ID   COBT_MYCTO              Reviewed;         361 AA.
AC   P9WP84; L0T8X8; P63841; Q10396;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase;
DE            Short=NN:DBI PRT;
DE            EC=2.4.2.21;
DE   AltName: Full=N(1)-alpha-phosphoribosyltransferase;
GN   Name=cobT; OrderedLocusNames=MT2263;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from
CC       nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
CC       {ECO:0000250}.
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   -!- PATHWAY: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-
CC       ribazole from 5,6-dimethylbenzimidazole: step 1/2.
CC   -!- SIMILARITY: Belongs to the CobT family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK46549.1; -; Genomic_DNA.
DR   PIR; H70785; H70785.
DR   RefSeq; WP_003411429.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WP84; -.
DR   SMR; P9WP84; -.
DR   EnsemblBacteria; AAK46549; AAK46549; MT2263.
DR   GeneID; 45426183; -.
DR   KEGG; mtc:MT2263; -.
DR   PATRIC; fig|83331.31.peg.2438; -.
DR   HOGENOM; CLU_002982_0_2_11; -.
DR   UniPathway; UPA00061; UER00516.
DR   Proteomes; UP000001020; 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..361
FT                   /note="Nicotinate-nucleotide--dimethylbenzimidazole
FT                   phosphoribosyltransferase"
FT                   /id="PRO_0000426996"
FT   ACT_SITE        314
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   361 AA;  36411 MW;  F3BF44AB70227A1F CRC64;
     MIGFAPVSTP DAAAEAAARA RQDSLTKPRG ALGSLEDLSV WVASCQQRCP PRQFERARVV
     VFAGDHGVAR SGVSAYPPEV TAQMVANIDA GGAAINALAD VAGATVRVAD LAVDADPLSE
     RIGAHKVRRG SGNIATEDAL TNDETAAAIT AGQQIADEEV DAGADLLIAG DMGIGNTTAA
     AVLVAALTDA EPVAVVGFGT GIDDAGWARK TAAVRDALFR VRPVLPDPVG LLRCAGGADL
     AAIAGFCAQA AVRRTPLLLD GVAVTAAALV AERLAPGAHR WWQAGHRSSE PGHGLALAAL
     GLDPIVDLHM RLGEGTGAAV ALMVLRAAVA ALSSMATFTE AGVSTRSVDG VDRTAPPAVS
     P