ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q54RB9 | MFANRVRQAQKLYQKRFFSLGNNSTISKQQFKNSSNNNNNKNGGNKNGFYQKAFIATTVALTTTLLTATTLLDDNTNSEKEILKSQRQTFEKYASTTLEGERQMTAEDFLSALTTLESDKQSGEHEILKASLDADKFKVLFQMADVDHTGYISFDEYVMFDELMAKPEAEYFLAFKLFDRDGNGYISKNDFKHVITASLDPSIPFNFDCELVNLYFGDGRTELNYSQFTQLLKDLQQERIKQEFKFHDKYNSGYIPRDKFAKVLGSVKLRKIPDHVRDKLESISELNLLSGHPNEVSYSQFVAANDMLLHIPSYGRVLKAAILKNKKDNINKEEFLTEARSSTSIEITPLEIDLIFHLFDLNKDGKLSISDFEKSTGLNINKIGGGTNYSDSYPSDSHVTIQNSSTTPSPSTPITNTAAAIALNKKHGKTFAQQVLESIENFALGSIAGGIGAAAVYPIDLVKTRMQNQRAVDPAKRLYVNSWDCFKKVVKFEGVRGLYKGILPQMVGVAPEKAIKLTVNDLLRDLFGDKSKGEIYFPLEVLAGGFAGMSQVCVTNPLEIVKIRLQVQSTGPKVSAITIIKELGLAGLYKGAGACLLRDIPFSAIYFPTYAKMKTILANEDGKLGPMDLLLAGAVAGIPAASLVTPADVIKTRLQVKANAGEQTYTGIRDCFQKILKEEGPRALFKGALARVFRSSPQFGVTLVSYELLQKALLPDAEYKPPTNAPITQKDFDVIRGNTNTVQRVIDMESKFGTLHQTRDNNKSSNGGENKN | Function: Mitochondrial and calcium-binding carrier that catalyzes the calcium-dependent exchange of cytoplasmic glutamate with mitochondrial aspartate across the mitochondrial inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 85648
Sequence Length: 772
Domain: Upon calcium binding, the EF-hand-containing regulatory N-terminal domain binds to the C-terminal domain, opening a vestibule which allows the substrates to be translocated through the carrier domain. In the absence of calcium, the linker loop domain may close the vestibule, which may prevent substrates from entering the carrier domain.
Subcellular Location: Mitochondrion inner membrane
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A0A2K3D5Z7 | MSVALASEYQLVQNAQLPQRWSQSARKSLAILEATARKEATAQMEAAGGSFCGQFPVDPAFKVLSLEYSAPNPDIARAIRRVDSVPNPPLPSHVVAIQSTAVDADLSLAMGVSLTPGRHTSYLVDARALQQSNSAAVAARKADGDKWGPACDEMFRGCRCVTGQEVVFYTAVKEPAGEVEGGEGSLFKPSFDGPAFRPSWGELSGKATGVVACVLQVPIGKETDIICAEYDNLVSKGQFATVDRFGGDHTVNMTGNALIQNDGKAISKGYAVAHRARVTSNVYGKANDVSLQRLAETVWSVVEKRLSFMPAYRDLVITEQGKPFMLGATATNIISLTENQGVMLHLDTDDGVWTIILWFHRHSGIIAGGEFVLPSLGISFQPLDFTIVVFAANTIVHGTRPLQTTGKIIRWGSSHFLRFKDVNALAQLGAAYGVDELDAKQRDQLEEVDAANSKDGVGAARRVASCMAAERKAAIEAQKAACVRGVVMNPCTGRMPSLLFWQVWRKPPALAVRANAVAGKKRAAADVDFCGA | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that catalyzes DNA modification by mediating the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-glyceryl-methylcytosine (5gmC) . Catalyzes the conjugation of a glyceryl moiety from L-ascorbate (vitamin C) to the methyl group of 5mC through a carbon-carbon bond . 5gmC DNA modification may be required during photosynthesis as an epigenetic mark that couteracts DNA methylation .
Catalytic Activity: a 5-methyl-2'-deoxycytidine in DNA + L-ascorbate + O2 = a (8S,9S)-5-glyceryl-2'-deoxycytidine in DNA + CO2 + glyoxylate
Sequence Mass (Da): 56994
Sequence Length: 532
Subcellular Location: Nucleus
EC: 1.14.99.-
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Q9U641 | MDSKYIQKTLSAITEQITKNAAVQKVLDNKFVKEHKYAAAAATVGLGVVAATTIVKAVNCEGKRYNYDAIPNLSFDDESIYDVATIGAGPSGSVLGYYLAREGRKVALLEKKVFPRDKYCGDAVATMAQDILREMGVMKELVDEDLGHFAQNGGFVSPNGNSFIGNSAKELKRDAKYNRGAVIAVKRIVLDEKVAKAAKRMGADLKENTTVENATFDRSTGVWTINCVDSEDNTKKIVYRARVLVCADGSPSNAARQLGYVHTEPNGICSRAYVKNNTTFRYDGVVFYPPSLLPGYCAIIREARDELNYLAYIIPGGKVTNDDLSKYHHQYMTEDPFISAALGPNPDIERMKAAPLRLGGIKKSYDDHLLIVGDAAGFIDPLTGEGIQYAMEGSRLASLALIQAFNERDLSHQSLKRYQDFWMAKFGHEFSMSMTMSLFLYRFPIVLDAAASLIEKRGSRFLAEWAAVMTGVKPKTWFLRPDVGPLIVLEIFGECFRRVFQGKKQIKKLD | Function: Receptor for cmfA, that appears to mediate the G-independent cmfA signal transduction.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56497
Sequence Length: 510
Subcellular Location: Membrane
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Q2I2P8 | MPKLGVSLFIFLVLFPLATLQLDGDQSAGRHAQERGEDLFKMYQYLRRALERRRTGEDFLEECMGGCAFDFCCKRSLRDTTSD | Function: This toxin inhibits both the TTX-sensitive and TTX-resistant sodium currents in adult rat dorsal root ganglion neurons. The inhibition on TTX-resistant sodium currents is stronger than on TTX-sensitive sodium currents . When intracranially injected into mice, the toxin induces tremors (50 nM), spasms (100 nM), and death (200 nM) .
PTM: Authors of PubMed:25600641 studied the activity of this peptide with the C-terminal Arg residue, which is probably cleaved in the native peptide.
Sequence Mass (Da): 9572
Sequence Length: 83
Domain: The cysteine framework is XVI (C-C-CC).
Subcellular Location: Secreted
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P05059 | MRSAAVLALLLCAGQVIALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSKECFETLRGDERILSILRHQNLLKELQDLALQGAKERTHQQKKHSSYEDELSEVLEKPNDQAEPKEVTEEVSSKDAAEKRDDFKEVEKSDEDSDGDRPQASPGLGPGPKVEEDNQAPGEEEEAPSNAHPLASLPSPKYPGPQAKEDSEGPSQGPASREKGLSAEQGRQTEREEEEEKWEEAEAREKAVPEEESPPTAAFKPPPSLGNKETQRAAPGWPEDGAGKMGAEEAKPPEGKGEWAHSRQEEEEMARAPQVLFRGGKSGEPEQEEQLSKEWEDAKRWSKMDQLAKELTAEKRLEGEEEEEEDPDRSMRLSFRARGYGFRGPGLQLRRGWRPNSREDSVEAGLPLQVRGYPEEKKEEEGSANRRPEDQELESLSAIEAELEKVAHQLEELRRG | Function: Strongly inhibits glucose induced insulin release from the pancreas.
PTM: In secretory granules, is attacked at both N- and C-terminal sides by proteolytic enzymes generating numerous peptides of various activities. Proteolytic processing can give rise to additional longer forms of catestatin peptides which display a less potent catecholamine release-inhibitory activity .
Sequence Mass (Da): 50015
Sequence Length: 449
Subcellular Location: Secreted
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P10645 | MRSAAVLALLLCAGQVTALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSQECFETLRGDERILSILRHQNLLKELQDLALQGAKERAHQQKKHSGFEDELSEVLENQSSQAELKEAVEEPSSKDVMEKREDSKEAEKSGEATDGARPQALPEPMQESKAEGNNQAPGEEEEEEEEATNTHPPASLPSQKYPGPQAEGDSEGLSQGLVDREKGLSAEPGWQAKREEEEEEEEEAEAGEEAVPEEEGPTVVLNPHPSLGYKEIRKGESRSEALAVDGAGKPGAEEAQDPEGKGEQEHSQQKEEEEEMAVVPQGLFRGGKSGELEQEEERLSKEWEDSKRWSKMDQLAKELTAEKRLEGQEEEEDNRDSSMKLSFRARAYGFRGPGPQLRRGWRPSSREDSLEAGLPLQVRGYPEEKKEEEGSANRRPEDQELESLSAIEAELEKVAHQLQALRRG | Function: Strongly inhibits glucose induced insulin release from the pancreas.
PTM: Sulfated on tyrosine residues and/or contains sulfated glycans.
Sequence Mass (Da): 50688
Sequence Length: 457
Subcellular Location: Secreted
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P04404 | SAAALALLLCAGQVIALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSQECFETLRGDERILSILRHQNLLKELQDLALQGAKERSHQQKKQSSYEDELSEVLEKQNDQAELKEGTEEASSKEAAEKRGDSKEVEKNDEDADGAKPQASLEPPXXXEAEDQTPGEEEAASTHPLASLPSKKRPGAQAEEDHEGPSQGPVDREKGPSAEQGPQAEREEEEEAEAGEKAVPEEEGPRSEAFDSHPSLGYKEMQRGWPQAPAMDGAGKTGAEEAQPPEGKGAREHSRQEEEEETAGAPQGLFRGGKRGEPAQEEEERLSEEWENAKRWSKMDRLAKELTAEKRLQGEEEEEEEEEDPDRSMKLSFRAPAYGFRGPGLQLRRGWRPSSREDSVEAGLPLQVRXYLEEKKEEEGSANRRPEDQELESLSAIEAELEKVAPQLQSLRRG | Function: Strongly inhibits glucose induced insulin release from the pancreas.
PTM: O-glycosylated; contains chondroitin sulfate (CS). CS attachment is pH-dependent, being observed at mildly acidic conditions of pH 5 but not at neutral pH, and promotes self-assembly in vitro.
Sequence Mass (Da): 49328
Sequence Length: 446
Subcellular Location: Secreted
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Q12N04 | MNSKQDRIYAKPAQTISDFQFDSRVAGVFNDMIRRSVPGYNQIIATLGDFARRYVTPNSKVFDLGSSLGSATLSIRRQIEGRQCQIIAIDNSQSMIERCEENLAAYVSDTQVTLVCDDIRNVDINNASMVVLNFTLQFLPPEDRDTLIKRIYDGMLPGGILVLSEKVKFDDACIQTLLDEQHLDFKRANGYSELEISQKRSALENVMRTDTLVQHQQRITDSGFSHFSVWFQCFNFASMVAIK | Function: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
Catalytic Activity: prephenate + S-adenosyl-L-methionine = 3-phenylpyruvate + carboxy-S-adenosyl-L-methionine + H2O
Sequence Mass (Da): 27569
Sequence Length: 243
EC: 2.1.3.-
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O34639 | MSDVVNIVVWSKKGCSYCEEVKNYLNEKGFPFQNIDVSEKEKLRDILQVKYGVRHVPVVEIGRGNQYQGITEIGIEHLDLALANHAQIKEAKR | Function: Involved in a cysteine salvage pathway from S-alkylcysteine. Catalyzes the reduction of N-acetyl-S-hydroxy-L-cysteine (N-acetyl-L-cysteine sulfenic acid) to N-acetyl-L-cysteine. This pathway is likely important in the catabolism of alkylated cysteine generated by proteolysis of alkylated glutathione formed in the detoxification of a wide range of electrophiles.
