ID A0A1Z4EJV8_9MYCO Unreviewed; 352 AA.
AC A0A1Z4EJV8;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
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 ECO:0000313|EMBL:BAX93241.1};
GN ORFNames=B2J96_09260 {ECO:0000313|EMBL:PRI15573.1}, MSG_03101
GN {ECO:0000313|EMBL:BAX93241.1};
OS Mycobacterium shigaense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=722731 {ECO:0000313|EMBL:BAX93241.1, ECO:0000313|Proteomes:UP000217736};
RN [1] {ECO:0000313|EMBL:PRI15573.1, ECO:0000313|Proteomes:UP000239044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UN-152 {ECO:0000313|EMBL:PRI15573.1,
RC ECO:0000313|Proteomes:UP000239044};
RA Yoshida M., Fukano H., Hoshino Y.;
RT "Draft genome sequence of Mycobacterium shigaense sp. nov.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000217736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UN-152 {ECO:0000313|Proteomes:UP000217736};
RA Fukano H., Yoshida M., Kazumi Y., Ogura Y., Mitarai S., Hayashi T.,
RA Hoshino Y.;
RT "Complete Genome Sequence of Mycobacterium shigaense.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:BAX93241.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 32072 {ECO:0000313|EMBL:BAX93241.1};
RA Yoshida M., Fukano H., Ogura Y., Kazumi Y., Mitarai S., Hayashi T.,
RA Hoshino Y.;
RT "Complete Genome Sequence of Mycobacterium shigaense.";
RL Genome Announc. 6:e00552-18(2018).
CC -!- FUNCTION: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from
CC nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
CC {ECO:0000256|ARBA:ARBA00002197, 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; AP018164; BAX93241.1; -; Genomic_DNA.
DR EMBL; MWON01000010; PRI15573.1; -; Genomic_DNA.
DR KEGG; mshg:MSG_03101; -.
DR OrthoDB; 9781491at2; -.
DR UniPathway; UPA00061; UER00516.
DR Proteomes; UP000217736; Chromosome.
DR Proteomes; UP000239044; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00230}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 313
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00230"
SQ SEQUENCE 352 AA; 35607 MW; 1E9BB21DBDAD08FE CRC64;
MEFPVIAPPD ADTAAAARGR QDTLTKPRGA LGRLEDLAVW VASCQGHCPP RQFERARVVV
FAGDHGVARS GVSAYPPEVT AQMVANIDAG GATINALSAI AGATVRIADL SVDADPLSEQ
IGAHKVRRGS GDIAVQDALT DEETARAIAA GQRIADDEVD GGADLLIAGD MGIGNTTAAA
VLVAALTNAE PVAVVGFGTG IDDAGWARKT AAIRDALFRA KSVLPDPVGL LRCCAGADLA
AMAGFCAQAA VRRTPVLLDG MAVTAAALVA ERLAPGARHW WQAGHRSTEP GHALALGALQ
LDPILDLGMR LGEGSGATVA VPVLRAAVAA LTSTATFAEA GVTGRATPDT SS
//
