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COBT_BACFR
ID   COBT_BACFR              Reviewed;         345 AA.
AC   Q64TE4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=BF2486;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; AP006841; BAD49235.1; -; Genomic_DNA.
DR   RefSeq; WP_011202890.1; NC_006347.1.
DR   RefSeq; YP_099769.1; NC_006347.1.
DR   AlphaFoldDB; Q64TE4; -.
DR   SMR; Q64TE4; -.
DR   STRING; 295405.BF2486; -.
DR   EnsemblBacteria; BAD49235; BAD49235; BF2486.
DR   KEGG; bfr:BF2486; -.
DR   PATRIC; fig|295405.11.peg.2394; -.
DR   HOGENOM; CLU_002982_0_0_10; -.
DR   OMA; AWMRKCA; -.
DR   UniPathway; UPA00061; UER00516.
DR   Proteomes; UP000002197; 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..345
FT                   /note="Nicotinate-nucleotide--dimethylbenzimidazole
FT                   phosphoribosyltransferase"
FT                   /id="PRO_1000021576"
FT   ACT_SITE        312
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00230"
SQ   SEQUENCE   345 AA;  37869 MW;  FA08158B1A46EE23 CRC64;
     MKTFQITRPD ETIREALTDK INNLTKPKGS LGTLEELALQ IGLIQQTLTP ELRHPQNIIF
     AADHGIVDEG VSLSPKEITW QQISNFLHGG AGVNFLCRQH GFELKIVDAG VDYDLPYEKG
     IINMKVRKSS RNYLYEAAMT EEEMNLCIER GAEVVRQCHA EGCNVLSLGE MGIGNTSSSS
     MWMTCFTHIP LELCVGAGSG LDNAGVHHKY NVLQQALDHY QGDGSAHDLI RYFGGLEMVM
     AIGAMLQAAE LKMIILVDGF IMTNCILAAS QLYPEVLHYA IFGHQGDEAG HKLVLDAMGA
     KPLLNLGLRL GEGTGAICSY PIIDSAIRMI NEMDNFAHAA ITKYF
 
 
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