Catalytic Activity: AH2 + N-acetyl-S-hydroxy-L-cysteine = A + H2O + N-acetyl-L-cysteine
Sequence Mass (Da): 10628
Sequence Length: 93
Pathway: Amino-acid metabolism.
EC: 1.8.4.-
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O34974 | MTRADFIQFGAMIHGVGGTTDGWRHPDVDPSASTNIEFYMKKAQTAEKGLFSFIFIADGLFISEKSIPHFLNRFEPITILSALASVTKNIGLVGTFSTSFTEPFTISRQLMSLDHISGGRAGWNLVTSPQEGAARNHSKSNLPEHTERYEIAQEHLDVVRGLWNSWEHDAFIHNKKTGQFFDQAKLHRLNHKGKYFQVEGPLNIGRSKQGEPVVFQAGSSETGRQFAAKNADAIFTHSNSLEETKAFYADVKSRAADEGRDPSSVRIFPGISPIVADTEEEAEKKYREFAELIPIENAVTYLARFFDDYDLSVYPLDEPFPDIGDVGKNAFQSTTDRIKREAKARNLTLREVAQEMAFPRTLFIGTPERVASLIETWFNAEAADGFIVGSDIPGTLDAFVEKVIPILQERGLYRQDYRGGTLRENLGLGIPQHQSVLHSSHH | Function: Involved in a cysteine salvage pathway from S-alkylcysteine. Catalyzes the C-S bond cleavage in N-acetyl-S-benzyl-L-cysteine sulfoxide leading to N-acetyl-S-hydroxy-L-cysteine and benzaldehyde. This pathway is likely important in the catabolism of alkylated cysteine generated by proteolysis of alkylated glutathione formed in the detoxification of a wide range of electrophiles. Has much less efficient activity with N-acetyl-S-methyl-L-cysteine sulfoxide as substrate. Cannot use S-alkylated L-cysteine sulfones and ketone analogs as substrates, demonstrating that the sulfoxide is required for activity.
Catalytic Activity: (R)-N-acetyl-S-benzyl-L-cysteine sulfoxide + FMNH2 + O2 = benzaldehyde + FMN + H(+) + H2O + N-acetyl-S-hydroxy-L-cysteine
Sequence Mass (Da): 49411
Sequence Length: 442
Pathway: Amino-acid metabolism.
EC: 1.14.14.-
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P36566 | MQDRNFDDIAEKFSRNIYGTTKGQLRQAILWQDLDRVLAEMGPQKLRVLDAGGGEGQTAIKMAERGHQVILCDLSAQMIDRAKQAAEAKGVSDNMQFIHCAAQDVASHLETPVDLILFHAVLEWVADPRSVLQTLWSVLRPGGVLSLMFYNAHGLLMHNMVAGNFDYVQAGMPKKKKRTLSPDYPRDPAQVYLWLEEAGWQIMGKTGVRVFHDYLREKHQQRDCYEALLELETRYCRQEPYITLGRYIHVTARKPQSKDKV | Function: Catalyzes the methylation of 5-carboxymethoxyuridine (cmo5U) to form 5-methoxycarbonylmethoxyuridine (mcmo5U) at position 34 in tRNAs. Four tRNAs (tRNA(Ala1), tRNA(Ser1), tRNA(Pro3) and tRNA(Thr4)) are fully modified with mcmo5U in stationary-phase E.coli. Also present at low frequency in tRNA(Leu3) and tRNA(Val1).
Catalytic Activity: 5-carboxymethoxyuridine(34) in tRNA + S-adenosyl-L-methionine = 5-methoxycarbonylmethoxyuridine(34) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29814
Sequence Length: 261
EC: 2.1.1.-
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O34846 | MIRLSILDQSLIGEGETAADTLQHTVKLAQMAEECGYHRFWVAEHHNNDEIAGSAPEVLLGYLAASTRKIRLASGGVMLQHYSSYKVAEQFHLLSALAPGRIDLGVGKAPGGFQLSTDALQAEYKKPVRQFDEKLEELTHFVRDDFPDTHRYAALRPRPQVDRKPGIFLLGGSTESAISAAKLGISFVFAYFINGEEEVLKEARRAFDAHLPPGSEAEFHLAPAVFAAHTKEEAEKHIVSRESIKVVLKDGRKVNVGSREQAEAYLENVTEPYDIIVQKTGIIAGTKEEVAEELTRLSGTYKINDFVIFTPIKNAVEKQLSYQLLSDAVLAAKR | Function: Involved in a cysteine salvage pathway from S-alkylcysteine. Catalyzes the oxidation of N-acetyl-S-benzyl-L-cysteine and N-acetyl-S-methyl-L-cysteine to (R)-N-acetyl-S-benzyl-L-cysteine sulfoxide and (R)-N-acetyl-S-methyl-L-cysteine sulfoxide, respectively. This pathway is likely important in the catabolism of alkylated cysteine generated by proteolysis of alkylated glutathione formed in the detoxification of a wide range of electrophiles.
Catalytic Activity: FMNH2 + N-acetyl-S-benzyl-L-cysteine + O2 = (R)-N-acetyl-S-benzyl-L-cysteine sulfoxide + FMN + H(+) + H2O
Sequence Mass (Da): 36944
Sequence Length: 334
Pathway: Amino-acid metabolism.
EC: 1.14.14.-
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P14204 | MKKILVIDDHPAVMEGTKTILETDSNLSVDCLSPEPSEQFIKQHDFSSYDLILMDLNLGGEVNGMELSKQILQENPHCKIIVYTGYEVEDYFEEAIRAGLHGAISKTESKEKITQYIYHVLNGEILVDFAYFKQLMTQQKTKPAPSSQKEQDVLTPRECLILQEVEKGFTNQEIADALHLSKRSIEYSLTSIFNKLNVGSRTEAVLIAKSDGVL | Function: Response regulator in the two-component regulatory system ComP/ComA involved in a major quorum response pathway that regulates the development of genetic competence. Regulates directly the expression of over 20 genes, including genes of the srfA operon, degQ, rapA, rapC, rapE, rapF, etc. Regulates indirectly, through the regulation of comK transcription, the expression of late competence genes.
PTM: Phosphorylated by ComP.
Sequence Mass (Da): 24129
Sequence Length: 214
Subcellular Location: Cytoplasm
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O13067 | MSTSTPQSGGRRKPETPDSAFLSPATRPQPISAAATPTLLNFTSNDDERERKLRRMSRVIDLQLSNANSPATAISPAQSRGADTPTSLLPKLNNTQISDHYSTCIKLSQENKITTKNAFGLHLIDYMGDILKHKDSELTNFKVAAGTLDASAKIYAVRVDAVHADVYKVLGGLGKESQATEDTENQETDTGPQDGRKNPKRRKCSYKTIERNLNSINRSETERKSEIDPLFQKAAASFDEFSTAGVFLSTLKCHSYHSELHFDADVKPLSTAEETEPPSPGSMDSTELKSLFLQCVEKRPLCPSLSGFRFMQWNSDAQNENLSLLMDKFKKSDHVFDINAEVEDDFVESEAPVADEFDADVCEGMDAGDIGEFAEHREACRLERKGAQLTQIGNGDIGTMCLQLSSCPGEYSYFSPRTMSMWAGPEHWRFRPRQKASTDSDQQRVKKAKKVFELNFEDDIDFEVHFRKTRAATTLTKSTLESQNKKSTTLPADFHYDPDNIARMSLRPKDRIRKTTVQESVSEPEDDIGDYDYNNPNDTSNFCPALQAADSDDDDGAFLGPESNSAGFSAENQMNITSYGESNLVAGQKVNKIEIQYAKTAKKMDMKRLKSSMWSLLANCPESQEEMPSSKEEIDAALITDEQVFSSVTHGLQKRLPPVMAQNLSVPLAFACLLHLANEKNLKLQGMDDLSDVMIMQDD | Function: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerase.
PTM: Phosphorylated by CDK1. Its phosphorylation, as well as that of XCAP-D2 and XCAP-G subunits, activates the condensin complex and is required for chromosome condensation.
Sequence Mass (Da): 77778
Sequence Length: 699
Subcellular Location: Nucleus
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Q9BPX3 | MGAERRLLSIKEAFRLAQQPHQNQAKLVVALSRTYRTMDDKTVFHEEFIHYLKYVMVVYKREPAVERVIEFAAKFVTSFHQSDMEDDEEEEDGGLLNYLFTFLLKSHEANSNAVRFRVCLLINKLLGSMPENAQIDDDVFDKINKAMLIRLKDKIPNVRIQAVLALSRLQDPKDDECPVVNAYATLIENDSNPEVRRAVLSCIAPSAKTLPKIVGRTKDVKEAVRKLAYQVLAEKVHMRAMSIAQRVMLLQQGLNDRSDAVKQAMQKHLLQGWLRFSEGNILELLHRLDVENSSEVAVSVLNALFSITPLSELVGLCKNNDGRKLIPVETLTPEIALYWCALCEYLKSKGDEGEEFLEQILPEPVVYADYLLSYIQSIPVVNEEHRGDFSYIGNLMTKEFIGQQLILIIKSLDTSEEGGRKKLLAVLQEILILPTIPISLVSFLVERLLHIIIDDNKRTQIVTEIISEIRAPIVTVGVNNDPADVRKKELKMAEIKVKLIEAKEALENCITLQDFNRASELKEEIKALEDARINLLKETEQLEIKEVHIEKNDAETLQKCLILCYELLKQMSISTGLSATMNGIIESLILPGIISIHPVVRNLAVLCLGCCGLQNQDFARKHFVLLLQVLQIDDVTIKISALKAIFDQLMTFGIEPFKTKKIKTLHCEGTEINSDDEQESKEVEETATAKNVLKLLSDFLDSEVSELRTGAAEGLAKLMFSGLLVSSRILSRLILLWYNPVTEEDVQLRHCLGVFFPVFAYASRTNQECFEEAFLPTLQTLANAPASSPLAEIDITNVAELLVDLTRPSGLNPQAKTSQDYQALTVHDNLAMKICNEILTSPCSPEIRVYTKALSSLELSSHLAKDLLVLLNEILEQVKDRTCLRALEKIKIQLEKGNKEFGDQAEAAQDATLTTTTFQNEDEKNKEVYMTPLRGVKATQASKSTQLKTNRGQRKVTVSARTNRRCQTAEADSESDHEVPEPESEMKMRLPRRAKTAALEKSKLNLAQFLNEDLS | Function: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.
