADVLKYDPLERFNALQCLCSPYFDELKLDDGKINQITTDLKLLEFDENVELGHLSPDELSSVKKKLYPKSK | Function: Serine/threonine protein kinase that is thought to function in regulating kinetochore activity and entry into meiosis. Could phosphorylate IME1.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 43005
Sequence Length: 370
EC: 2.7.11.1
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Q9VQ37 | MAQNTADTLIHLIAGGSAGTVGAVVTCPLEVVKTRLQSSTAFMTPSRLAENAGGGPANGGQSELLRPEQRRKLSTTILRNRSQPQVIGGVRRIMAISHCGISSTTPKSMSIVQCLRHIVQNEGPRALFKGLGPNLVGVAPSRAIYFCTYSQTKNTLNSLGFVERDSPLVHIMSAASAGFVSSTATNPIWFVKTRMQLDYNSKVQMTVRQCIERVYAQGGVAAFYKGITASYFGICETMVHFVIYEFIKSKLLEQRNQRHTDTKGSRDFLEFMMAGAVSKTIASCIAYPHEVARTRLREEGNKYNSFWQTLHTVWKEEGRAGLYRGLATQLVRQIPNTAIMMATYEAVVYVLTRRFNNKSNEFYDF | Function: Mitochondrial transporter that imports purine and pyrimidine nucleotides into the mitochondria. Essential for maintaining mitochondrial structure and function. Appears to be important for mitochondrial gene transcription and mitochondrial respiration.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40476
Sequence Length: 365
Subcellular Location: Mitochondrion
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O67156 | MMEEYVVIGKVLDTFGLEGELKVRPYAPPEVFENLEKVYLKRKGGDWVPFEVEWVDFIDDKVIIKFKGYDSIDEVEQFKGAKLFLPKEELPELGEEEYYAYELVGMEVETDKGKKLGKVERVQDMGPYDALVLDKENLLVPFVSDIVLKVDKENKKIIVKEELLPV | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19223
Sequence Length: 166
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A0JXU0 | MQLQVARIGKPHGIRGEVTVQVLTDAPEDRFIPGTRFVVEPASAGPLTVDSARWNKDILLLGFEGIETRNQAEALRGAKLFIETEELEEEDDEGWYEHELVGLDVRVGDAVVGTISGLRTLPVQDLIVVESPDGKEILIPFVEEIVPEVNVGEKYILVTPPPGLFEINVEDSGETSDAGESGPGEAEPGKAEAGDNA | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 21210
Sequence Length: 197
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A8IKV0 | MTDRILIARIGAPHGVKGEVRLFAFGEDPLALKRYPLTDESGARRFKVQSLRAAKDHFVARLEGIADRNAAEALTNTDLFVPRDALPAAEDEDTFYHADLMGLRVEDQSGALLGTVLAMHDFGAGDVLEYTPEGGGRTLLLPFTKAAVPVVDVPGGRIVVVPDTNPDETPPEDADQA | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19032
Sequence Length: 177
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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B6YRA4 | MINFNELIKVGNFNKSHGIKGEISFVFTNNFFFKGKNSFLICEMEGIFIPFRVESYRSISNSTVLVKLKNINTIEQTKLLTYQEVFLPKKQSAENTKLNYFSWDHYIGFNIIDEKNREIGSITDIDKSTINTLFIVEKESKEILIPTANEMIVTIDEKRKIIYMKLPVGLL | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19860
Sequence Length: 171
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A1K9L0 | MMVLGRIVAPFGVQGWLKIHPFGDDPAAWRKMTHWWLAEDPDGPESAWVQYKLASCRPHGKGLVALLEGVPDRNAAEAIEGRYVGAPRDAMPAPEKDEYYWGDLVGLDVVNETDETLGRVSGLISTGAHDVLQVEDGETERLIPFVAAYVLDVDLAARRIRVAWQKDW | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 18692
Sequence Length: 168
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A0RHL5 | MTKWFNVGKIVNTHGVKGEIRVVSRTDFPEERYKVGNTLYISNEKGGEPFPVKITSHRQHKTFDLLTFEGYGNVNEVEQFKGSLLKVPEDQLGELAEGEYYYHEIIGCNVVTEEGEALGTIKEVLSPGANDVWVIKRPKGQDLLIPYIDDVVLQVNIENKLVTIHVMEGLL | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19302
Sequence Length: 171
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A7GRH2 | MTKWFNVGKIVNTHGVRGEVRVISRTDFPEERYKVGNTLYIWGEKGTEPLPVKVTSHRQHKTFDLLTFEGYSNVNEVEKFKGSLLKVPEEQLGELAEGEYYYHEVIGCKVVTENGEELGTITEILSPGANDVWVIKRPKGQDLLIPYIDDIVLQVNVEQKQVTIHVMEGLL | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19471
Sequence Length: 171
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q2J6Z8 | MAEEIVVGRIGRPHGIRGEVTIEIRTDVPHRRFVVGAVLGREGGGTALTVSGAHWHSGRLLLHFRGVDDRGAAEALRGVLLTIDADQAGSPLDDADGDGEAVEMWWDRDLVGLRAVTTAGMLLGHVTDIIHSPAGDLLAIGGPDGGEHLVPFVRDIVPTVDPPAGRIVVDPPPGLLDLD | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 18807
Sequence Length: 179
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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B0TX17 | MSQDFVEIAKIGATYKLDGELNLYPLASSIETLLSYGDWYIQLPANSAWQPLKDESVLRRADKLYIKLASVNDVETAKKYVNSLIGVPKEALPKVGNDEAYFTDLIGCTIVNTANDSFGKVIGIIETGANEVLVCKKDSDEYLIPYVKQYIVSEDLDLKKIVVDWEYDY | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 18973
Sequence Length: 169
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A8L5A4 | MGEPVVVGRVGRPHGIRGDVTVDVRTDLPERRFAPGARLVRQVADGPASRPAADAAGAADAVGTAAGPGSAGDSGAARAAGPPVATVLSVVASRWHSGRLLVRFDGVTDRDAAEALRGSFLTIDSDECGPAVDPDDEDDDGELWWDRDLVGLHARTPAGDVLGEVVDVIHSPGGEILAIGRPEGGEYLVPFVREIVPTVDPAAGHIVVDPPPGLLDLD | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 22386
Sequence Length: 218
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q8RGK8 | MELLIAGKVLGSHNLKGEVKVISDLDNIEVLVGNKVILELADSQQKLLTIKKIEHLVANKWIFSFEEIKNKQDTIEIRNANIKVRRDIVGIGEDEYLVSDMIGFKVYDVKGDEYLGEITEIMDTAAHDIYVIESEEFETMIPDVDVFIKNIDFENRKMLVDTIEGMKESKVKK | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19788
