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Database: UniProt
Entry: A0A348AGA0_9FIRM
LinkDB: A0A348AGA0_9FIRM
Original site: A0A348AGA0_9FIRM 
ID   A0A348AGA0_9FIRM        Unreviewed;       358 AA.
AC   A0A348AGA0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
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_1 {ECO:0000313|EMBL:BBB90098.1};
GN   Synonyms=cobT {ECO:0000256|HAMAP-Rule:MF_00230};
GN   ORFNames=MAMMFC1_00746 {ECO:0000313|EMBL:BBB90098.1};
OS   Methylomusa anaerophila.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Methylomusa.
OX   NCBI_TaxID=1930071 {ECO:0000313|EMBL:BBB90098.1, ECO:0000313|Proteomes:UP000276437};
RN   [1] {ECO:0000313|EMBL:BBB90098.1, ECO:0000313|Proteomes:UP000276437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMFC1 {ECO:0000313|EMBL:BBB90098.1,
RC   ECO:0000313|Proteomes:UP000276437};
RX   PubMed=29458677; DOI=10.1099/ijsem.0.002635;
RA   Amano N., Yamamuro A., Miyahara M., Kouzuma A., Abe T., Watanabe K.;
RT   "Methylomusa anaerophila gen. nov., sp. nov., an anaerobic methanol-
RT   utilizing bacterium isolated from a microbial fuel cell.";
RL   Int. J. Syst. Evol. Microbiol. 68:1118-1122(2018).
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; AP018449; BBB90098.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A348AGA0; -.
DR   KEGG; mana:MAMMFC1_00746; -.
DR   OrthoDB; 9781491at2; -.
DR   UniPathway; UPA00061; UER00516.
DR   Proteomes; UP000276437; 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   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:UP000276437};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00230}.
FT   ACT_SITE        318
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00230"
SQ   SEQUENCE   358 AA;  37763 MW;  3CC01BC869ECBAF3 CRC64;
     MKSLESIIRS IEPLNQDSML LTQQRLDSLT KPPGSLAVLE KMACQLAGIQ GKLPITLPNK
     AILLMAADHG VAVEGVSAFP AEVTEQMVYN FVNGGAAINV LARHANARLI LVDVGVKADF
     PAGLPIRRRK IRKGTDNMRY RPAMERPEVL QALQTGMDMV NELADDGIEV IGLGEMGIAN
     TTASSAITSL LAGKPPAQVV GRGTGIEQKV ISQKIRVIEE AVARHKPDPH DVIDVLAKVG
     GLEIAALAGA VLGAAARRIL IILDGFISSA AVLAAYRLCN SVQPYLLASH LSEEPGHAAI
     LQALGLEPCI RLNMRLGEGT GAALGMTLLD AAVKIVNEMA TFGEAKVAEA YNAGDKEV
//
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