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Database: UniProt
Entry: A0A1G9UBM6_9FIRM
LinkDB: A0A1G9UBM6_9FIRM
Original site: A0A1G9UBM6_9FIRM 
ID   A0A1G9UBM6_9FIRM        Unreviewed;       347 AA.
AC   A0A1G9UBM6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00015486, ECO:0000256|HAMAP-Rule:MF_00230};
DE            Short=NN:DBI PRT {ECO:0000256|HAMAP-Rule:MF_00230};
DE            EC=2.4.2.21 {ECO:0000256|ARBA:ARBA00011991, ECO:0000256|HAMAP-Rule:MF_00230};
DE   AltName: Full=N(1)-alpha-phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00030686, ECO:0000256|HAMAP-Rule:MF_00230};
GN   Name=cobT {ECO:0000256|HAMAP-Rule:MF_00230};
GN   ORFNames=SAMN04515677_11625 {ECO:0000313|EMBL:SDM57351.1};
OS   Romboutsia lituseburensis DSM 797.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Romboutsia.
OX   NCBI_TaxID=1121325 {ECO:0000313|EMBL:SDM57351.1, ECO:0000313|Proteomes:UP000199068};
RN   [1] {ECO:0000313|EMBL:SDM57351.1, ECO:0000313|Proteomes:UP000199068}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 797 {ECO:0000313|EMBL:SDM57351.1,
RC   ECO:0000313|Proteomes:UP000199068};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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:0000256|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:0000256|ARBA:ARBA00001058, ECO:0000256|HAMAP-
CC         Rule:MF_00230};
CC   -!- PATHWAY: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-
CC       ribazole from 5,6-dimethylbenzimidazole: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005049, ECO:0000256|HAMAP-Rule:MF_00230}.
CC   -!- SIMILARITY: Belongs to the CobT family. {ECO:0000256|ARBA:ARBA00007110,
CC       ECO:0000256|HAMAP-Rule:MF_00230}.
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DR   EMBL; FNGW01000016; SDM57351.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9UBM6; -.
DR   STRING; 1121325.SAMN04515677_11625; -.
DR   UniPathway; UPA00061; UER00516.
DR   Proteomes; UP000199068; Unassembled WGS sequence.
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   NCBIfam; TIGR03160; cobT_DBIPRT; 1.
DR   PANTHER; PTHR43463; NICOTINATE-NUCLEOTIDE--DIMETHYLBENZIMIDAZOLE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR43463:SF1; NICOTINATE-NUCLEOTIDE--DIMETHYLBENZIMIDAZOLE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF02277; DBI_PRT; 1.
DR   SUPFAM; SSF52733; Nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT); 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW   Rule:MF_00230};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00230}; Reference proteome {ECO:0000313|Proteomes:UP000199068};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00230}.
FT   ACT_SITE        317
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00230"
SQ   SEQUENCE   347 AA;  37129 MW;  FE7CDB114A880509 CRC64;
     MYLLENISKN IYSLDKNSIQ QAKDRLDTLI KPKGSLGKIE DICMQLAGIY GTAKFDTSKK
     AIIAFAGDHG VYEEGVAPDP QDITQLQFPN FTKGLCGVGA LSKFVGADVI AVDVGVNCDH
     KLDGVRDYKI RKGTSNMAKG AAMTREEAIK CLEIGIEMAE ECIEKGYKVI GIGEMGICNT
     TPSSAIISVI DGCDPAIVTG IGAGLKKERL KHKADTIRNA IELNKPNPDD GIDILSKVGG
     FEIGSMAGVI LGCSANKTPV VLDGFISYAA ALLAYKINPK SREYMIASHL SAEAGTQKAL
     EMLDLSPVLN MDMRLGEGSG AALAFNIIEA SNYAYQNMAT FDEVEWV
//
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