Sequence Length: 173
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q74FG4 | MRQDDLKLLGKIVTTHGIRGQLKVASFSGEFDTILSLETVVLKGKDGRMETFPVARATVHHDRVLLSLTPFTNINEVLHLISAVSYAHRDQFPPLEEGEYYWCDLIGLQVVTAAGTVIGRLDSILPTESHDVYVVRGADREYLIPAVEDVVVQVDLEAGTMTVSPPEGLLDL | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 18954
Sequence Length: 172
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A9BD47 | MSRKDSWLTIGKLVGAQGLRGEVKVNPSSDFPERFINPGERWLQKNTEEPSRIELKSGRQLPGKSIYIVSFIGITDRNKAESIVGNKLLVPSDQKPKLKEGEFHLVDLLGLKAKFTQDGSDVGEVIDLTSAGNDLLVIKLVEGKTVLIPFVKEIVPVINLKQGWLLIKPPPGLLEL | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19432
Sequence Length: 176
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A2BYY9 | MINHDEWLIVGLITSPQGINGKIKVKSLSDFEERFTKPGIRWIQKETESPKKLQLISGFQKPGKESFVITFKEIKNRNEAEKLKGYKLLVKVDEIPKLNKNEFHLTELMNLKVKILENNKLKIIGKVVNLENEKNNLLVIKLLTNDKEVLVPFVKEIIPEIDIKNKFLIITPPPGLLEL | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 20646
Sequence Length: 179
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q7V9R4 | MCKKIIWLTIGKIVAPQGLSGKVRINPSSDFPERFIKSGDRWLQYDNEEPQKIQLNSGRQIPGKSIYVVEFQGIDDREKAKALVGKKLLIDSSHRPTLAPGEFHLLDLLGLKVRLKNDHREIGEVTNLTSAGNDLLEVRLLSGKKVLVPFVKEIVPEIKLQEGWLMVCPPPGLFDL | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19773
Sequence Length: 176
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q7V4K0 | MNGDEDWLTVGKVVAAQGMQGELRINPSSDFPERFTLPGQRWLKERNGEPRPIELLTGRQLPGRSLYVVKFAGVNNRNAAEALVGQKLLVPSSDRPSLAEGEFHLLDLVGLEARLQAEGPAIGHVIDLTTAGNDLLEIELLTGRRVLVPFVEAIVPEVQLNQGWLRLTPPPGLLEL | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19282
Sequence Length: 176
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q46IK7 | MFEKDKWMTIGEIVAPQGLRGDLRIKPSSDFPERFTKPGKRWIQKTDELPTEIKLTKGKLIPGKSIYVLSIEGVSTRSSAEEIIGWKLVIPIDSRPMLSKDEYHYHDLIGLEARRGPSKALIGYVTDLIKGGNDLLEIELVEGKKVLVPFVKEIVPEIEIKEKWLLINPPPGLLEL | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19910
Sequence Length: 176
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q9HXQ0 | MPTPADDLVVIGKIVSVYGIRGEVKVYSFTDPLDNLLDYRRWTLRRDGEIRQAELVRGRLHGKVLAAKLKGLDDREEARTFTGYEICIPRSELPSLEEGEYYWHQLEGLKVIDQGRQLLGVIDHLLETGANDVMVVKPCAGSLDDRERLLPYTGQCVLSIDLAAGEMRVDWDADF | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19790
Sequence Length: 175
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A8F3G2 | MSDYVVIGKITKTHGLFGSVKVLPLTNALEVFQKLENVFIKNDAQSNTHRLQIEEIRKAGKGFLIKFSGIDDEERARKIVGLSLAVRVTDLPKPKSPNEYYYYELLNVEVLDQSGNFIGRVEDIIQTGSNEVAVVKNGSFEMLIPVIHDYIIKFEKRKRLVVKVPEWI | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19149
Sequence Length: 168
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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B2V7T6 | MKKDLIAIGKIHGTHGVKGNLKFEIFVKNFYLPEEIYIKDEENELQPLNIETVDRKKGLIKFKNYDTPEKAKEISHRLIYVPEDLLPKLGEDEFYEFQLIGMDVYYNDKLIGKVEKIDDRLSQAYLIIKCTDEKTRHLPFINEFVKDVNVKENKMQITPPEGWFSL | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19567
Sequence Length: 166
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q67PD9 | MAGQSRPDLIRIGQVTAPHGVRGAVRVYPTTDFPERFVTLKRVMIDGPDRAVGARFRGFVKNLVILELEGITDRNQAERLRGADLLVPREEVHPLPEGYYYDFDIIGIEVVDPDGRQLGRVVEVDHTSPVHDLYVVETAPGKRYLVPAVRRFVKEIDLETGRMVIDPIPGLLED | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19565
Sequence Length: 174
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q2LVU6 | MKFFEIGEIVKSHGLKGRMKAKSYVENGEDLSSVHEAMIVKGKEEPRGYKVRKIVLHKTYFFLELETIDTVESADSLVGSTVLIPEDDRAALSGDEYYWRDLMGLQVVTEEGRFLGRIESIFPTGSNDVYVCAGGSREILLPAISDVILKIDLDKKEMVVRLLPGL | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 18597
Sequence Length: 166
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q3A2E6 | MVLQQSDLLILGVVIGTHGLRGDLKIRGSDQDFPLLSKMHQLVFLREGETVLKCARRKAGWYKGHLLLQIAGYRDVRAVQHLVGCEVAVRRDDVPGLPAGEYYWFQLKGMTAVDRRLGALGCLEDIFTTAAHDIYVINGDYGEVLVPAVKAFIADVDLESNRILFDLPDGLVQET | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19449
Sequence Length: 175
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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A0LMM1 | MSKTVEPACLVPVGKVTRTHGIRGALKIFPYGESLAAQAAGERFFLRSKNGGYCTLTLIGLRAQGRMLVCGFEEIKDVNGAQPFVGEEIFLPEDRLPPVSEGEYYHYRLIGLDIVTLDGESLGVLRKIIETGGNDVYVAEREGREILIPAIEDVIREIDLERKRMVVDLPEGLVDA | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19417
Sequence Length: 176
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q2JUD0 | MVASRDTAWLLVGQVVAAHGLRGWLRVKCWSDFPERLTEPGPRWLQRDSDPEPLLHPLIEGQFFPAKGLYLVRLEGIPDRTAAEAWVGAKVLVPASQRLPLEPEEYHYSDLIGLAVYHQGRLLGHVSAIWAAGQDVLEIATPDKRQVLIPFVKALVPVVDLEKGELQVQPPPGLVESFLGQDRARN | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 20702
