COBT_MYCA1
ID COBT_MYCA1 Reviewed; 349 AA.
AC A0QEZ9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=MAV_2283;
OS Mycobacterium avium (strain 104).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=243243;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) 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: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; CP000479; ABK65706.1; -; Genomic_DNA.
DR RefSeq; WP_009976509.1; NC_008595.1.
DR AlphaFoldDB; A0QEZ9; -.
DR SMR; A0QEZ9; -.
DR EnsemblBacteria; ABK65706; ABK65706; MAV_2283.
DR KEGG; mav:MAV_2283; -.
DR HOGENOM; CLU_002982_0_2_11; -.
DR OMA; AWMRKCA; -.
DR OrthoDB; 1765140at2; -.
DR UniPathway; UPA00061; UER00516.
DR Proteomes; UP000001574; 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..349
FT /note="Nicotinate-nucleotide--dimethylbenzimidazole
FT phosphoribosyltransferase"
FT /id="PRO_1000021602"
FT ACT_SITE 313
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00230"
SQ SEQUENCE 349 AA; 35344 MW; A6A239E9BB84C874 CRC64;
MEFATVSPPD PGAAAAARAR QDTLTKPRGA LGRLEDLSVW IAACQGQCPP RQFERARVVV
FAGDHGVARC GVSAYPPEVT AQMVANFDAG GAAINALAGV AGASVRVADL AVDADPPDDR
IGANKVRRGS GDITVQDALT AEETERALSA GAAIADEEVD AGADLLIAGD MGIGNTTAAA
VLVAALTNVE PVVAVGFGTG IDDAGWARKT AAVRDALFRA RRVLPDPVAL LRCAGGADLA
ALAGFCAQAA VRRTPLLLDG MAVTAAALVA EHLAPGARLW WQAGHRSTEP GHALALTALD
LEPILDLRMR LGEGTGAALA LPIVRAAVAA LSSMATFAQA GVSDPSAHP