ID   COBT_ECOHS              Reviewed;         359 AA.
AC   A8A1K5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00230};
DE            Short=NN:DBI PRT {ECO:0000255|HAMAP-Rule:MF_00230};
DE            EC=2.4.2.21 {ECO:0000255|HAMAP-Rule:MF_00230};
DE   AltName: Full=N(1)-alpha-phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00230};
GN   Name=cobT {ECO:0000255|HAMAP-Rule:MF_00230}; OrderedLocusNames=EcHS_A2114;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
CC   -!- FUNCTION: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from
CC       nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
CC       {ECO:0000255|HAMAP-Rule:MF_00230}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide =
CC         alpha-ribazole 5'-phosphate + H(+) + nicotinate;
CC         Xref=Rhea:RHEA:11196, ChEBI:CHEBI:15378, ChEBI:CHEBI:15890,
CC         ChEBI:CHEBI:32544, ChEBI:CHEBI:57502, ChEBI:CHEBI:57918; EC=2.4.2.21;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00230};
CC   -!- PATHWAY: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-
CC       ribazole from 5,6-dimethylbenzimidazole: step 1/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00230}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00230}.
CC   -!- SIMILARITY: Belongs to the CobT family. {ECO:0000255|HAMAP-
CC       Rule:MF_00230}.
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DR   EMBL; CP000802; ABV06409.1; -; Genomic_DNA.
DR   RefSeq; WP_001193781.1; NC_009800.1.
DR   AlphaFoldDB; A8A1K5; -.
DR   SMR; A8A1K5; -.
DR   KEGG; ecx:EcHS_A2114; -.
DR   HOGENOM; CLU_002982_0_0_6; -.
DR   OMA; AIWYAGW; -.
DR   UniPathway; UPA00061; UER00516.
DR   Proteomes; UP000001123; Chromosome.
DR   GO; GO:0008939; F:nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd02439; DMB-PRT_CobT; 1.
DR   Gene3D; 1.10.1610.10; -; 1.
DR   Gene3D; 3.40.50.10210; -; 1.
DR   HAMAP; MF_00230; CobT; 1.
DR   InterPro; IPR003200; Nict_dMeBzImd_PRibTrfase.
DR   InterPro; IPR017846; Nict_dMeBzImd_PRibTrfase_bact.
DR   InterPro; IPR023195; Nict_dMeBzImd_PRibTrfase_N.
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; Glycosyltransferase; Transferase.
FT   CHAIN           1..359
FT                   /note="Nicotinate-nucleotide--dimethylbenzimidazole
FT                   phosphoribosyltransferase"
FT                   /id="PRO_1000058765"
FT   ACT_SITE        318
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00230"
SQ   SEQUENCE   359 AA;  36925 MW;  F8F54BDA8BE2983A CRC64;
     MQTLADLLNT IPAIDPAAMS RAQRHIDGLL KPVGSLGRLE ALAIQLAGMP GLNGIPHVGK
     KAVLVMCADH GVWEEGVAIS PKEVTAIQAE NMTRGTTGVC VLAAQAGANV HVVDVGIDSA
     EPIPGLINMR VARGSGNIAS APAMSRRQAE KLLLDVICYT RELAKNGVTL FGVGELGMAN
     TTPAAAIVST ITGRDPEEVV GIGANLPTDK LANKIDVVRR AITLNQPNPQ DGIDVLAKVG
     GFDLVGIAGV MLGAASCGLP VLLDGFLSYA AALAACQMSP AIKPYLIPSH LSVEKGARIA
     LSHLGLEPYL NMDMRLGEGS GAALAMPIIE AACAIYNNMG ELAASNIVLP GNTTSDLNS