Sequence Length: 186
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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B1XKY8 | MAEQDWIIIGQVVAAQGLKGEVRINPSTDFPERFEVPGQRWLQLPNQDPQSVELERGRQIPGKNLFVVKFEHIQDRTQAENIRGAKVLVRAGDRPELEADEYHVSDLIGLEVFDYNTQAKLGIVSDLYTAAQDVLEVTDANQKKHLVPFVKAIVPVVDLVENRLEVDAPPGLFEI | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19677
Sequence Length: 175
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q0IDP0 | MTSTPSPSTADPNSTNDWLPVGTLVGAQGLKGELRLNPASDFPERFTEPGTRWLQAKGSAPKEVELLEGRQLPGKSLYVVRLKGVNNRASAEALVGCTVLVPAKDRPELAEGEFHLLDLVGLEARLAGSDEPIGTVSNLISGGNDLLEIKLNSGKTVLVPFVEAIVPDVQLEEGWLLLTPPPGLLEL | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19879
Sequence Length: 187
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q0AWV6 | MNSDKLVAIGKIAGTYGYAGWLKVIPLTDFPERFYKLDKVILNQGGKLGTFLVDGLKAHNNFYLFKFSGIDTVEVAQGFQNGILQIDESELYPLPEGYFYHFQLQGLSVYDEEKGLLGELTDIIETGANDVYVVDSPQYGEILIPAIKDVILAVKLEEKRMEIKLLPGLIED | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 19253
Sequence Length: 172
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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P74035 | MAEPMTEQQKTENWLEIGTIVAAQGIQGEVRVLSASDFPARFLTKGQRWIRKTPQETPQPLTLKKGKQIPGKNLYILRFTEITDRNQAEALVNYQLLVPATDRLPLEPGEFHVTDLLGLIVYDHDNGDRLGIVTDFYSAGNDLLGITLDKNPDKEVLVPFVEAIVPTVELAEQRLEIKTIPGLLD | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 20716
Sequence Length: 185
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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B7IEQ6 | MINTLRELLSGKVAVAILGKTHGLKGELKLHPFTNFPEIIESLEEIFLYNEKTKQFMVATVENLRLADGYYIIKLNGVENVENARKFVGSKVYINKDELPNLSKDEYYFFEIVGSQVIDESGKVLGVVDEVIQTGSNDVIVVNKNKEDEILIPVIYDYIITLDKENKKIVVKVPEWLD | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Sequence Mass (Da): 20265
Sequence Length: 178
Domain: The PRC barrel domain binds ribosomal protein uS19.
Subcellular Location: Cytoplasm
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Q97I40 | MDKLKFGLVSLGCDKNRVDSEIILGSMNRDYEIVNDPREADVILVNTCGFIESAKQESINTILEMNKYKEKYNCKMLIATGCLTQRYGKELKELVPEIDAILGVNDYKSLDDAIEDFFNLGKKDIYCNYSDQSINEGKRIITTGEYSSYVRISEGCNNSCSYCIIPKIRGKYRSRQFENIIDEVRELSENGTKEVILIAQDTTRYGVDLYGRKRLHELLKEMSLIQGIEWIRIMYCYPEEITEELIEEIASNEKVCNYIDMPIQHISDNILKNMFRKTRKSEILDKVEKIRKKVPNIAIRTSLIVGFPGETEGDFNELCDFVKDANINNLGVFRYSREEGTKAALMPMQIADTVKEKREEDIMLIQQQVSKNLNAKKIGKVYKVIVEGFNGDYWYGRNFEMAPEIDGKVFFKSQSEIKVGSFINIKITENLEYDLIGVVYNEFSK | 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 an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 51336
Sequence Length: 445
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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Q18BJ2 | MLKIALESLGCSKNLVDAEIMMGILNNKGYKLIGDFEEADVIIVNTCGFIESAKQESIDTIINFAELKKTGNLKLLIVTGCLAQRYSEELKTEIPEIDAIVGTGSYQNIDKILKELSEIHQIVSLNDIEFVFNEDLPRYISTPSYMAYLKIGEGCSNNCTYCIIPKLRGKYRSRKFEDIIKEAKKLAESGVKELVVIAQDTTKYGFDLYGKERLSELLEELAKIDGFKWIRVMYSYPESITEELIQVIKKYDNICSYFDMPIQHASNNILKLMNRKTTKEDILNKINLIRSNIPDAILRTTIIVGFPGETEDDFKQLVDFVEEVKFDRLGAFAYSREEDTPADRLPNHIDEEVKIQRRDTLMMIQQKISEELNDKKIGKTYEVLIEEQIEDNVYTGRTQGDAEEIDSIVYVKSVDNLEVGEFVSVQINDAMEYDLMGDVLYELA | 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 an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 50755
Sequence Length: 444
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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A5N854 | MDKLKVGLISLGCDKNRVDSEIILGNVKSAYEIVTDPKLADFIIINTCGFIESAKQESIDTILEMSQYKGKYNCRGIVVTGCLAQRYGIELMELLPEIDIMLGVNDYDKLVENINNFISDKQNKIHNCGYSDLNINEGKRILTTKSHTAYLRIAEGCDNYCTYCIIPKIRGKYRSRSIENILQECNELSLRGVKEVILIAQDTTRYGIDLYNKKMLPELMRSISKIEGIEWIRLLYCYPEEITEDIIDEIALNDKVCNYIDIPLQHISDNILKLMGRRGRKKDILRNINELRKKINDISIRTTIIVGFPGESEEDFKELKNFIENIKFDNLGVFKYSREEGTRAYKMKDQVSEELKTAREGELMMLQKHIIYSMQKYKIGNKYKVLVEGKKEGVWYGRNYAMAPDIDGVIYIKSKKELKVGTMIDVKITNSVEYDLVGVVYDESGK | 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 an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 51338
Sequence Length: 446
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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A1S2T9 | MNKTVETFDPKQTTTLETPAKTLAAEAKASDGTIQGNRIGFVSLGCPKNLVDSERILTQLRIDGYEVTNSYDNADLVIVNTCGFIDAAVEESLDAVREALEENGKVIVTGCLGAKENQIREVHPDVLEITGPHSYEAVLNHVHKYVPKPEHNPFTSLIPQTGVKLTPKHYAYLKISEGCDNRCTFCIIPALRGDLDSRGVGSVLDEAKRLVESGVQEILVVSQDTSAYGKDKDGRTDFWNGMPVKQDITSLARQLGKMGAWVRLHYVYPYPWVDDLIPLMAEGLILPYLDLPLQHASPRVLKMMKRPGRVDRQLDAIKKWREICPDLVIRSTFIVGFPGETEEDFEMLLDFLREARLDRVGCFKYSEVDGAVANTLAELISEEVKEDRYERFMEVQAEISAERLARLVGRELDILIDDVDEEGAIGRSYADAPEIDGMVFINGETELTPGDMVRARIVASDEHDLWAELVALED | 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 an aspartic acid residue of ribosomal protein uS12.