PTM: Phosphorylated by CDK1. Its phosphorylation, as well as that of NCAPD2 and NCAPH subunits, activates the condensin complex and is required for chromosome condensation (By similarity).
Sequence Mass (Da): 114334
Sequence Length: 1015
Subcellular Location: Nucleus
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A0A059WLZ7 | MFLQNAWYAVAWCDEVTDGIVTRKVLGRELALFRDGEGQPRAILNRCPHRFAPLSLGKRIGDAIQCPYHGLHFGPDGRCVHNPHGDGVVPDVATPTFPARERHKLIWAWMGDPALATDDIAGGEYGYLDDVELDLLPRGHLHLDCDYRLVIDNLMDPAHVAVLHDSALASEALIRAVPRVWREEDVIRVESWAPDSKPSFLFGAWLGNHDDPVDHWVASRWQAAGLLSVEGGVVAVGGDREDGLRVRGAHMITPETETSAHYFWAVVRNFREDDAEQSEQIRATTAAIFTGEDKWMLEAIERSMDGEEFWSLRPAILGTDRAAVMVRRALESEIKAEGRPKVVAVSAG | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Component of the chloroacetanilide N-alkylformylase multicomponent enzyme system involved in the degradation of chloroacetanilide herbicides (N-alkoxyalkyl-N-chloroacetyl-substituted aniline derivatives). In vitro, catalyzes the N-dealkylation of butachlor, alachlor and acetochlor to yield 2-chloro-N-(2,6-diethylphenyl)acetamide (CDEPA) (for alachlor and butachlor) and 2-chloro-N-(2-methyl-6-ethylphenyl)acetamide (CMEPA) (for acetochlor).
Catalytic Activity: butachlor + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = butyl formate + H2O + N-(2,6-diethylphenyl)-2-chloroacetamide + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 38664
Sequence Length: 348
EC: 1.14.15.23
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P9WP64 | MHRLRAAEHPRPDYVLLHISDTHLIGGDRRLYGAVDADDRLGELLEQLNQSGLRPDAIVFTGDLADKGEPAAYRKLRGLVEPFAAQLGAELVWVMGNHDDRAELRKFLLDEAPSMAPLDRVCMIDGLRIIVLDTSVPGHHHGEIRASQLGWLAEELATPAPDGTILALHHPPIPSVLDMAVTVELRDQAALGRVLRGTDVRAILAGHLHYSTNATFVGIPVSVASATCYTQDLTVAAGGTRGRDGAQGCNLVHVYPDTVVHSVIPLGGGETVGTFVSPGQARRKIAESGIFIEPSRRDSLFKHPPMVLTSSAPRSPVD | Cofactor: Binds 1 Fe(3+) ion per subunit.
Function: Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP.
Catalytic Activity: a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 3'-phosphate + H(+)
Sequence Mass (Da): 34233
Sequence Length: 318
Domain: The C-terminal extension (CTE) is used to better adjust the substrates into the active sites and mediates in vivo subcellular localization of the protein.
Subcellular Location: Cytoplasm
EC: 3.1.4.16
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Q2FVF0 | MTLLTVKHLTITDTWTDQPLVSDVNFTLTKGETLGVIGESGSGKSITCKSIIGLNPERLGVTGEIIFDGTSMLSLSESQLKKYRGKDIAMVMQQGSRAFDPSTTVGKQMFETMKVHTSMSTQEIEKTLIEYMDYLSLKDPKRILKSYPYMLSGGMLQRLMIALALALKPKLIIADEPTTALDTITQYDVLEAFIDIKKHFDCAMIFISHDLTVINKIADRVVVMKNGQLIEQGTRESVLHHPEHVYTKYLLSTKKKINDHFKHVMRGDVHD | Function: Part of the ABC transporter complex CntABCDF (Opp1) involved in the uptake of metal in complex with the metallophore staphylopine (StP). Involved in the import of divalent metals ions such as nickel, cobalt and zinc. Probably responsible for energy coupling to the transport system . Plays a major role in nickel/cobalt import in zinc-depleted conditions. Contributes to virulence. Required for full urease activity in vitro .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30469
Sequence Length: 271
Subcellular Location: Cell membrane
EC: 7.2.2.-
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A0A0H3JTK0 | MKGAMAWPFLRLYILTLMFFSANAILNVFIPLRGHDLGATNTVIGIVMGAYMLTAMVFRPWAGQIIARVGPIKVLRIILIINAIALIIYGFTGLEGYFVARVMQGVCTAFFSMSLQLGIIDALPEEHRSEGVSLYSLFSTIPNLIGPLVAVGIWNANNISLFAIVIIFIALTTTFFGYRVTFAEQEPDTSDKIEKMPFNAVTVFAQFFKNKELLNSGIIMIVASIVFGAVSTFVPLYTVSLGFANAGIFLTIQAIAVVAARFYLRKYIPSDGMWHPKYMVSVLSLLVIASFVVAFGPQVGAIIFYGSAILIGMTQAMVYPTLTSYLSFVLPKVGRNMLLGLFIACADLGISLGGALMGPISDLVGFKWMYLICGMLVIVIMIMSFLKKPTPRPASSL | Function: Involved in the export of the metallophore staphylopine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43295
Sequence Length: 397
Subcellular Location: Cell membrane
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Q71DR4 | MAAPVPWACCAVLAAAAAVVYAQRHSPQEAPHVQYERLGSDVTLPCGTANWDAAVTWRVNGTDLALDLLNGSQLVLHGLELGHSGLYACFHRDSWHLRHQVLLHVGLPPREPVLSCRSNTYPKGFYCSWHLPTPTYIPNTFNVTVLHGSKIMVCEKDPALKNRCHIRYMHLFSTIKYKVSISVSNALGHNATAITFDEFTIVKPDPPENVVARPVPSNPRRLEVTWQTPSTWPDPESFPLKFFLRYRPLILDQWQHVELSDGTTHTITDAYAGKEYIIQVAAKDYEIGTWSDWSVAAHATPWTEEPRHLTTEAQAPETTTSTTSSLAPPPTTKICDPGELGSGGGPSAPFLIHVPVTLALAAAAATANSLLI | Function: Binds to CNTF. The alpha subunit provides the receptor specificity (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 40831
Sequence Length: 372
Domain: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
Subcellular Location: Cell membrane
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P51641 | MANPVPSACCVVLAAVVVVYAQRHSQQDSHIQYERVGADVTMKCGSMDWDAAVTWTANGTDIDDSHLNGSYLILKNVDLTQSGQYSCYEGSSWHLKYQTYLRVGVPPKEPVLMCRSNNYPKGFYCSWHLPSPTYIPNSFNISVIHGTREMVCEKDIFPKNRCHIRYLQLFSTVKYKVTLTVTNALGKNSTTLTFDEFAIVKPDPPESVVAKPVPNNPRRLEVSWQNPSSWPDPESFPLKFFLRYRPLILDQWQHVELSDGTSHTITDAYAGKEYIIQVAAKDNDIGTWSDWSVAVHATPWTEEPKHLTTEVQITETTSTSTSSFMPPPTTKICDKGAGVGSGAVAVCWTAGLVLAAYGVLFI | Function: Binds to CNTF (GPA). The alpha subunit provides the receptor specificity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 40308
Sequence Length: 362
Domain: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
Subcellular Location: Cell membrane
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P26992 | MAAPVPWACCAVLAAAAAVVYAQRHSPQEAPHVQYERLGSDVTLPCGTANWDAAVTWRVNGTDLAPDLLNGSQLVLHGLELGHSGLYACFHRDSWHLRHQVLLHVGLPPREPVLSCRSNTYPKGFYCSWHLPTPTYIPNTFNVTVLHGSKIMVCEKDPALKNRCHIRYMHLFSTIKYKVSISVSNALGHNATAITFDEFTIVKPDPPENVVARPVPSNPRRLEVTWQTPSTWPDPESFPLKFFLRYRPLILDQWQHVELSDGTAHTITDAYAGKEYIIQVAAKDNEIGTWSDWSVAAHATPWTEEPRHLTTEAQAAETTTSTTSSLAPPPTTKICDPGELGSGGGPSAPFLVSVPITLALAAAAATASSLLI | Function: Binds to CNTF. The alpha subunit provides the receptor specificity. Receptor for heterodimeric neurotropic cytokine composed of CLCF1/CLC and CRLF1/CLF-1 . Acts as a receptor for the neuroprotective peptide humanin as part of a complex with IL6ST/GP130 and IL27RA/WSX1 .
Location Topology: Lipid-anchor
Sequence Mass (Da): 40633
Sequence Length: 372
Domain: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
Subcellular Location: Cell membrane
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O88507 | MAASVPWACCAVLAAAAAAVYTQKHSPQEAPHVQYERLGADVTLPCGTASWDAAVTWRVNGTDLAPDLLNGSQLILRSLELGHSGLYACFHRDSWHLRHQVLLHVGLPPREPVLSCRSNTYPKGFYCSWHLPTPTYIPNTFNVTVLHGSKIMVCEKDPALKNRCHIRYMHLFSTIKYKVSISVSNALGHNTTAITFDEFTIVKPDPPENVVARPVPSNPRRLEVTWQTPSTWPDPESFPLKFFLRYRPLILDQWQHVELSDGTAHTITDAYAGKEYIIQVAAKDNEIGTWSDWSVAAHATPWTEEPRHLTTEAQAPETTTSTTSSLAPPPTTKICDPGELGSGGGPSILFLTSVPVTLVLAAAAATANNLLI | Function: Binds to CNTF. The alpha subunit provides the receptor specificity (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 40801
Sequence Length: 372
Domain: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
Subcellular Location: Cell membrane
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Q08406 | MAASVPWACCAVLAAAAAAVYTQKHSPQEAPHVQYERLGTDVTLPCGTASWDAAVTWRVNGTDLAPDLLNGSQLILRSLELGHSGLYACFHRDSWHLRHQVLLHVGLPPREPVLSCRSNTYPKGFYCSWHLSAPTYIPNTFNVTVLHGSKMMVCEKDPALKNRCHIRYMHLFSTIKYKVSISVSNALGHNTTAITFDEFTIVKPDPPENVVARPVPSNPRRLEVTWQTPSTWPDPESFPLKFFLRYRPLILDQWQHVELSNGTAHTITDAYAGKEYIIQVAAKDNEIGTWSDWSVAAHATPWTEEPRHLTTEAQAPETTTSTTSSLAPPPTTKICDPGELSSGGGPSIPFLTSVPVTLVLAAAAATANNLLI | Function: Binds to CNTF. The alpha subunit provides the receptor specificity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 40822
Sequence Length: 372
Domain: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
Subcellular Location: Cell membrane
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Q2FVF1 | MIKIKDVEKSYQSAHVFKRRRTPIVKGVSFECPIGATIAIIGESGSGKSTLSRMILGIEKPDKGCVTLNDQPMHKKKVRRHQIGAVFQDYTSSLHPFQTVREILFEVMCQCDGQPKEVMEVQAITLLEEVGLSKAYMDKYPNMLSGGEAQRVAIARAICINPKYILFDEAISSLDMSIQTQILDLLIHLRETRQLSYIFITHDIQAATYLCDQLIIFKNGKIEEQIPTSALHKSDNAYTRELIEKQLSF | Function: Part of the ABC transporter complex CntABCDF (Opp1) involved in the uptake of metal in complex with the metallophore staphylopine (StP). Involved in the import of divalent metals ions such as nickel, cobalt and zinc. Probably responsible for energy coupling to the transport system . Plays a major role in nickel/cobalt import in zinc-depleted conditions. Contributes to virulence. Required for full urease activity in vitro .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28180
Sequence Length: 249
Subcellular Location: Cell membrane
EC: 7.2.2.-
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Q9HUX6 | MVLDLLKSGVLLAVLASFTFSVMNALVKEASATLPAAEIVFFRSAIGTLLIYLLMRQAGVALSRQGVPMLLVRGVMGALYLVCYFYAIAHIPLADASILAHMSPFFVILFSALFLGERIPRAVYWLLLVVVLGALMIVKPFSYSSYSVYAVVGLLSAVFAAGASVAIRQLSARHHTYEIVFYFLAVATLVAIPLMWNDFVVPATLREWGLLLAIGVVSLLGQVFLTRAFSHESATIVAVTRYIGIVFNAGWGWLFWSEVPDALTIAGGVLIVVACIALSRTKKG | Function: Transports the metallophore pseudopaline, which is involved in the acquisition of nickel and zinc, and thus enables bacterial growth inside the host, where metal access is limited. Is probably involved in the export of pseudopaline (By similarity). Essential for iron acquisition during the interaction with airway mucus secretions (AMS) .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30723
Sequence Length: 284
Subcellular Location: Cell inner membrane
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A0A0H3JU78 | MNRQVIEFSKYNPSGNMTILVHSKHDASEYASIANQLMAATHVCCEQVGFIESTQNDDGNDFHLVMSGNEFCGNATMSYIHHLQESHLLKDQQFKVKVSGCSDLVQCAIHDCQYYEVQMPQAHRVVPTTINMGNHSWKALEIIYETYVHYVIPVKQVTTEIQHLVEAFVREQQWSHKYKTVGMMLFDEQRQFLQPLIYIPEIQSLIWENSCGSGTASIGVFNNYQRNDACKDFTVHQPGGSILVTSKRCHQLGYQTSIKGQVTTVATGKAYIE | Function: Catalyzes the reversible interconversion of the L- and D-stereoisomers of histidine. Functions in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, cobalt, zinc, copper, and iron, and thus enables bacterial growth inside the host, where metal access is limited. Therefore, this enzyme probably contributes to staphylococcal virulence. Appears to be specific for histidine, as it cannot use L-alanine and L-methionine as substrate.
