ID A0A2D7NQ86_9DELT Unreviewed; 339 AA. AC A0A2D7NQ86; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 23-MAY-2018, entry version 2. DE RecName: Full=Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00230, ECO:0000256|SAAS:SAAS00726629}; DE Short=NN:DBI PRT {ECO:0000256|HAMAP-Rule:MF_00230}; DE EC=2.4.2.21 {ECO:0000256|HAMAP-Rule:MF_00230, ECO:0000256|SAAS:SAAS00726625}; DE AltName: Full=N(1)-alpha-phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00230}; GN Name=cobT {ECO:0000256|HAMAP-Rule:MF_00230, GN ECO:0000313|EMBL:MAJ49090.1}; GN ORFNames=CL937_05215 {ECO:0000313|EMBL:MAJ49090.1}; OS Deltaproteobacteria bacterium. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=2026735 {ECO:0000313|EMBL:MAJ49090.1}; RN [1] {ECO:0000313|EMBL:MAJ49090.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MED631 {ECO:0000313|EMBL:MAJ49090.1}; RA Tully B.J., Graham E.D., Heidelberg J.F.; RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from RT the Global Oceans."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of alpha-ribazole-5'-phosphate CC from nicotinate mononucleotide (NAMN) and 5,6- CC dimethylbenzimidazole (DMB). {ECO:0000256|HAMAP-Rule:MF_00230, CC ECO:0000256|SAAS:SAAS00726623}. CC -!- CATALYTIC ACTIVITY: Beta-nicotinate D-ribonucleotide + 5,6- CC dimethylbenzimidazole = nicotinate + alpha-ribazole 5'-phosphate. CC {ECO:0000256|HAMAP-Rule:MF_00230, ECO:0000256|SAAS:SAAS00726632}. CC -!- PATHWAY: Nucleoside biosynthesis; alpha-ribazole biosynthesis; CC alpha-ribazole from 5,6-dimethylbenzimidazole: step 1/2. CC {ECO:0000256|HAMAP-Rule:MF_00230, ECO:0000256|SAAS:SAAS00726628}. CC -!- SIMILARITY: Belongs to the CobT family. {ECO:0000256|HAMAP- CC Rule:MF_00230, ECO:0000256|SAAS:SAAS00726624}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:MAJ49090.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; NZHX01000074; MAJ49090.1; -; Genomic_DNA. DR UniPathway; UPA00061; UER00516. DR CDD; cd02439; DMB-PRT_CobT; 1. DR Gene3D; 1.10.1610.10; -; 2. DR HAMAP; MF_00230; CobT; 1. DR InterPro; IPR003200; Nict_dMeBzImd_PRibTrfase-like. DR InterPro; IPR023195; Nict_dMeBzImd_PRibTrfase_N. DR InterPro; IPR017846; Nict_dMeBzImd_PRibTrfase_pro. DR InterPro; IPR036087; Nict_dMeBzImd_PRibTrfase_sf. DR Pfam; PF02277; DBI_PRT; 1. DR SUPFAM; SSF52733; SSF52733; 1. DR TIGRFAMs; TIGR03160; cobT_DBIPRT; 1. PE 3: Inferred from homology; KW Cobalamin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00230, KW ECO:0000256|SAAS:SAAS00726630}; KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00230, KW ECO:0000256|SAAS:SAAS00726626, ECO:0000313|EMBL:MAJ49090.1}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00230, KW ECO:0000256|SAAS:SAAS00726622, ECO:0000313|EMBL:MAJ49090.1}. FT DOMAIN 2 333 DBI_PRT. {ECO:0000259|Pfam:PF02277}. FT ACT_SITE 304 304 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00230}. SQ SEQUENCE 339 AA; 35948 MW; 23EC4BA103B024ED CRC64; MNEELASPLQ SKVDGKTKPP GSLGDLEQLA LRIGLIQGTL EPQLKSPTML VFAGDHGITK EGVSPYPSEV TAQMVXNFLS GGAAINVFCR QHGXDLKVID AGVASDFEKH PLLVDEKIAX GTANFXXEKA MSENQAKECI SRGEKXAEEL PDXSCNVIGF GXMGIGNTSS SALXMHRXXG IXXESCVGRG TGLDDQGLSH KXXVLQEASE IHSGARGXIX VIAAFGGFEI AMMCGAMIAS SRXXRILLID GFXASTALLL AREMDPKVMD HAVFTHVSGE QGHRXLLEHL QVKPLLDLXL RLGEGTGAXL AYPLLVSAVA FXNXMASFES AGVSDRXDA //