ID   COBT_SALPC              Reviewed;         356 AA.
AC   C0Q1R0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=SPC_1699;
OS   Salmonella paratyphi C (strain RKS4594).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=476213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKS4594;
RX   PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA   Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA   Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT   "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT   and pathogenic convergence with Salmonella typhi.";
RL   PLoS ONE 4:E4510-E4510(2009).
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; CP000857; ACN45846.1; -; Genomic_DNA.
DR   RefSeq; WP_001193975.1; NC_012125.1.
DR   AlphaFoldDB; C0Q1R0; -.
DR   SMR; C0Q1R0; -.
DR   EnsemblBacteria; ACN45846; ACN45846; SPC_1699.
DR   KEGG; sei:SPC_1699; -.
DR   HOGENOM; CLU_002982_0_0_6; -.
DR   OMA; AIWYAGW; -.
DR   UniPathway; UPA00061; UER00516.
DR   Proteomes; UP000001599; 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..356
FT                   /note="Nicotinate-nucleotide--dimethylbenzimidazole
FT                   phosphoribosyltransferase"
FT                   /id="PRO_1000125113"
FT   ACT_SITE        317
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00230"
SQ   SEQUENCE   356 AA;  36559 MW;  800405FD7AEB6295 CRC64;
     MQTLHALLRD IPAPDAEAMA RAQQHIDGLL KPPGSLGRLE TLAVQLAGMP GLNGTPQVGE
     KAVLVMCADH GVWDEGVAVS PKIVTAIQAA NMTQGTTGVC VLAAQAGAKV HVIDVGIDAE
     PIPGVVNMRV ARGCGNIAVG PAMSRSQAEA LLLEVSRYTC DLAQRGVTLF GVGELGMANT
     TPAAAMVSVF TGSDAKEVVG IGANLPPSRI DNKVDVVRRA IAINQPNPRD GIDVLSKVGG
     FDLVGMTGVM LGAARCGLPV LLDGFLSYSA ALAACQIAPA VRPYLIPSHF SAEKGARIAL
     AHLSMEPYLH MAMRLGEGSG AALAMPIVEA ACAMFHNMGE LAASNIVLPE GNANAT