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 52925
Sequence Length: 474
Subcellular Location: Cytoplasm
EC: 2.8.4.4
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A0QVH8 | MMFGIGIVLFALAILVSVALHECGHMWVARATGMKVRRYFVGFGPTLWSTRRANRLGSTEYGIKAIPLGGFCDIAGMTSVDEIAPEDRPYAMYKQKVWKRVAVLFAGPAMNFVIGLVLIYGIAIVWGLPNLHQPTTAIVGETGCVAPQITLEEMGECTGPGPAALAGIQAGDEIVKVGDTEVKDFAGMAAAVRKLDGPTRIEFKRDGRVMDTVVDVTPTQRFTSADASAPSTVGAIGVSAVPVQPPAQYNPITAVPATFAFTGDLAVELGKSLAKIPTKIGALVEAIGGGERDKETPISVVGASIIGGETVDAGLWVAFWFFLAQLNFVLGAINLVPLLPFDGGHIAVATYEKIRNMIRSARGMVAAGPVNYLKLMPATYVVLAVVAGYMLLTVTADLVNPLSIFQ | Function: A probable intramembrane site-2 protease (S2P) that cleaves type-2 transmembrane proteins within their membrane-spanning domains. Degrades PbpB (PBP3, FtsI) under conditions of oxidatives stress; degradation is inhibited by Wag31-PbpB interaction. Also cleaves anti-sigma factors RskA, RslA and RslM. Site-1 proteases have not yet been identified in this organism.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42910
Sequence Length: 406
Subcellular Location: Cell membrane
EC: 3.4.24.-
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P10297 | MKSMLVVTISIWLILAPTSTWAVNTIIYNVGSTTISKYATFLNDLRNEAKDPSLKCYGIPMLPNTNTNPKYVLVELQGSNKKTITLMLRRNNLYVMGYSDPFETNKCRYHIFNDISGTERQDVETTLCPNANSRVSKNINFDSRYPTLESKAGVKSRSQVQLGIQILDSNIGKISGVMSFTEKTEAEFLLVAIQMVSEAARFKYIENQVKTNFNRAFNPNPKVLNLQETWGKISTAIHDAKNGVLPKPLELVDASGAKWIVLRVDEIKPDVALLNYVGGSCQTTYNQNAMFPQLIMSTYYNYMVNLGDLFEGF | Function: Possesses antiviral potency. Inhibits viral infection of plants (tobacco mosaic virus) . Inhibits protein synthesis . Releases both adenine and guanine from Escherichia coli rRNA in vitro. Activity on guanine is 20 times slower than that on adenine .
Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Sequence Mass (Da): 35219
Sequence Length: 313
EC: 3.2.2.22
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Q7M1L7 | VTSITLNLANPTAGQYSSFVDKIRNNVRDP | Function: Exhibits N-glycosylase activity . Catalyzes the release of one adenine from a ribosome . Acts as a ribosome-inactivating protein and inhibits protein synthesis in a rabbit-reticulocyte lysate system and in various cell lines (in vitro) .
Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Sequence Mass (Da): 3292
Sequence Length: 30
EC: 3.2.2.22
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P98185 | VIIYELNLQGTTKAQYSTILKQLRDDIKDPNLXYGXXDYS | Function: Ribosome-inactivating protein of type 1, inhibits protein synthesis in animal cells.
Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Sequence Mass (Da): 4625
Sequence Length: 40
EC: 3.2.2.22
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P56626 | MALSFFFLAISLGSPTAIGDVSFDLSTATKKSYSSFITQLRDALPTQGTVCGIPLLPSTASGSQWFRFFNLTNYNDETVTVAVNVTNVYIVAYRADAVSYFFEDTPAEAFKLIFAGTKTVKLPYSGNYDKLQSVVGKQRDMIELGIPALSSAITNMVYYDYQSTAAALLVLIQCTAEAARYKYIEQQVSSHISSNFYPNQAVISLENKWGALSKQIQIANRTGHGQFENPVELYNPDGTRFSVTNTSAGVVKGNIKLLLYYKASVGSEYDIPTTILHPGAMGMLHNQNGNYVTM | Function: Inhibits protein synthesis by depurinating 28S rRNA in ribosomes.
Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Sequence Mass (Da): 32235
Sequence Length: 294
EC: 3.2.2.22
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P98184 | MRSIGFYSVLALYVGAHVTEDVDINFSLIGATGATYKTFIRNLRTKLTVGTPRVYDIPVLRNAAAGLARFQLVTLTNYNGESVTVALDVVNVYVVAYRAGNTAYFLADASTEANNVLFAGINHVRLPYGGNYDGLETAAGRISRENIELGFSEISSAIGNMFRHNPGTSVPRAFIVIIQTVSEAARFKYIEQRVSENVGTKFKPDPAFLSLQNAWGSLSEQIQIAQTRGGEFARPVELRTVSNTPTFVTNVNSPVVKGIALLLYFRVNVGTDNVFAMSLSTY | Function: Ribosome-inactivating protein of type 1, inhibits protein synthesis in animal cells.
Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Sequence Mass (Da): 30754
Sequence Length: 282
EC: 3.2.2.22
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P24477 | AVKTITLNLVSPSANRYATFLTEIRDNVRXRSLDYSHSGIDVIGAPSSRDSXLNINFQSP | Function: Single-chain ribosome-inactivating protein.
Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Sequence Mass (Da): 6602
Sequence Length: 60
EC: 3.2.2.22
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P04399 | AAKMAKNVDKPLFTATFNVQASSADYATFIAGIRNKLRNPAHFSHNEPVLPPVEPNVPPSRWFHVVLKASPTSAGLTLAIRADNIYLEGFKSSDGTWWELTPGLIPGATYVGFGGTYRDLLGDTDKLTNVALGRQQLEDAVTALHGRTKADKASGPKQQQAREAVTTLLLMVNEATRFQTVSGFVAGLLHPKAVEKKSGKIGNEMKAQVNGWQDLSAALLKTDVKPPPGKSPAKFTPIEKMGVRTAEQAAATLGILLFVEVPGGLTVAKALELFHASGGK | Function: Inhibits the elongation phase of protein synthesis. It inactivates fungal ribosomes even more effectively than mammalian ribosomes and is thought to function as a constitutive antifungal agent in plants.
Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Sequence Mass (Da): 29863
Sequence Length: 280
Subcellular Location: Cytoplasm
EC: 3.2.2.22
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A0QQH5 | MNIRPLRQSVRPSPIFLLVIAVTAAGGALAWIAADTIRPLSYVGVFILVIAGWLMSLCLHEFGHAFTAWRFGDHGVETRGYLTLNPLKYTHPMLSLGLPVLIIALGGIGFPGGAVYLQTHWMTARQKSIVSLAGPAANLVLAVLLLGLTRAFWDPAHAVFWSGIAFLGFLQVTALVLNLLPIPGLDGYGALEPHLNPETQRALAPAKQWGFLIVVVLLITPALNRWFFELVYWFFDFSGVSSYLVSAGGQLTRFWSAWF | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28371
Sequence Length: 259
Subcellular Location: Cell membrane
EC: 3.4.24.-
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D3ZUQ0 | MEEPLGSPPAALSALEKNVAELTVMDVYDIASLVGHEFERVIDQHGCEAIARLMPKVVRVLEILEVLVSRHHVAPELDELRLELDRLRVERMDRIEKERKHQKELELVEDVWRGEAQDLLSQIAQLQEENKQLMTNLNHKDVGFSEEELQKHEGMSERERQVMKRLKEVVDKQRDEIRAKDRELVLKNEDVEALQQQQTRLMKINHDLRHRVTVVEAQGKALIEQKVELEADLQTKEQEMGSLRAELGKLRERLQGEHSQNGEEEEAEIPPQPDGEESISDAEKAALDLKDPNRPRFTLQELRDVLHERNELKSKVFLLQEELAYYKSEEIEEENRIPQPPPITHPRTSPQPESGIKRLFSFFSRDKRRLANTQRPTHIHESFGQWAITHRDDGYTEQGQEALQHL | Function: Plays a role in the regulation of cell shape and polarity (By similarity). Plays a role in cellular protein transport, including protein transport away from primary cilia (By similarity). Neuroprotective protein, which acts by sequestring GAPDH in the cytosol and prevent the apoptotic function of GAPDH in the nucleus . Competes with SIAH1 for binding GAPDH . Does not regulate lysosomal morphology and distribution (By similarity). Binds to RAB10 following LRRK2-mediated RAB10 phosphorylation which leads to inhibition of ciliogenesis (By similarity).
PTM: S-nitrosylation is required for the interaction with GAPDH.
Sequence Mass (Da): 47330
Sequence Length: 406
Subcellular Location: Cytoplasm
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P85101 | RPSWTVDSDSAKYSSFLDSLREEFGRGTPKVCNIPVTKKANNDKFVLVNLVLPFNRNTITLAFRASDAYLVGFQDRDSKTNKLRANFFSDEYRALSGKYKSIFTDAEVLAPALPCASTYTDLQNKAGVSREKLSLGVSSLQTAFTAVYGKVFTGKNVAKFALISIQMVAEAARFKYIEDQVINRGMYSSFEAGARITLLENNWSKISEQYHKSCKLGGGQFTEEEMKLGLLLYN | Function: Ribosome-inactivating protein of type 1, inhibits protein synthesis in animal cells. Inhibits cell-free translation in rabbit reticulocyte lysate system with an IC(50) of 0.17 nM.
Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Sequence Mass (Da): 26132
Sequence Length: 234
EC: 3.2.2.22
|
P84073 | PRGSPRTEYEAARR | Function: Has antifungal activity against F.oxysporum and M.arachidicola. Inhibits cell-free translation in rabbit reticulocyte lysate system. Has some N-glycosidase activity.
Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Sequence Mass (Da): 1646
Sequence Length: 14
EC: 3.2.2.22
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Q2WG80 | MNSVCFATPHTKHMDSKMQLTSSPASLWRPWLVTRKDAQTECRRTKLACPYSRPEVPGNTTTDGKMQSFQHPVRLYWPRSKSFDYLFSDGEALLRNFPVQATINFYDESDSEDEEESCDEDDESDVEDCLKHNSHFTAFN | Function: Plays a role in somitogenesis. Essential for transcriptional repression of the segmental patterning genes, thus terminating the segmentation program in the presomitic mesoderm, and also required for the maintenance of rostrocaudal polarity in somites.
Sequence Mass (Da): 16209
Sequence Length: 140
Domain: The ripply homology domain is required for transcriptional repression.
Subcellular Location: Nucleus
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Q0D2K3 | MDSAACAAAATPVPALALALAPDLAQAPLALPGLLSPSCLLSSGQEVNGSERGTCLWRPWLSSTNDSPRQMRKLVDLAAGGATAAEVTKAESKFHHPVRLFWPKSRSFDYLYSAGEILLQNFPVQATINLYEDSDSEEEEEDEEQEDEEEK | Function: Plays a role in somitogenesis. Essential for transcriptional repression of the segmental patterning genes, thus terminating the segmentation program in the presomitic mesoderm, and also required for the maintenance of rostrocaudal polarity in somites (By similarity).
Sequence Mass (Da): 16379
Sequence Length: 151
Domain: The ripply homology domain is required for transcriptional repression.
