ID A0A1Y4HVG3_9BACT Unreviewed; 345 AA.
AC A0A1Y4HVG3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=B5F34_04965 {ECO:0000313|EMBL:OUP10269.1};
OS Mediterranea sp. An20.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Mediterranea.
OX NCBI_TaxID=1965586 {ECO:0000313|EMBL:OUP10269.1, ECO:0000313|Proteomes:UP000196631};
RN [1] {ECO:0000313|Proteomes:UP000196631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An20 {ECO:0000313|Proteomes:UP000196631};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUP10269.1}.
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DR EMBL; NFJV01000006; OUP10269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4HVG3; -.
DR OrthoDB; 9781491at2; -.
DR UniPathway; UPA00061; UER00516.
DR Proteomes; UP000196631; 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:UP000196631};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00230}.
FT ACT_SITE 312
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00230"
SQ SEQUENCE 345 AA; 37772 MW; BCB87905333F2CDB CRC64;
MKSFNITCPD GLIRRALTDK INNLTKPKGS LGRLEELALQ IGLIQQTLSP VLKHPQNVIF
AADHGIVEEG VSVSPKEVTW QQILNFLNGG AGINFLCRQH GFELKIVDAG VDNELPYERG
IINRKVRRGS RNFLHEPALT EEEFEQCIEY GAEIVRLCHA EGSNVLSFGE MGIGNTSPSS
VWMHLLTGIP LEQCIGAGSG LNQDGIHHKY EVLQQAVAHY RGDGSACDVL RHFGGLEMVM
ATGAMLQAAE LKMVILVDGF IMTNCILAAS RLCPEVLSYA IFAHGGDEAG HHLLLDYLHT
RPLLNLGLRL GEGTGAVCAY PLVDSAVRMI NEMDSFTHAE ITKYF
//