Catalytic Activity: L-histidine = D-histidine
Sequence Mass (Da): 31004
Sequence Length: 273
EC: 5.1.1.24
|
C8CK74 | MEKLTVLILVATVLLTIQVLGQSDRDKHLKRRPKQYATKRLSARMRGHRQCTGAGYECEETPECCPNLTCKCSGSPLCTRYSCQA | PTM: Contains 4 disulfide bonds.
Sequence Mass (Da): 9546
Sequence Length: 85
Domain: The cysteine framework is XV (C-C-CC-C-C-C-C).
Subcellular Location: Secreted
|
Q3SYW2 | MDPLMAVLCLLPLYPGLATAALSCPKNVNISGGSFTLSNGWNPGSILTYSCPLGHYPYPVVTRLCKSNGQWQIPRSTRSTKAICKPVRCPAPVSFENGVYIPRLGSHPVGGNLSFECEDGFTLRGSAVRQCRPNGMWDGETAVCDNGASHCPNPGISVGAVRTGSRFGLGDKVRYRCSSNLVLTGSAERECQDDGVWSGTEAICRQPYSYDFPEDVAPALGTSFSHLLATTNPIQQKKKQNLGRKIQIQRSGHLNLYLLLDASQSVSKDDFEIFKDSASRMVDRIFSFEIKVSVAIITFASKPKIIMSVLEDRSRDVTEVENSLRNINYKDHENGTGTNIYEALHAVYIMMNNQMNRPHMNPGAWQEIRHAIILLTDGKSNMGGSPKVAVDNIKEVLNINQKRKDYLDIYAIGVGSLHVDWKELNNLGSKKDGERHAFILKDVQALSQVFEHMLDVSQLTDPICGVGNMSANASAQERTPWHVTIKPKSQETCRGALISDQWVLTAAHCFRNAEDRTLWRVSVGDPNFQGSKEFQIEEAVISPGFNVFSKKSQGIPEFYGDDIALLKLTQKVKMSTHARPICLPCTVGANLALRKLPGSTCRDHEKELLNQVSIPAHFVALNGDKLNINLKTGSEWTNCVKVVLKDKTTFPNLTDVREVVTDQFLCSGTQGDDSPCKGESGGAVFLERRLRFFQVGLVSWGLYNPCGGSSKNSRKPAPHGKVPRDFHINLFRLQPWLRQHLEGILNFVPL | Function: Component C2 which is part of the classical pathway of the complement system is cleaved by activated factor C1 into two fragments: C2b and C2a. C2a, a serine protease, then combines with complement factor C4b to generate the C3 or C5 convertase (By similarity).
Catalytic Activity: Selective cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to form C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha-chain to form C5a and C5b.
Sequence Mass (Da): 82906
Sequence Length: 750
Domain: The MIDAS-like motif in the VWFA domain binds divalent metal cations.
Subcellular Location: Secreted
EC: 3.4.21.43
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P06681 | MGPLMVLFCLLFLYPGLADSAPSCPQNVNISGGTFTLSHGWAPGSLLTYSCPQGLYPSPASRLCKSSGQWQTPGATRSLSKAVCKPVRCPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVCDNGAGHCPNPGISLGAVRTGFRFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPICRQPYSYDFPEDVAPALGTSFSHMLGATNPTQKTKESLGRKIQIQRSGHLNLYLLLDCSQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSVLNDNSRDMTEVISSLENANYKDHENGTGTNTYAALNSVYLMMNNQMRLLGMETMAWQEIRHAIILLTDGKSNMGGSPKTAVDHIREILNINQKRNDYLDIYAIGVGKLDVDWRELNELGSKKDGERHAFILQDTKALHQVFEHMLDVSKLTDTICGVGNMSANASDQERTPWHVTIKPKSQETCRGALISDQWVLTAAHCFRDGNDHSLWRVNVGDPKSQWGKEFLIEKAVISPGFDVFAKKNQGILEFYGDDIALLKLAQKVKMSTHARPICLPCTMEANLALRRPQGSTCRDHENELLNKQSVPAHFVALNGSKLNINLKMGVEWTSCAEVVSQEKTMFPNLTDVREVVTDQFLCSGTQEDESPCKGESGGAVFLERRFRFFQVGLVSWGLYNPCLGSADKNSRKRAPRSKVPPPRDFHINLFRMQPWLRQHLGDVLNFLPL | Function: Component C2 which is part of the classical pathway of the complement system is cleaved by activated factor C1 into two fragments: C2b and C2a. C2a, a serine protease, then combines with complement factor C4b to generate the C3 or C5 convertase.
Catalytic Activity: Selective cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to form C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha-chain to form C5a and C5b.
Sequence Mass (Da): 83268
Sequence Length: 752
Domain: The MIDAS-like motif in the VWFA domain binds divalent metal cations.
Subcellular Location: Secreted
EC: 3.4.21.43
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Q03692 |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| Function: Type X collagen is a product of hypertrophic chondrocytes and has been localized to presumptive mineralization zones of hyaline cartilage.
PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Sequence Mass (Da): 66158
Sequence Length: 680
Subcellular Location: Secreted
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A8HYS9 | MDQRLDPGLSPYRTFTRAEWAQLREDTPMTLGAEEILRLQGLNDRLSIREVEEIYLPLSRLLSMYVGATQKLFRAMSQFLDHRNNAEGKMPYIIGVAGSVAVGKSTTARVLQALLARWPHTPKVDLVTTDGFLLPNAVLQREGLMEKKGFPESYDLSLLLRFLTDIKAGRRPVKAPLYSHFFYDVLPDQMVEVDRPDILIVEGLNVLQTGRPPRDGKAIPFVSDFFDFSVYIDADEDVLEHWYVQRFMRLRETAFKDPLSYFHRYSKLTEEEARETALSIWHRINLTNLRENILPTRQRANLILRKAGDHEVAEVQLRKL | Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 36973
Sequence Length: 320
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
P54556 | MKNKELNLHTLYTQHNRESWSGFGGHLSIAVSEEEAKAVEGLNDYLSVEEVETIYIPLVRLLHLHVKSAAERNKHVNVFLKHPHSAKIPFIIGIAGSVAVGKSTTARILQKLLSRLPDRPKVSLITTDGFLFPTAELKKKNMMSRKGFPESYDVKALLEFLNDLKSGKDSVKAPVYSHLTYDREEGVFEVVEQADIVIIEGINVLQSPTLEDDRENPRIFVSDFFDFSIYVDAEESRIFTWYLERFRLLRETAFQNPDSYFHKFKDLSDQEADEMAASIWESVNRPNLYENILPTKFRSDLILRKGDGHKVEEVLVRRV | Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 36640
Sequence Length: 319
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
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Q89WM2 | MDIRAPEQQYNPYRVYTREQWARLRDDTPMTLEPGEFDRLRSLHDRLDLQEVEDIYLPLSRLLSIYVDAMQRLYYAERQFLNIRDRKMPYIIGVAGSVAVGKSTTARVLQALLARWSPRPKVDLITTDGFLYPNAVLDRQGIMQKKGFPESYDLPLLLGFLSDIKAGRRHVRAPVYSHLTYDIVPNQWVEIDQPDILIVEGVNVLQTGKLPRDGKAVPVVSDFFDFSVYIDADEAALRRWYIKRFLALRDTAFTNPKSYFNRYALLSDEEATATAIAIWERTNLANLEDNILPTRPRATLILKKGPDHVVESVALRRL | Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 36712
Sequence Length: 318
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
A7HSG6 | MGDDALTADSGRDETQSLSPFRYFTAAEWGRLRQDTPLPLSQGELEELKGFGERISLDEVSEIYLPLSRLLNLYVGETQELYRVTSDFLGREQDKVPYIIGVAGSVAVGKSTTARILRTLLARWPNHPKVDLITTDGFLYPNKVLEERGLMQRKGFPESFDIKRLLRFLSDVKAGSRHVEAPVYSHFTYDILPGETIPVDYPDILVVEGLNVLQPWKPADGDEPQPFVSDFFDFSIYLDADEASIRRWYIERFLSLRRTSFKDPAAYFHRYSKLTEEEAVETADAIWTSINLANLRKNILPTRQRADLILRKGDDHRIRDVLLRKL | Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 37414
Sequence Length: 326
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
B7GN19 | MTIAVCPGSYDPVTAGHLDVIERSARFFDEVHVVVAVNAAKTPMFSDATRVDVIRRALDKAGCKNVTVSSTDGLITDYCKKVGATVIVKGLRQNGDYEAELGMALVNRKLAGIETLFLPADPILEHISSSIVKDVARHGGDVTGMVPDCVVPMLADALAEERQRKD | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 17810
Sequence Length: 166
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.7.3
|
Q491X2 | MTIQAMYPGTFDPLTYGHLDIIIRAHKIFDKIFLAVAENSQKHPLFSLEERVIFAKQATAMLDYVTVFGFNDLTINVMKKKQVNILIRGLRNRSDFEYEIQLAKINNYFSNEVETVFMISTDIWACLSSKLVKEIAQYGGRIDHFIPNFIVEKVIEKLRNTEKKNKNISFL | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 19885
Sequence Length: 171
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.7.3
|
O51645 | MRVAVFPGSFDPITWGHIDLIKRSLAIFDKVIVLVAKNKSKKYFLSDIERFSLTKDVISSLNFSNVLVDRYSGFIVDYALINSIKFIVRGIRAFNDFDIEFERYLVNNKLNFEIDTIFLPSSAEHLYVRSDFVKELMLKKDVDLSNFVPELVFNRLKSKFIDK | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 19016
Sequence Length: 163
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.7.3
|
C0R0Q0 | MKNGKVIFPGTFDPFTLGHLDVLYRLADIFNKVYISVAVNLDKSPTFSIDERKNMIKKVIGDNDTIEIVTISGLVTEYMKQNDIKVLARGIRDSEDLYYELRMSRMNKLLYPEMDTIFLHTSEHYAYVSSSLIKEILKFNGPIDGLVPEILVEDIRSKFIKK | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 18671
Sequence Length: 162
