ID   COBT_GEOMG              Reviewed;         353 AA.
AC   Q39YG4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=Gmet_0467;
OS   Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=269799;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Geobacter metallireducens GS-15.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the CobT family. {ECO:0000255|HAMAP-
CC       Rule:MF_00230}.
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DR   EMBL; CP000148; ABB30710.1; -; Genomic_DNA.
DR   RefSeq; WP_004513836.1; NC_007517.1.
DR   AlphaFoldDB; Q39YG4; -.
DR   SMR; Q39YG4; -.
DR   STRING; 269799.Gmet_0467; -.
DR   EnsemblBacteria; ABB30710; ABB30710; Gmet_0467.
DR   KEGG; gme:Gmet_0467; -.
DR   eggNOG; COG2038; Bacteria.
DR   HOGENOM; CLU_002982_0_0_7; -.
DR   OMA; AWMRKCA; -.
DR   OrthoDB; 1765140at2; -.
DR   UniPathway; UPA00061; UER00516.
DR   Proteomes; UP000007073; 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..353
FT                   /note="Nicotinate-nucleotide--dimethylbenzimidazole
FT                   phosphoribosyltransferase"
FT                   /id="PRO_1000021597"
FT   ACT_SITE        318
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00230"
SQ   SEQUENCE   353 AA;  36518 MW;  CCB55A3C201A5CFB CRC64;
     MTLLTETLSN IRPVDAGLMA QAQARLDNKT KPIGSLGRLE EFARRTVAIS GSLDPSTAKK
     AIFTFAADHG VVEEGVSAFP KEVTVQMVFN FLKGGAGINV LANHVGADVL VVDMGIDHDF
     GDTPGLIDRK VARGTRNMAK GPAMTREEAV TALEAGIELA CGCKADGVAM AGTGEMGIGN
     TTAASAIIAA FSGKTVADVT HRGTGINDAA LAKKVTIIEQ ALAVNRPDPK DPIDVLAKVG
     GLEIAGIAGL VLGCAANRIP VVVDGFISTA GALIACELCP TVKEYIFAAH ESVEIGHRFM
     LERIGAEPIL DLHLRLGEGT GAALAMGLIE AGVKILKEMA TFAEAGVEKG RDQ