Subcellular Location: Nucleus
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Q2WG77 | MDPAASPAAAPPAAPAAAPAADPAADPAAALPGQALAQAPALAQINGQEGARNERAAYLWRPWLSSINDQPRQARSLVDWADNRATAAEAAKTDSDFHHPVRLYWPKSHSFDYLYSAGEILLNNFPVQATINLYEDSDSADNEEDKEEEEEEEEEEDDEEEEEDEDKDVNENEPEVCMGVSEATTHKATAHSPDPHSACPN | Function: Plays a role in somitogenesis. Essential for transcriptional repression of the segmental patterning genes, thus terminating the segmentation program in the presomitic mesoderm, and also required for the maintenance of rostrocaudal polarity in somites (By similarity).
Sequence Mass (Da): 21804
Sequence Length: 201
Domain: The ripply homology domain is required for transcriptional repression.
Subcellular Location: Nucleus
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Q2WG79 | MENITFTSGLNSEMDANQPWRPWLSQTSRKAPDYKPYKRPADDEQHKLSIFKHPVKLFWPKSQCFDYLYEDAEVLLRNYPVQATICLYEDPDTEDEEDYSDEEDEKELR | Function: Plays a role in somitogenesis. Required for somite segregation and establishment of rostrocaudal polarity in somites (By similarity).
Sequence Mass (Da): 13070
Sequence Length: 109
Domain: The ripply homology domain is required for transcriptional repression.
Subcellular Location: Nucleus
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Q5TAB7 | MENAGGAEGTESGAAACAATDGPTRRAGADSGYAGFWRPWVDAGGKKEEETPNHAAEAMPDGPGMTAASGKLYQFRHPVRLFWPKSKCYDYLYQEAEALLKNFPIQATISFYEDSDSEDEIEDLTCEN | Function: Plays a role in somitogenesis. Required for somite segregation and establishment of rostrocaudal polarity in somites (By similarity).
Sequence Mass (Da): 13906
Sequence Length: 128
Domain: The ripply homology domain is required for transcriptional repression.
Subcellular Location: Nucleus
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P69925 | MAYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLISIPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSYYDELIEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGLNKDILCQYVEYITNIRMQAVGLDLPFQTRSNPIPWINTWLVSDNVQVAPQEVEVSSYLVGQIDSEVDTDDLSNFQL | Cofactor: Binds 2 iron ions per subunit.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2 contains the tyrosyl radical required for catalysis.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 43517
Sequence Length: 376
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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P28847 | MSIENSKEAALTAELSLAGAFFYTPECPDIEHLRSLSVANRWLDTDLPISDDLKDVAKLTPAEREFYRFLFAFLSAADDLVNLNLGDLSALFTQKDILHYYIEQESIEVTHSRVYSAIQLMLFGNDAAARARYVASIIGDAAIGRKVAWLQAKVRECGSVAEKYILMILIEGLFFASSFASIAYLRTHNLFVVTCQSNDLISRDEAIHTRASCCIYNNYLGGFEKPEPKRIYELFSEAVNIECEFLLSHAPQYSHLLDIGAIISYVRYSADRLLGEIGLSPLFNAPKPSPSFPLAFMTVEKHTNFFERRSTAYSGTLINDL | Function: Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 36017
Sequence Length: 321
Pathway: Genetic information processing; DNA replication.
Subcellular Location: Host membrane
EC: 1.17.4.1
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Q8SRR2 | MSHGEETELLLDPKEERFVLLPIKYHDIWKMYKKAESSFWTVEEVSLDKDIDDWGKLNAKERHFISYVLAFFAASDGIVNLNLVERFSTEVKVLEARFFYGFQMAIENIHSEMYSLLIDTYIRDNDEKNFLFDAIRTIPSVKEKADWAIRWIEDKNSDFATRLVAFACVEGIFFSGAFASIFWLKKRGLMPGLTFSNELISRDEGLHCEFACLLHYHLKKKCNRIKEVVMDAVEIEKKFLSESLPVNLIGMNCNLMCRYIEFVADRLLENLGEERVYNATNPFDFMENISLVGKTNFFDKRESQYQKAFVGIENGNDSFRIDVDF | Cofactor: Binds 2 iron ions per subunit.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 37987
Sequence Length: 325
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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Q6GZQ8 | MFPHVTIVEKPGCGNCVTLKRALKEKSVPHTVMPYVPGVPGSYPIATVGGQRVGYREITKALAMDMFTTSKCFKPFRYNWAEDIRTKHEKVHWVETEINLRDDVTDWKSGVMTPGEKAFVSCVLRLFTQLDVEVGALYLDHLTQVFRCNEIRNMLTSFACREAIHQKAYSLLNDTLGMPDCEYQAFADYGEMTDKLDFMREMDCSTLPGLARSLLRAVLNEGVSLFAAFVMLLTFQRSGKMKGMGKVVEWSVRDENIHVEGVSKLFETLNSEYPWVVTKDLIELFKEDAERVAELEEAFVDLAFQECGPVCGLEPKQVKDYVLYVINLRAANMGLPKLIERAPEACPIPWVKWLIDGADLTNFFENHVTEYETGGLTGSWSYEPLDI | Cofactor: Binds 2 iron ions per subunit.
Function: Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 43890
Sequence Length: 387
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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Q9KFH7 | MEQLQKRKIYDTTASNASTGILNGKSSNVLNWDDVRFSWAYPLYKNMLANFWTPFEINMSHDAKQFPTLTETEQEAFKKIIGLLAFLDSVQTDYSMRAAEYLTDSSLAALMSVLSFQEVVHNQSYSYVLSSLVPKATQDEIFEYWKHDDVLKERNEFIIDGYEKFVDNPTPKTFLESIVYDVILEGLNFYSGFAFFYNLARNQKMVSTSTMINYINRDEQLHVYLFTNIFKELLVEFPELNTEETKTFVKTTLMKAADLEKDWFRYIIGDKIPGINPEDMETYISFIANKRAVQLGMEKPYPEIKHNPMKWIRAYEDVNSGKSDFFEQKSRQYAKVSADNGFDEL | Cofactor: Binds 2 iron ions per subunit.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 40242
Sequence Length: 345
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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P55983 | MEVSRKKIYNPNSTESVNERKIFGGNPTSMFDLNKIKYQWADHLWKTMLANTWFAEEVSMNDDKRDYLKLSAEEKIGYDRALAQLIFMDSLQANNLIDNINPFITSPEINLCLVRQAYEEALHSHAYAVMVESISANTEEIYDMWRNDMQLKSKNDYIAQVYMELAKNPTEENILKALFANQILEGIYFYSGFSYFYTLARSGKMLGSAQMIRFIQRDEVTHLILFQNMINALRNERADLFTPQLINEVIGMFKKAVEIEALWGDYITQGKILGLTSSLIEQYIQFLADSRLSKVGIAKVYGVQHPIKWVESFSSFNEQRSNFFEARVSNYAKGSVSFDDF | Cofactor: Binds 2 iron ions per subunit.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 39482
Sequence Length: 341
Pathway: Genetic information processing; DNA replication.