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.7.3
|
A5EJR7 | MQRIALYPGSFDPVTNGHLDVVRQAVHLCDRLIVAVGVHHGKKPLFSTEERLAMVHEVLEPVAAAAGCGFEASTYDDLTVTAAQKAGAIMMIRGLRDGTDFDYEMQLAGMNQTMVPGIQTVFVPASVAVRPIAATLVRQIAAMGGDVSHFVPAAVAASLKAKFN | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 17417
Sequence Length: 164
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.7.3
|
Q31EA3 | MSITAVYPGTFDPITCGHFDLIERAARFYDRLVIAVADNRNKTALFSLEKRVALAKEVTADMPNVEVIGFSGLLVDFVREIDGNVLLRGLRAVSDFEYEFQLASMNRKLAPEVETMFMTPAEQYAFISSSLVREISALGGDVSEFVHPVVAKALNEKQL | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 17664
Sequence Length: 159
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.7.3
|
B2GFL8 | MRRAICPGSFDPLHLGHCAVIRRATLLFDEVVVAVSTNPNKTHRFSEAQRIELVREVFADDPAVVVEPLESGLIADYAERRGAVALVKGLRNGADYDYELPMATMNRSLTGVETVFLPGEPSLLHVSSSLVMEVAALGGDVTSFVPPEVLRALEDE | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 16958
Sequence Length: 156
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.7.3
|
C5CFP6 | MKAIYPGSFDPITYGHMDILKRASKIFDEVVVLVMKNINKRYFFTFSERLSMVEKAVEGIQNARADSYEGLLVDYARKAGIKIVVRGLRAISDFEMEIQVAHINKAMYADLETVFLMTDPKYSFLSSSIVREAASFGGDVSLWVPPYVEEALKRKFSGST | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 18095
Sequence Length: 160
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.7.3
|
Q5FKS7 | MTIALFPGSFDPITNGHVETAKKAAQMFDKVFVVAMTNTSKKYLFTAEERTAFAKDALKNISNIEVLEKPEELTVKLAHELKANVIVRGVRNSADFLYEQEIAGINKRLAPDINTVLLFSSPDNSFVASSMIKELARFDEDVSQFLPIKAAKALRKKLRHE | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 18015
Sequence Length: 161
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.7.3
|
Q9CDQ6 | MTEKIGLFTGTFDPLTNGHLDVIKRASQHFDQLYVGIFKNDQKNPLFPTDKRVEMLEEALTSLSVTHKVKVIKHERDLTVNIAKKLGVTALVRSLRNSQDLEYEKNMFYFNMEMTGIETIFFLAKPELEPLNSTRMRELHAFGQDVSAWVPENVSRELRKLDEKK | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 19128
Sequence Length: 165
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.7.3
|
Q88VC8 | MVTAVFPGSFDPITRGHLDMIQRASRLVDRLIVAVMVNTSKQPLFTMTEKVAMISDELTGLPNVEVQAATGLTVDFMASVHATVLVRGLRNEQDFGYERDIAWMNKSLDETIETICLIARPPYAYFSSSLIKEVAKMGADVSKYVPTAVAQKLHQRLGTDQHD | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 18072
Sequence Length: 163
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.7.3
|
Q8E8I0 | MHTRAIYPGTFDPITNGHADLIERAAKLFKHVIIGIAANPSKQPRFTLEERVELVNRVTAHLDNVEVVGFSGLLVDFAKEQRASVLVRGLRAVSDFEYEFQLANMNRRLSPDLESVFLTPAEENSFISSTLVKEVALHGGDVSQFVHPEVASALAAKLKLAKA | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 17951
Sequence Length: 163
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.7.3
|
Q2NQU5 | MTNKAIYPGTFDPLTNGHLDLVTRAAKMFDVVVLAIAASPSKRPLFDLNERVALATQVTAHLPNVKVTGFSDLMADFARQQQANILIRGVRAMTDVDYEMPLAKMNRHLMPALETVFMLPAEAWSYISSTLVKEVALHGGDVDHFLPAPIAKEVRARLHP | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 17662
Sequence Length: 160
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.7.3
|
Q8RBE5 | MRVVGLTGGIGSGKSTVSGILAKLGAKIIDADLVSREIMEKGKEAYNEIVDCFGKEILDKEGNIDRKKLGSIVFSDKEKLKRLNEITHPKIIDKIKKMIEEEKDKDKVIVIDAALLIETGLYKLVDEVWLVVVDIDTQIKRVMERDGFSCEEALKRIKSQMPLEEKIKYADFIINNSKDLRKTEEQVRLLWQRFDRRSYFD | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 23106
Sequence Length: 201
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
|
Q9PMD9 | MKNAFFVTASIACGKSTFIEIANSLGFKSISADKIAHKILDENALELEKIFSPFSLKNLLKKEKKIDRKILGEIVFNNKEAKKILENFTHPKIRAKILEQMQILDKENKAFFVEIPLFFESGAYENLGKVIVIYTPKELSLKRIMQRDKLSLEAAKARLDSQIDIEEKLKKADFIIKNTNSYADFRQECVKVIQEISKGNM | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 23048
Sequence Length: 201
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
|
Q3ABL6 | MLVLPIIGLTGGIASGKSTVSRILQELGFAIIDADRIARDILTPGHPAYQKVIDTFGKNILTEDGQIDRAKLGKIVFGNREKLLVLNSITHPEVLKEIRKKIKELTSSGIDWIVLDIPLLFEAKMTSLVDEIWVVYVPEEEQLKRLMARNGFSRDEALARIRAQMPLEEKVKLADVVIDNSGSIESTREQILTILQKWKWKDWSKK | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 23299
Sequence Length: 206
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
|
P58100 | MLILGLTGSIGMGKSTTSKMFQDEGVPVYDADAAVHALYASGGAAVAPVETAFPGVVVDGAIDRAKLSAQVVGNSEALAKLEAIVHPLVGAHRIGFFEQAKAEGHEIVVLDIPLLFETGGEKRVDKVVVVSAPAEVQRERVLARPEMTPEKFEAILARQTPDADKRARADFVIDTGQGLDHARRQVRDLLTLLRTARSA | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 21188
Sequence Length: 199
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
|
Q3B3J7 | MTPSHPFLVGVTGGIGSGKSTLCRFLEKMGCELFEADKVARQLQVSDPEIMEGIKSLFGKDVYSKTRSGKLSLDRKRIAREVFSHPATLGALNNLIHPKVYNAFRQRALEAFGRGTAILVMEAAILFETGRAADLDFVVVVAADTETRIKRAVTRGLGTPEDIRKRIALQWPQEMLVARADYVVNNDIGKTKLKEEAGRLYSVLVEAAASGPDCQSKRR | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 24093
Sequence Length: 219
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
|
Q9Z7U3 | MLKLLKVSITGDLSSGKTEACQVFQELGAYVVSADEISHSFLIPHTRIGRRVIDLLGSDVVVDGAFDAQAIAAKVFYNSVLLQGLEAILHPEVCRIIEEQYHQSIQDGNYPLFVAEVPLLYEIHYAKWFDSVILVMANEDIRRERFMKKTGRSSEDFDQRCSRFLNVEEKLAQADVVVENNGTKKELHQKIEEYFYALKGAL | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22913
Sequence Length: 202
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.24
|
P37564 | MLLVIDVGNTNTVLGVYHDGKLEYHWRIETSRHKTEDEFGMILRSLFDHSGLMFEQIDGIIISSVVPPIMFALERMCTKYFHIEPQIVGPGMKTGLNIKYDNPKEVGADRIVNAVAAIHLYGNPLIVVDFGTATTYCYIDENKQYMGGAIAPGITISTEALYSRAAKLPRIEITRPDNIIGKNTVSAMQSGILFGYVGQVEGIVKRMKWQAKQEPKVIATGGLAPLIANESDCIDIVDPFLTLKGLELIYERNRVGSV | Cofactor: Monovalent cations. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. Cannot utilize a phosphoryl donor other than ATP.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 28576
Sequence Length: 258
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
Q89ZL1 | MNLIIDIGNTTAKVALFNRSEMVEVLTESNQSLDSLEALCSKYRIERGIVATVVDLNERILAELAALPFPLLWLNHETPLPVGNLYETPETLGYDRIAAVVGANEQFPHNDILVIDAGTCITYEFIDSKGQYHGGNISPGMQMRYKALHQFTGRLPLIDSNGRKLPMGRDTETAIRAGVLKGMEYEISGYIEAMKHKYPELLVFLTGGDDFSFDSSVKSAIFADRFLVLKGLNRILNYNNGRI | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27060
Sequence Length: 243
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
Q6MHI0 | MILCLDVGNTQIYAGLFDKDKMVLSFRKNSKSGASSDETGIFLRTAIRENGFDPAKVKQIAICSVVPEVIYSLRGACMKYFNINPFILQAGVKTGLKIKYRNPLEVGADRIANSIAATHLHPGKNLILVDLGTATTFCAVSKDKDYLGGSIVAGLRLCMEALESKTAKLPSVEIVAMHEALGRATIESIQSGLYYGHLGTIKELTERITKECFQGERPMVIGTGGFSYLFEKEKVFDEIVPDLVLKGMLIALQHNA | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27952
Sequence Length: 256
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
B8DTP8 | MILAVDIGNTNIVIGLMEGTETVDTYRITTRSNHTSDEYGLMILQFLQLSNSSPDDVQDAIISSVVPKVMHSFISSMIKFLGIDPMIIGPGIKTGMNIRMDDPRSLGADLLADCAGAYTTYGGPVLVIDMGTATTYNYVDEKGAILAGLITTGIGTAAAALASNTAQLPEVQITRPKSILAANTKDAMQAGLYYDCLGGIERTITQFREELDTDFKVVATGGMSRIFDCPLIDIVDPTLIFKGMASIYAKNV | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 26948
Sequence Length: 252
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
