ID   COBT_MYCLE              Reviewed;         351 AA.
AC   O32953;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 130.
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=ML0868; ORFNames=MLCB22.08;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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; Z98741; CAB11373.1; -; Genomic_DNA.
DR   EMBL; AL583920; CAC31249.1; -; Genomic_DNA.
DR   PIR; T44886; T44886.
DR   RefSeq; NP_301655.1; NC_002677.1.
DR   AlphaFoldDB; O32953; -.
DR   SMR; O32953; -.
DR   STRING; 272631.ML0868; -.
DR   EnsemblBacteria; CAC31249; CAC31249; CAC31249.
DR   KEGG; mle:ML0868; -.
DR   PATRIC; fig|272631.5.peg.1597; -.
DR   Leproma; ML0868; -.
DR   eggNOG; COG2038; Bacteria.
DR   HOGENOM; CLU_002982_0_2_11; -.
DR   OMA; AWMRKCA; -.
DR   UniPathway; UPA00061; UER00516.
DR   Proteomes; UP000000806; 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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..351
FT                   /note="Nicotinate-nucleotide--dimethylbenzimidazole
FT                   phosphoribosyltransferase"
FT                   /id="PRO_0000167055"
FT   ACT_SITE        313
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   351 AA;  36017 MW;  919231520D5FE2A0 CRC64;
     MEFAPVSPPD GHAAAAARAR QDTLTKPRGA LGRLEDLSIW VASCQGQCPP RQFQRARIVV
     FAGDHGVARS GVSAYPPQLT AQMVANIDRG GAAINALASI ADATIRIADL AVDADPLSQQ
     IGIHKVRRGS GDIAIQDALT EDETARAIIA GQRIADEEVD RGADLLIAGD IGIGNTTAAA
     VLVAALTNAE PVAVVGFGTG IDDASWARKT AAVRDALCRI RLVLPDPVGL LRCCGGADLA
     AMAGFCAQAA VRRTPLLLDG MVVTAAALVA ERLAPGSWQW WQAGHQSTEP GHALALAALD
     LDPILDLRMR LGEGTGATAA LLVLRAAVAA LTSMTTFAEA GVAGTSTSPP S