EC: 1.17.4.1
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P61720 | MGKIKVGVVTARWNQEITSKLEEGAISYLEACEDVEIFAALVPGAVEIPLACQAFLEAGCDGVVALGVVIRGDTSHYDYVCNSVTDGVTRLMLDYKKPIGFGVLTTENEEQALARAGGDHGNKGEEAAQVTMEMIGLTQEIPAAMKTALMLAKKAPAKAAKKPAKAAAKTQKKKKKVRK | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 19035
Sequence Length: 179
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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B2ICH3 | MAEPRRALAQMDDARISVGNARFLIIEAPYYEDIAAQLRAGAEAALTRAQARFDVVSVPGALEIPIALAIALDRAPALYQGAIALGCIIRGETYHFEIVANESARALTQLVVERKLPFGNGILTVETETQALERASVESGDKGGDAARAALALYRFSQEFGQVVEQAQIQAQRPVLTSGAR | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 19408
Sequence Length: 181
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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Q7VRI2 | MDVIEGNTVVSNITKIVVVVARFNKAINNHLLEGTIDTLKRVGQVQDENITIVWVPGAYELPLVSQALSISNKYDAIIVLGTIIRGITEHFEFIYKSCNFGLSNISISNLVPIGLGLLVTNDIGQAVERIGIKGNNKGSEAALAALEMINILKTIKNNN | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 17214
Sequence Length: 159
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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Q494E6 | MNIIESDTIANKAKIAIAVVRFNRFVNNNLLEGALDVLKRIGHVKDENITIIWVPGSYELPLIAKALAISHKYDGIIALGTVIRGFTIHFEFVAKECSSGLSRISMENTLPIGFGLLTTDNISQAIERSGIKANNKGSEAALAVLEMINILKIIKNSS | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 17190
Sequence Length: 158
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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Q7VTN4 | MNPYILTPDLNGEGLHIGIVRARFNEEIGQAQLQACLEELGKLGVDERDVMVVSVPGALELGVALARMAESYEFDALIALGAVIRGETYHFEVVSNESAAAISRIALETGIPVANGVLTVDTDEQAQARAAGKGADCAQVAVEMANLAAALEPEEDDEDDEDEDFDDEEDDGR | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 18433
Sequence Length: 173
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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Q8K9A6 | MNIIQSGINVKNASITIIIARFNEFINKNLLSGAIDTLTRIGQIDKEKILTIYVPGTYEIPIVASYIANTNKYDAIIAIGTIIKGSTDHFKHIANDAYSNLSRISTKYFIPITMGILTTENIQQSIERSGTKMGNKGSEAALAALEMINIMKKLKKINN | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 17520
Sequence Length: 159
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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C5D3M9 | MKVMEGNLVGTGLKIAIVISRFNEFITSKLLSGAMDGLKRHGVNENDVTVAWVPGAFEIPLIAKKLAESRQYDAVIALGAVIRGATSHYDYVCNEVAKGVSHAALSTGTPVIFGVLTTDTIEQAIERAGTKAGNKGWEAAVSAIEMANLLRTFA | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 16319
Sequence Length: 154
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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Q7NLS9 | MTVFEGNLQDTRDLKFAIVIARFNDLVVGKLLSACEDSLRRHGVAVGPDSHQVDYAWVPGSFEIPMVARQLALSGRYDAIVCLGAVIRGQTSHYDHVASEVAKGIQALAFQTGVPVTFGVLTTDTMQQAIERAGIKSNLGWEYGENAIEMATLTRKIRHLVAVRAVQPELPEQTPPSLLQ | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 19656
Sequence Length: 180
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
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Q7VM44 | MAKITGNLVATGLKFSIVTARFNDFINDKLLSGAVDTLVRHGAVESDIDTVWVPGAFEIPLVAKKMAESGKYDAVICLGTVIRGSTTHYDYVCNEVAKGIGAVALQTGVPIMFGVLTTESIEQAIERAGTKAGNKGAECALGAIEMVNVLKAL | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 16045
Sequence Length: 153
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
|
P45149 | MKVLEGSVAAPNAKVAVVIARFNSFINESLLEGAIDALKRIGQVKDENITIVRTPGAYELPLVARRLAESKKFDAIVALGTVIRGGTAHFEYVAGEASSGLGKVAMDAEIPVAFGVLTTENIEQAIERAGTKAGNKGAEAALTALEMVNLIQQIDAA | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 16419
Sequence Length: 157
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
|
B9LUV3 | MVSLGLVVARFNDSVTEPMAEAAREAATDRDAVIVDEVSVPGAYDSPLAADRLARRDDVDAVAVVGAIVTGDTDHDHVIASATADKLTQVSLDRDTPVTFGVSGPGMSGAEARERIDKGADAAEAAIDLADELD | Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 13820
Sequence Length: 134
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
|
O28856 | MKIGIADTTFSRINMGKIAIDELRKISSIPYERYTVPGIKDLPIAAKKLLEEKGCDIVITLGWVGGTQKDMLSYIVLSMGLVIVQLMTNKHVIDVTIHEDEAEDEKTLMMVAENRVREHVRNAVDLLVNPKRLQKLAGTGQRQGYPDVGPILK | Catalytic Activity: 2 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) = 5-amino-6-(D-ribitylamino)uracil + riboflavin
Sequence Mass (Da): 17083
Sequence Length: 153
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 2/2.
EC: 2.5.1.9
|
Q9HB40 | MELALRRSPVPRWLLLLPLLLGLNAGAVIDWPTEEGKEVWDYVTVRKDAYMFWWLYYATNSCKNFSELPLVMWLQGGPGGSSTGFGNFEEIGPLDSDLKPRKTTWLQAASLLFVDNPVGTGFSYVNGSGAYAKDLAMVASDMMVLLKTFFSCHKEFQTVPFYIFSESYGGKMAAGIGLELYKAIQRGTIKCNFAGVALGDSWISPVDSVLSWGPYLYSMSLLEDKGLAEVSKVAEQVLNAVNKGLYREATELWGKAEMIIEQNTDGVNFYNILTKSTPTSTMESSLEFTQSHLVCLCQRHVRHLQRDALSQLMNGPIRKKLKIIPEDQSWGGQATNVFVNMEEDFMKPVISIVDELLEAGINVTVYNGQLDLIVDTMGQEAWVRKLKWPELPKFSQLKWKALYSDPKSLETSAFVKSYKNLAFYWILKAGHMVPSDQGDMALKMMRLVTQQE | Function: May be involved in vascular wall and kidney homeostasis.