O51477 | MNKPLLSELIIDIGNTSIAFALFKDNQVNLFIKMKTNLMLRYDEVYSFFEENFDFNVNKVFISSVVPILNETFKNVIFSFFKIKPLFIGFDLNYDLTFNPYKSDKFLLGSDVFANLVAAIENYSFENVLVVDLGTACTIFAVSRQDGILGGIINSGPLINFNSLLDNAYLIKKFPISTPNNLLERTTSGSVNSGLFYQYKYLIEGVYRDIKQMYKKKFNLIITGGNADLILSLIEIEFIFNIHLTVEGVRILGNSIDFKFVN | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 29823
Sequence Length: 262
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
Q82S93 | MNTSSLLLAVDSGNTAIKWGLHDGRQWLAHGKTLQSERRMLKQNWTALPAPASILIANVAGLQAADDLKALLAPWHVHLEWATASARQCGVISRYSNPAQLGCDRWVALIAAWHRLQQACLVVDVGTAMTVDALSASGEFLGGVIVPGPDAMRQALADRAGIFSMPLSGSFQNFPINTGNALYSGMIQALTGAVERMYDQLSEYTGKQMVVETILTGGGAALLAPHIHIPHQIVDDLVLEGLVIIAGAQAEIPATR | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27261
Sequence Length: 256
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
Q2Y796 | MNPLLLAVDSGNTRVKWGLHDGRNWLMQGVAAQGDRVQLEREWRDLREPSRVVISNVANAGVKGSLSELLAQWKAEPQWITAVPYQCGVRNYYSNPAQLGSDRWAALVAAWVLERQGCLVVDAGTAMTVDALSDTGEFLGGLITPGLDLMQKILVEDLGSLESEGGKFCDYPDSTADALYSGAVHAMAGAIERMAALLAGTLGHMPECILSGGAAQQLQPQLNVNVKVMDNLVLQGLLAIARETSETASGGVVASPEDSIEN | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27916
Sequence Length: 262
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
Q3JEM4 | MILLVDIGNSRIKWARLDGGKPADMGAVTRGKTGIKRVLSKAWKEFGDVNRVVVANVGGPKVAEQLEQWLQTHWQIAPEFLTARSNGYGIRNAYSKPETLGIDRWLGLVAVRQRYRGGDRKKAICIVDCGTAITLDVLAADGKHLGGLIIPGLAMMPKFLADHTAGINETTEAVEYSLLASTTSAAINAGALYGAVAFIDRVSHDVAVEMKGELKFVITGGDAPRILPLLRDKYEHLPDLVLRGLARVAKDTSKVRRETDLDCAAQ | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 28841
Sequence Length: 266
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
A1SDX1 | MPLLCADIGNSHTVLGLVSGGSVLADWRVATDERNTADDWSVLLRGLLGAALEEIDGIAVCATVPAVLHEWREMLTRHFPAVRHVVVEPGVRTGVPVLMDNPREVGTDRIINALAAVHEYGGPAIVVDFGGTATTFDVVSAQGQYVGGSISPGIELSLESLGRRGAQLRKVELLRPRSVIAKNTVEALQSGMVFGVAAQVEGIVDRMIGELGVGATDVQVIATGYLAPVVLDECRCFTHHAPWLTLRGLELVFERNA | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27360
Sequence Length: 257
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
B2JKK7 | MSTPYLLIDAGNSRVKWALVQADGTQTHSGAFSHGGQLVKGTGDPLQSRHEPDWSALPAPGSAWLSNVAGDAVARRIDAFIDRHWPGLARTTVRSAAQQCGVTNAYTTPSQLGSDRWAGMIGARAAFPGEPLLIATFGTATTLEALTADGVFVGGLIAPGWSLMMRSLGEHTAQLPTLDSTAARGLLDGDNAAGQREPAERGAWFATDTPRSLSSGCALAQIGLIERMWRHLQDEWQVSVRLVVGGGAAGELVQALSVPYTRHDSLVLAGLALIAAQAPVYPSTHTRPV | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 30377
Sequence Length: 289
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
Q4FM76 | MIIVGDIGNTETKICLVNSKNIIIKRVILLTKKINHSSLNKSLLGLNLKNKSINKCLFCSVVPKKFNAVKIFFKKVYKIKCHELKKLNLNKLIKIKVNYKQIGSDRLANAISIINNKDNFIILDFGTATTFDVLIKNTYHGGVIAPGVKLSLDTLTDKASQIPKINLKKTNRVIGLNTISAVRAGFFWGYEGLIDNIVNLIKKETKMSFKIIITGGFSGLFKNSIKTKVTLNKDITIKGLIRATTLIK | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27648
Sequence Length: 248
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
C0QU76 | MILGIDIGNTTSEFGFIYNGKRINSYKLRSDHTKTVDDWLIDISAIFSIEGMKKESVKDCVISSVVPPLEDRIYSACKKFLGKKPLRIGKELKVPIKINYKNPEEVGIDRVVNAFAGVKRYGKPLILVDLGTAITFDVVNQKGEYEGGAIFPGIDSSIEALFSKTAKLPKVSIENVKKVVGKTTVESIQSGIFFGYISLIEGMIKRIIREKGFSPKVILTGGSGEIITKGLEIDHIFDMYLSLEGIYDIYSYHGN | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 28255
Sequence Length: 255
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
A9BIX4 | MELLFDVGNSYTMVGIHQDGKFLTWRIGPSSFESEDGLFVIISNLLNRVNVDLNKITLAGISSVVPNVNFILEQMLKKYFNVEIIFVGTKNKINNIAYLVDYPKEVGADRICNVIACKQEYGDNVIALDFGTAITVDVLEGGNFVGGAIIPGFKTAIGALFSRTAQLPKVEIKIPEYHLGKNTIDNIQIGVIKTTLYGIERLIDEIKRERNKDFVVVATGGDMSFLSSKISIFKHYDPYLTLKGILYYSKEIKKL | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 28441
Sequence Length: 255
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
|
Q97CS1 | MIVVLIGALSIDIIFGEPKEYIHPVVFSGRVASAIEGYFRKFDNRFRAGILFSIAVIVLTAIPYFLAVYLSSFILVVYVVVSMVILKTTFSITSMGEHIKLITDSLKKGNIMEARMHLSMIVRRDTSRLNENEISSAAIESIAEGLVDGYITPLFFFVFFGLPGAFIARIINTLDSMYGYKDRKNFEFGRFSAFMDTVINYIPARISWFFITFSSDILNYRSKAIPVRRYIRRFDSVNAGWPIASMASALNLRLEKKGHYIVNDDGYQPGVADIEKSMKIYYLAAYSYIVIFVLPLLVIMAVFL | Function: Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34484
Sequence Length: 304
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Subcellular Location: Cell membrane
|
P21636 | MAEAGMRKILIIGIGSGNPEHMTVQAINALNCADVLFIPTKGAKKTELAEVRRDICARYVTRKDSRTVEFAVPVRRTEGVSYDGSVDDWHAQIAGIYEALLSKELGEEGTGAFLVWGDPMLYDSTIRIVERVKARGEVAFAYDVIPGITSLQALCASHRIPLNLVGKPVEITTGRRLHESFPEKSQTSVVMLDGEQAFQRVEDPEAEIYWGAYLGTRDEIVISGRVAEVKDRILETRAAARAKMGWIMDIYLLRKGADFDE | Function: Catalyzes the methylation of C-1 in precorrin-5 and the subsequent extrusion of acetic acid from the resulting intermediate to form cobalt-precorrin-6A.
Catalytic Activity: H2O + precorrin-5 + S-adenosyl-L-methionine = acetate + 2 H(+) + precorrin-6A + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28945
Sequence Length: 261
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 5/10.
EC: 2.1.1.152
|
P21637 | MTDLMTSCALPLTGDAGTVASMRRGACPSLAEPMQTGDGLLVRVRPTDDSLTLPKVIALATAAERFGNGIIEITARGNLQLRGLSAASVPRLAQAIGDAEIAIAEGLAIEVPPLAGIDPDEIADPRPIATELREALDVRQVPLKLAPKLSVVIDSGGRFGLGAVVADIRLQAVSTVAGVAWVLSLGGTSTKASSVGTLAGNAVVPALITILEKLASLGTTMRGRDLDPSEIRALCRCETSSERPAAPRSAAIPGIHALGNADTVLGLGLAFAQVEAAALASYLHQVQALGANAIRLAPGHAFFVLGLCPETAAVAQSLAASHGFRIAEQDPRNAIATCAGSKGCASAWMETKGMAERLVETAPELLDGSLTVHLSGCAKGCARPKPSELTLVGAPSGYGLVVNGAANGLPSAYTDENGMGSALARLGRLVRQNKDAGESAQSCLTRLGAARVSAAFEQG | Function: Catalyzes the elimination of C-20 in precorrin-3A to form precorrin-3B.
Catalytic Activity: 2 H(+) + NADH + O2 + precorrin-3A = H2O + NAD(+) + precorrin-3B
Sequence Mass (Da): 46691
Sequence Length: 459
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 2/10.
EC: 1.14.13.83
|
P63840 | MLDYLRDAAEIYRRSFAVIRAEADLARFPADVARVVVRLIHTCGQVDVAEHVAYTDDVVARAGAALAAGAPVLCDSSMVAAGITTSRLPADNQIVSLVADPRATELAARRQTTRSAAGVELCAERLPGAVLAIGNAPTALFRLLELVDEGAPPPAAVLGGPVGFVGSAQAKEELIERPRGMSYLVVRGRRGGSAMAAAAVNAIASDRE | Function: Catalyzes the conversion of precorrin-8X to hydrogenobyrinate.
Catalytic Activity: 3 H(+) + precorrin-8X = hydrogenobyrinate
Sequence Mass (Da): 21614
Sequence Length: 208
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 8/10.
EC: 5.4.99.61
|
Q9HZU2 | MIDYIRDGQAIYRQSFATIRAEANLAGIPADLEKLAVRVIHACGMVDVVDDLRFSPGAGAAGRAALAAGAAILCDARMVAEGVTRSRLPAANRVICTLNEADVPALATELGNTRSAVALEHWREHLEGSVVVIGNAPTALFYLLEMLDAGAPKPALILGFPVGFVGAAESKEMLAADSRGVPYVIVRGRRGGSAMAAAAVNALATERE | Function: Catalyzes the conversion of precorrin-8X to hydrogenobyrinate.
Catalytic Activity: 3 H(+) + precorrin-8X = hydrogenobyrinate
Sequence Mass (Da): 21650
Sequence Length: 208
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 8/10.
EC: 5.4.99.61
|
P21638 | MPEYDYIRDGNAIYERSFAIIRAEADLSRFSEEEADLAVRMVHACGSVEATRQFVFSPDFVSSARAALKAGAPILCDAEMVAHGVTRARLPAGNEVICTLRDPRTPALAAEIGNTRSAAALKLWSERLAGSVVAIGNAPTALFFLLEMLRDGAPKPAAILGMPVGFVGAAESKDALAENSYGVPFAIVRGRLGGSAMTAAALNSLARPGL | Function: Catalyzes the conversion of precorrin-8X to hydrogenobyrinate.
