ID   COBT_CERS1              Reviewed;         338 AA.
AC   A3PIN5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 88.
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};
GN   OrderedLocusNames=Rsph17029_1091;
OS   Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=349101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17029 / ATH 2.4.9;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.,
RA   Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC 17029.";
RL   Submitted (FEB-2007) 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; CP000577; ABN76201.1; -; Genomic_DNA.
DR   RefSeq; WP_011840794.1; NC_009049.1.
DR   AlphaFoldDB; A3PIN5; -.
DR   SMR; A3PIN5; -.
DR   EnsemblBacteria; ABN76201; ABN76201; Rsph17029_1091.
DR   GeneID; 57469774; -.
DR   KEGG; rsh:Rsph17029_1091; -.
DR   HOGENOM; CLU_002982_0_1_5; -.
DR   OMA; AIWYAGW; -.
DR   UniPathway; UPA00061; UER00516.
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..338
FT                   /note="Nicotinate-nucleotide--dimethylbenzimidazole
FT                   phosphoribosyltransferase"
FT                   /id="PRO_1000058767"
FT   ACT_SITE        306
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00230"
SQ   SEQUENCE   338 AA;  34267 MW;  AA2915F52B3D6E70 CRC64;
     MKAPFTSLAG FRAVFETLPQ VDAEAVEAAT ARNETLTKPK GALGRLEDLA IWYAGWIGDG
     RPALERPQVA IFAGNHGIAA RGVSAFPPEV TVQMVANYRA GGAAVNQLCR VAGASMTVTE
     LELDRPTLDF TVSPAMTEDE LVAALAAGWE AVDDESDLLV VGEMGIGNTT AAAAIAAALF
     GGTAAEWTGR GSGVAGSALE AKTRVVAEGL ELHADALSDP LEVLRCLGGR EIAAMAGAIA
     RARVGRTPVI LDGFICTSAA AVLHALTPSA LDHAIAGHVS AEGAHPAALA RIGKEPLLDL
     GMRLGEGTGA IVAINILRSA VACLSGMATF AEAGVSGG