Sequence Mass (Da): 50831
Sequence Length: 452
Subcellular Location: Secreted
EC: 3.4.16.-
|
Q58584 | MTKKVGIVDTTFARVDMASIAIKKLKELSPNIKIIRKTVPGIKDLPVACKKLLEEEGCDIVMALGMPGKAEKDKVCAHEASLGLMLAQLMTNKHIIEVFVHEDEAKDDKELDWLAKRRAEEHAENVYYLLFKPEYLTRMAGKGLRQGFEDAGPARE | Catalytic Activity: 2 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) = 5-amino-6-(D-ribitylamino)uracil + riboflavin
Sequence Mass (Da): 17495
Sequence Length: 156
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 2/2.
EC: 2.5.1.9
|
Q59587 | MIKVGICDTTFARYDMGGAAIDEIKKHATGIKIIRRTVPGIKDLPVACKKLIEEEGCEMVMALGMPGPEEKDKVCAHEASTGLIQAQLMTNTHILEVFVHEDEEDDPEDLKVLADNRAREHAQNLIMMLFRPERLTRDAGMGMREGKPDVGPL | Function: The relatively low activity of this enzyme suggested that 6,7-dimethyl-8-ribityllumazine might not be its natural substrate.
Catalytic Activity: 2 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) = 5-amino-6-(D-ribitylamino)uracil + riboflavin
Sequence Mass (Da): 16969
Sequence Length: 153
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 2/2.
EC: 2.5.1.9
|
Q920A5 | MELSRRICLVRLWLLLLSFLLGFSAGSAIDWREPEGKEVWDYVTVRKDAHMFWWLYYATNPCKNFSELPLVMWLQGGPGGSSTGFGNFEEIGPLDTQLKPRNTTWLQWASLLFVDNPVGTGFSYVNTTDAYAKDLDTVASDMMVLLKSFFDCHKEFQTVPFYIFSESYGGKMAAGISVELYKAVQQGTIKCNFSGVALGDSWISPVDSVLSWGPYLYSMSLLDNQGLAEVSDIAEQVLDAVNKGFYKEATQLWGKAEMIIEKNTDGVNFYNILTKSSPEKAMESSLEFLRSPLVRLCQRHVRHLQGDALSQLMNGPIKKKLKIIPEDISWGAQASYVFLSMEGDFMKPAIDVVDKLLAAGVNVTVYNGQLDLIVDTIGQESWVQKLKWPQLSKFNQLKWKALYTDPKSSETAAFVKSYENLAFYWILKAGHMVPSDQGEMALKMMKLVTKQE | Function: May be involved in vascular wall and kidney homeostasis.
Sequence Mass (Da): 50965
Sequence Length: 452
Subcellular Location: Secreted
EC: 3.4.16.-
|
Q920A6 | MELSRRICLVRLWLLLLSFLLGFSAGSALNWREQEGKEVWDYVTVREDARMFWWLYYATNPCKNFSELPLVMWLQGGPGGSSTGFGNFEEIGPLDTRLKPRNTTWLQWASLLFVDNPVGTGFSYVNTTDAYAKDLDTVASDMMVLLKSFFDCHKEFQTVPFYIFSESYGGKMAAGISLELHKAIQQGTIKCNFSGVALGDSWISPVDSVLSWGPYLYSVSLLDNKGLAEVSDIAEQVLNAVNKGFYKEATQLWGKAEMIIEKNTDGVNFYNILTKSTPDTSMESSLEFFRSPLVRLCQRHVRHLQGDALSQLMNGPIKKKLKIIPDDVSWGAQSSSVFISMEEDFMKPVIDIVDTLLELGVNVTVYNGQLDLIVDTIGQESWVQKLKWPQLSRFNQLKWKALYTNPKSSETSAFVKSYENLAFYWILKAGHMVPADQGDMALKMMRLVTQQE | Function: May be involved in vascular wall and kidney homeostasis.
Sequence Mass (Da): 51175
Sequence Length: 452
Subcellular Location: Secreted
EC: 3.4.16.-
|
Q92963 | MDSGTRPVGSCCSSPAGLSREYKLVMLGAGGVGKSAMTMQFISHRFPEDHDPTIEDAYKIRIRIDDEPANLDILDTAGQAEFTAMRDQYMRAGEGFIICYSITDRRSFHEVREFKQLIYRVRRTDDTPVVLVGNKSDLKQLRQVTKEEGLALAREFSCPFFETSAAYRYYIDDVFHALVREIRRKEKEAVLAMEKKSKPKNSVWKRLKSPFRKKKDSVT | Function: Plays a crucial role in coupling NGF stimulation to the activation of both EPHB2 and MAPK14 signaling pathways and in NGF-dependent neuronal differentiation. Involved in ELK1 transactivation through the Ras-MAPK signaling cascade that mediates a wide variety of cellular functions, including cell proliferation, survival, and differentiation.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 25145
Sequence Length: 219
Subcellular Location: Cell membrane
EC: 3.6.5.2
|
P70426 | MESGARPIGSSCSSPAALSREYKLVMLGAGGVGKSAMTMQFISHRFPEDHDPTIEDAYKIRIRIDDEPANLDILDTAGQAEFTAMRDQYMRAGEGFIICYSITDRRSFHEVREFKQLIYRVRRTDDTPVVLVGNKSDLKQLRQVSKEEGLSLAREFSCPFFETSAAYRYYIDDVFHALVREIRKKEKELVLAMEKKAKPKNSVWKRLKSPFRRKKDSVT | Function: Plays a crucial role in coupling NGF stimulation to the activation of both EPHB2 and MAPK14 signaling pathways and in NGF-dependent neuronal differentiation. Involved in ELK1 transactivation through the Ras-MAPK signaling cascade that mediates a wide variety of cellular functions, including cell proliferation, survival, and differentiation (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 25169
Sequence Length: 219
Subcellular Location: Cell membrane
EC: 3.6.5.2
|
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