Catalytic Activity: 3 H(+) + precorrin-8X = hydrogenobyrinate
Sequence Mass (Da): 22064
Sequence Length: 210
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 8/10.
EC: 5.4.99.61
|
P66878 | MSARGTLWGVGLGPGDPELVTVKAARVIGEADVVAYHSAPHGHSIARGIAEPYLRPGQLEEHLVYPVTTEATNHPGGYAGALEDFYADATERIATHLDAGRNVALLAEGDPLFYSSYMHLHTRLTRRFNAVIVPGVTSVSAASAAVATPLVAGDQVLSVLPGTLPVGELTRRLADADAAVVVKLGRSYHNVREALSASGLLGDAFYVERASTAGQRVLPAADVDETSVPYFSLAMLPGGRRRALLTGTVAVVGLGPGDSDWMTPQSRRELAAATDLIGYRGYLDRVEVRDGQRRHPSDNTDEPARARLACSLADQGRAVAVVSSGDPGVFAMATAVLEEAEQWPGVRVRVIPAMTAAQAVASRVGAPLGHDYAVISLSDRLKPWDVIAARLTAAAAADLVLAIYNPASVTRTWQVGAMRELLLAHRDPGIPVVIGRNVSGPVSGPNEDVRVVKLADLNPAEIDMRCLLIVGSSQTRWYSVDSQDRVFTPRRYPEAGRATATKSSRHSD | Function: Methylates precorrin-2 at the C-20 position to produce precorrin-3A.
Catalytic Activity: precorrin-2 + S-adenosyl-L-methionine = H(+) + precorrin-3A + S-adenosyl-L-homocysteine
Sequence Mass (Da): 53911
Sequence Length: 508
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 1/10.
|
Q9HZU3 | MMSVVKGRLLGLGVGPGDPELITLKALRLLRAAPVVGYFVAKGKKGNAFGIIEAHLDQAQVRLPLVYPVTTEKLEPPLCYETIISDFYDTAAEQLAAHLDAGRDVAVICEGDPFFYGSYMYLHDRLATRYESEVVPGVCSMLGGAAVLGAPLVYRNQSLSVLSGVLPEEELRRRLADADAAVVMKLGRNFDKVRRVLVELGLERRALYVERATMANQRIVPLERVEPMASPYFSLIVVPGDKWQGGAGGE | Function: Methylates precorrin-2 at the C-20 position to produce precorrin-3A.
Catalytic Activity: precorrin-2 + S-adenosyl-L-methionine = H(+) + precorrin-3A + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27275
Sequence Length: 250
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 1/10.
EC: 2.1.1.130
|
P21639 | MSGVGVGRLIGVGTGPGDPELLTVKAVKALGQADVLAYFAKAGRSGNGRAVVEGLLKPDLVELPLYYPVTTEIDKDDGAYKTQITDFYNASAEAVAAHLAAGRTVAVLSEGDPLFYGSYMHLHVRLANRFPVEVIPGITAMSGCWSLAGLPLVQGDDVLSVLPGTMAEAELGRRLADTEAAVIMKVGRNLPKIRRALAASGRLDQAVYVERGTMKNAAMTALAEKADDEAPYFSLVLVPGWKDRP | Function: Methylates precorrin-2 at the C-20 position to produce precorrin-3A.
Catalytic Activity: precorrin-2 + S-adenosyl-L-methionine = H(+) + precorrin-3A + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25895
Sequence Length: 245
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 1/10.
EC: 2.1.1.130
|
P21640 | MTGTLYVVGTGPGSAKQMTPETAEAVAAAQEFYGYFPYLDRLNLRPDQIRVASDNREELDRAQVALTRAAAGVKVCMVSGGDPGVFAMAAAVCEAIDKGPAEWKSVELVITPGVTAMLAVAARIGAPLGHDFCAISLSDNLKPWEVITRRLRLAAEAGFVIALYNPISKARPWQLGEAFELLRSVLPASVPVIFGRAAGRPDERIAVMPLGEADANRADMATCVIIGSPETRIVERDGQPDLVYTPRFYAGASQ | Function: Methyltransferase that catalyzes the methylation of C-17 in precorrin-3B to form precorrin-4.
Catalytic Activity: precorrin-3B + S-adenosyl-L-methionine = 3 H(+) + precorrin-4 + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27105
Sequence Length: 254
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 3/10.
EC: 2.1.1.131
|
P9WP88 | MTRVLLLGGTAEGRALAKELHPHVEIVSSLAGRVPNPALPIGPVRIGGFGGVEGLRGWLREERIDAVVDATHPFAVTITAHAAQVCGELGLPYLVLARPPWDPGTAIIAVSDIEAADVVAEQGYSRVFLTTGRSGIAAFANSDAWFLIRVVTAPDGTALPRRHKLVLSRGPYGYHDEFALLREQRIDALVTKNSGGKMTRAKLDAAAALGISVVMIARPLLPAGVAAVDSVHRAAMWVAGLPSR | Function: Catalyzes the reduction of the macrocycle of precorrin-6X into precorrin-6Y.
Catalytic Activity: NADP(+) + precorrin-6B = 2 H(+) + NADPH + precorrin-6A
Sequence Mass (Da): 25737
Sequence Length: 244
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 6/10.
EC: 1.3.1.54
|
Q89Q75 | MIPGTETIRNVIADLRIAASFVTLLPVGSSKPAADGAIARATWALPVAGLLVGLAGALVYKISSRLGLTPNLAALLALATTALITGALHEDGLADTADGLGGGRTRERKLEIMRDSRIGTYGVCALILSFGLRWSALAAIANPWLVTLALCAAHCAARAGVPAFMSLVPPARPDGLSASAGAPPGRSVAIAFAVGTLVLTLALGPGKALVGLILLSLAGLILARLAIRQIGGQTGDILGAFEQTGEIVILLVAAAFQMGR | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26251
Sequence Length: 260
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell inner membrane
EC: 2.7.8.26
|
C0Z7H6 | MNAFLHAISFFTRIPVPWLRPSEEAWRKSVNWYPAVGLVIGLLLWGVHQAGLVLFSPWIAAILTLIAWVYVTGGLHMDGWMDLADGLGSSRPREQILAIMKDSRVGAMGVLAAIMLLLIKAGAVAELAHPGWGSFLIVAPVAARTHVLLSIKLWPYLSADKGIGKGISSGLSVSSIIVSYIIVFAAGWYLGGLQVMTAIFLSLLFALWFSRSVAKKLGGLNGDCYGAVIESSEAVVLLVLVGSWWL | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26515
Sequence Length: 246
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell membrane
EC: 2.7.8.26
|
A6X1H1 | MQRNSLIGDTIRSLGFLSRLPLPQRWFEDGDDSLPRNARAFPLAGAVLGLLAGAVLFMAYKVNLPPLACAMLAIGALAAMTGALHEDGLGDTADGFFGASSPDRRLDIMKDSRIGTFAALTLIVFVGLKAALLMTIIDRAGAGYAALALVGCEAASRSGMLAFWHALPSARPGGLSDSVGQPQWETVVCGFGIGLAFLVFTLIPAGGFLSLINALVLATGLLFGFARLCIAKIGGQTGDTLGAAQQIGSVAVLAGLVMAL | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26734
Sequence Length: 260
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell inner membrane
EC: 2.7.8.26
|
Q8RCN8 | MEELKALILSIQFMTGIPIPINIDVKEDKIYKIASYFPVVGLLIGGILYIAYLLLKDLFSREIVMTFLVAFSYILTRGMHIDGLADTFDGLFSNKDREKIIEIMKDSRLGTNGVLALVFMVILKILFLSDIRQSLLFSALLVSPVIARLSVVFSIAISKSARGGKGLGGLLLERAGLREFVIALLISTIAGYFVMPLKDLALLYVISLSFTCLISKYISKKIGGMTGDTLGAVNEFVELIAFIYFSIL | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27351
Sequence Length: 248
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell membrane
EC: 2.7.8.26
|
Q3AE01 | MLTTFLLGLTFFTRIPVPGKLNFSEEKFNRAPIFLPAYGLVTGGILALIIELFGRSFPGFFWAGVIIAGQIYLSGALHIDGLLDSLDAIYSNRDREKRLEILKDSRVGSMAVAFFGAFLILKYGSYASFTPKVQAFTVLISEIILRGTGYLVIYSFPYVGSSLGRGFKDNASTAGLIFTLGQTLIFTLGAAAFFNFSLIKILIILLLAYLFAFVVAARWQQFFGGLTGDNYGGIMELTGLFVPVAVLLINNIGVV | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27809
Sequence Length: 255
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell membrane
EC: 2.7.8.26
|
Q8KDU6 | MLSGLVTALRTLTALPVPGRDAERFSSSLYWFPVVGLVIGGIVVLLARAGMGVGWPELAAVLALLGGLILTRGLHADGLADLADGFFGGRTREAALRIMKDPNVGSFGSLALIGVMLFKWICLLELARAEAYGMIAAGAVLSRTAQVLLAARMPYARSDGGTAMAFVEDAGWPHLLVASISGVVLLFVLLDWQLAPSLILLFGSVVALFFVGWLSHRKIGGITGDVLGACSELVEAAVWLLAALWLKGLFWAIA | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26727
Sequence Length: 254
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell inner membrane
EC: 2.7.8.26
|
B0KCS0 | MEEIKRLVLAMQFMTRLPIPIEIDVEKREFYRIASYFPIVGIVIGGILSLLYIALKDFFSREIVMTFIVAFSYVLTGAMHIDGLADTFDGLFSNKDKSKMLEIMRDSRLGTNGVLAAIFIVVLKILFLTNIHENITLTALLITPIIGRLSIVFSMMISKSARGGEGLGGLMLGKVGIREFAIAFVISIATSYFILPLAVFVKILTISLFVTYIVSKYISLRIGGMTGDTLGAVNELAELTALICFVSVSL | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27523
Sequence Length: 250
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell membrane
EC: 2.7.8.26
|
Q8DJ91 | MKSLWQEWLGAIAFYTCLPISPRWPIQLAGAAKWCPWVGLVLGGMLWGVQWLLDFLQVPSPVASAVLVALWLALTGGLHLDGAMDTADGLAVRDQQRRLEVMADSRAGAFGVMAAMVILLLKVTSLSSLEKGSVLVWVLVLGRLAQVWAIARYPYLKPQGTGQIHKTSGVFPRDFWPSGLLVLLLSFLLPLPLGQLLFGLLLILLIPAWFQSQLGGHTGDSYGAVVEWTEALLLVAFTVGSAS | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26329
Sequence Length: 243
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell inner membrane
EC: 2.7.8.26
|
Q97BG1 | MMISGLRSSFSFFTLVPSRQKDIGNPITFLPLVVTVGALIGDSILYITWQFSHLIASFLSISSIIIYNGLNHFDATADLGDALMVRDKSRIPEVIKDHHVGAGGIFAVIFVYGIAVLSLARSTLYIGLVGILIGQVVSGSSMMISLIGSQPFVPGLADYFISLFRKHSVGYTIEFLAIPIIVSFIFSPLYVVIVALNLLIVQLTKTMISRRFGGINGDVIGFLGEFSRSLFIFMLIIIAHYNVASTYDIFSKMLSSFTS | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28310
Sequence Length: 259
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell membrane
EC: 2.7.8.26
|
B5YL84 | MINRFLIALSFLTVLPLKFKEINEKELIRSIIFFPFIGFLEGVFCIFLVNIFKQIFSSSVISIILLVFLFSVRGIFHIDGLSDTFDALFYKGTGQKEKDLQQRLQIMKDSVIGVAGAVALVLDVLCRFAFVKELIDINQFLIFLFMFCFSRWIVIPLMYYGKPARTTGLGVLFIGKISSWQVIISTVLPIFLLVYFTIEKNFIFLPLIALFLFFISYILKKFFERKFNGITGDHLGATVEITEIVFLICFLLGEKLWLSY | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29998
Sequence Length: 260
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell inner membrane
EC: 2.7.8.26
|
Q3SFE7 | MRGLILALGFLTRLPLPVLRDFQCAELVRAVVWFPAAGLVVGAAVALAAALGTVLDPWLGALAGVVMWAWITGGLHLDGLADTADALGAAHRDPARFLTVLADPHVGSFGVIVLVLQLAAKLVLLHWLLTLDLPWPALVLIPAWTRWAAAGWTLLLPPLKPGLGERFAWQGNRAGWGAGGLALAAVSAITPIAFVALIPAVLWGVWMWLKLGGQTGDILGAGIEWSESAALLLAGVSLALARGIIAG | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25699
Sequence Length: 247
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell inner membrane
EC: 2.7.8.26
|
Q73K39 | MKGFILALQFFTRIPININIDFNEKNIKRAFYFLPLIGGLIAGLVLIPIYFLPQKYIEISGFISLLLYLFLTGSIHLDGVGDTIDGFFSARKKEKILEIMQDPRIGTYGTIGLNVFLLLRYINYSTIIPDAGLLILAGIISRLSGLAVVVFSKPAKDTGLGLLFHKSASKFSFFFWLVLVCFLSLFTPEIAAFSKIQGTFILVERLKYLLLPLTAFILTFIIIRISYKKIGGITGDVNGLIVELTELAVLSTSFFINVHL | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29031
Sequence Length: 260
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell inner membrane
EC: 2.7.8.26
|
A5F1U5 | MAAILRYQLELFLLAVSFFSRIPVPVSLPYSSERMNQAGRYFALVGLLLGAICALVYSLATQLFSTNISVFLTMVLSLLLTGAFHEDGLADMADGVGGGMTAERRLEIMKDSRIGTYGSSALIMVLLGKYLLLTELADLTSLVPVWLLAYTLSRAVAASLIRNTPYVSDTDSSKSKPLAQQLSGTDVAVLSLTALATLLYFSWQFIGVMIAASLIFRQIFRQWLIRRLGGFTGDCLGAAQQLMEILIYLILLAFLQHEVMI | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28593
Sequence Length: 261
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell inner membrane
EC: 2.7.8.26
|
Q8D922 | MKTWQYQYQLFCLAVSFFSRLPVPKSTPYSDERMNQAGRYFALVGTLLGLLCVLVYAFASLFFPYQVAIVLMMAFSLLLTGAFHEDGLTDMADGIGGGMTLDKRLTIMKDSRIGTYGSATLTMALIGKFVFLTTLARQPDFGLMIVVAYTLSRAVAATLIYDMPYVSDSDTSKSKPLANAQSSTELAILILTGVLAAISLGLGVGLLLILFAILFRWAFKRWLLARLGGFTGDCLGGAQQLMELGIYLVLIAVVQ | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27797
Sequence Length: 255
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell inner membrane
EC: 2.7.8.26
|
A7IB66 | MQLDRIAQDLVAALRFYSRLPLPAGRDDPDAFAVPSLNRIAYAIPLAGAVIGLIGAVVLVGALALKLPAFLASVLAVTALVLTTGAFHEDGLADTADGLGGGRDKAQRLAIMRDSRIGTYGGCALILALLLRVAALEALVASAGMFRAALALVVAEAASRAAGVLLLLALPPARADGAGASFGRPSESAGLACALVAALLVVVILVPGFGISTAFAGLIAPLVALFAMMRLSGRLIGGQTGDVAGATQQVAVIVFLLGVLIFPGR | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26639
Sequence Length: 265
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell inner membrane
EC: 2.7.8.26
|
A3DF00 | MLFQTLKSIGELYKEPMDMVQRRLDSLSKPLGSLGRLEDIIKKLAGITGEVFPCVDKKAVIIMCADNGVVEEGISSCPKDVTSKVTRNFLKGITAINAFAKHTGSDIVVVDIGVDDDMDCEGIVKRKVRKGTWNIAKGPAMTRKEAIEAIEVGISIVEELGRKGVNLLGTGEMGIGNTTTSSAVSTVLTDSKAENMVGRGAGLSDEALKRKISIVKKAIDLNRPDANDPIDVVSKVGGFDIAGLAGCFIGAAACRIPILIDGFISATAALAAVRMEPKVKNFIFPSHGSAEPGSKKVMEALGFEPILNLEMRVGEGTGAALAFHIFDCAVSVYRNMGTFEDACIEQYQPQV | Function: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Mass (Da): 37352
Sequence Length: 351
Pathway: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 1/2.
EC: 2.4.2.21
|
A6TKH4 | MNKLKETIRMIEELDQETMQKARERVDNLIKPPKSLGRLEDLAVQLAGITKTIHPTVANKAIIVMAADHGVYEEGIAGFPQEITVVQTLNFVKGVTGVCALGKVSGTKIIPVDIGVKEDLDPNAGVLIRKIKYGTDNMAKGPAMSREEAIRALEVGIEVANEEIKNGVTLLGTGEMGIGNTTASTAILSVLGNFDPKEITGRGAGLSPEGIQRKAAVIKRAIEVNQPDATDGIDVVAKVGGLEIAGMAGVMLAAAANRIPVVVDGYIATAAALIAVSLEPKTKQYLIPSHASAEIGSIKATELLGIKPMIHMDLCLGEGSGAALVFPIVEAACHMINCMPTFEEAGITI | Function: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Mass (Da): 36603
Sequence Length: 349
Pathway: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 1/2.
EC: 2.4.2.21
|
Q82AM7 | MSSLNLDDFSDLIERPDGGVRRDAEARRERQIVPPGSLGRLDDLGEWLAAAQSAVPVRPVERPRVVLFAGDHGVASLGVSARPAGSADQLVRAVLEGASPASILARRLNVPVRVVDMALDCEPDALPESVVRHRVRRGSGRIDVEDALTLEEAEAAFRAGVAVADEEADAGTDLVVLGDVSVGGTTAAAVLIAALCGTDASVVTGRGGLAIDDLAWMRKCAAVRDALRRARPVLGDQLQLLAAVGGADLAAMTGFLLQSAARKTPVILDGVVSAACALVGQRIAFRAPDWWLAGQNSGEPAQAKALDRMALEPLLNHGVTVGEGAGALLALPLVQAAAALAAELPEKPEELEAGEGPEAAEESSPEPENPEALAE | Function: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Mass (Da): 38743
Sequence Length: 375
Pathway: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 1/2.
EC: 2.4.2.21
|
A0LF21 | MEKLDRLLERIEPASKDWEAKAWERLHAQIRPRDSLGRLEVIAARLAAIKRSLTPAVGRKIIFTMAGDHGVAAEGVSAYPQEVTAQMVGSFVRGWASINILAVHCGAAVRVVDCGVASDLPPDWPVLRRKLGKGTANIAVGPAMSREVAVRGLTIGAEIVQDAHLKEGYLLFGTGDMGIGNTTPSTAIIAALGGKPVRDLTGRGTGIDDVAFERKVRVIERALAVNRPDPNDPLGVLAGVGGFEIAALGGAVLGAAALRVPIICDGFIATAGALVACRLAPKAADYLFVSHRSREVGHTAMVDMLGMRPILDLDMRLGEGTGSALAMNIVEAAAKVLVECKTFEEAGVTDTGH | Function: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Mass (Da): 37072
Sequence Length: 353
Pathway: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 1/2.
EC: 2.4.2.21
|
Q7SIC7 | MDPEVFAQARLRMDQLTKPPRALGYLEEVALRLAALQGRVKPELGRGAVVVAAADHGVVAEGVSAYPQEVTRQMVLNFLRGGAAINQFALAADCAVYVLDVGVVGELPDHPGLLKRKVRPGTANLAQGPAMTPEEAERALLAGREAARRAIAEGATLLAAGDMGIGNTTAAAALTAALLGLPPEAVVGRGTGVGEEGLRRKRQAVARALARLHPGMGPLEVAAEVGGLELVAIAGIYLEGYEAGLPLVLDGFPVTAGALLAWKMAPGLRDHLFAGHLSREPGHRHQLEALGLRPLLDLDLALGEGTGAVLAMPLLRAAARILHMATFQEAGVSRG | Function: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Mass (Da): 34747
Sequence Length: 335
Pathway: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 1/2.
EC: 2.4.2.21
|
C5CKN8 | MTDSNQTIPSISDIHDGALAARLQSALDNKTKPLGALGRLESLALRIGLVLGSETPVLEAPQMLVCAADHGLAARGVSAFPSDVTWQMVENFLAGGAAVSVLALQHGLALTVVDCGVRRDFQARPGLVSRRIAAGTADASAGPAMTAEQCAQAIANGREVVRALPGNALLLGEMGIGNSSAAALLLARLAGLDIDGCTGSGTGLDAAGLARKREVLRDVLALHAAASEPLDALAAFGGFEIATLVGAVLQAAQERRVIVIDGFIASAAVLVAQALQPHVAQRCVAAHSSAEPGHALLLKHLGLEPLLNLDLRLGEGSGGALAWPLLESACRILREMASFEAAGVSRKDS | Function: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Mass (Da): 35615
Sequence Length: 349
Pathway: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 1/2.
EC: 2.4.2.21
|
Q9KSL9 | MLDRSFSAEIQQRIDQKTKPLGALGQLERVAHHLALIQSQNQDQAVTQLAIHQPTVLVFAADHGIAAQGVSIAPSAVTEQMVQNFLAGGAAINCFCRTEHAAMRVIDCGILRAQPAHADLIEQRLGAGTHNLAEQAAMSSEQVQEGIALGKALIHREVESGCNLLMFGEMGIGNTSSAAAILAALSGLPIEVCVGRGTGITDEQYQRKRALVTQGVERCLGAAPQDVLQQVGGFEIVQMVGAFMGAYEKQTPVLVDGFIVTVAAYVATLIEPNVRDFLLFAHCSQETGHRAVLEMLAAEPLLDLGLRLGEGTGAVLALGLVRAAVEFYNHMASFADAGVTV | Function: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Mass (Da): 36084
Sequence Length: 341
Pathway: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 1/2.
EC: 2.4.2.21
|
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