COBU_SINSX
ID COBU_SINSX Reviewed; 338 AA.
AC P29935;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase;
DE Short=NN:DBI PRT;
DE EC=2.4.2.21;
DE AltName: Full=N(1)-alpha-phosphoribosyltransferase;
GN Name=cobU;
OS Sinorhizobium sp.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=42445;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-16.
RC STRAIN=SC510;
RX PubMed=1917841; DOI=10.1128/jb.173.19.6066-6073.1991;
RA Cameron B., Blanche F., Rouyez M.-C., Bisch D., Famechon A., Couder M.,
RA Cauchois L., Thibaut D., Debussche L., Crouzet J.;
RT "Genetic analysis, nucleotide sequence, and products of two Pseudomonas
RT denitrificans cob genes encoding nicotinate-nucleotide:
RT dimethylbenzimidazole phosphoribosyltransferase and cobalamin (5'-
RT phosphate) synthase.";
RL J. Bacteriol. 173:6066-6073(1991).
CC -!- FUNCTION: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from
CC nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
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 -!- PATHWAY: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-
CC ribazole from 5,6-dimethylbenzimidazole: step 1/2.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the CobT family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to originate from Pseudomonas
CC denitrificans, but similarity searches show that the sequence is much
CC closer to Sinorhizobium. The entry's taxonomy has been changed.
CC {ECO:0000305}.
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DR EMBL; M62868; AAA25788.1; -; Genomic_DNA.
DR AlphaFoldDB; P29935; -.
DR SMR; P29935; -.
DR KEGG; ag:AAA25788; -.
DR BioCyc; MetaCyc:MON-13241; -.
DR SABIO-RK; P29935; -.
DR UniPathway; UPA00061; UER00516.
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 1: Evidence at protein level;
KW Cobalamin biosynthesis; Direct protein sequencing; Glycosyltransferase;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1917841"
FT CHAIN 2..338
FT /note="Nicotinate-nucleotide--dimethylbenzimidazole
FT phosphoribosyltransferase"
FT /id="PRO_0000167061"
FT ACT_SITE 305
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 338 AA; 34682 MW; B7E7B51CCA471861 CRC64;
MSASGLPFDD FRELLRNLPG PDAAALVAAR ERDAQLTKPP GALGRLEEIA FWLAAWTGKA
PVVNRPLVAI FAGNHGVTRQ GVTPFPSSVT AQMVENFAAG GAAINQICVS HDLGLKVFDL
ALEYPTGDIT EEAALSERDC AATMAFGMEA IAGGTDLLCI GEMGIGNTTI AAAINLGLYG
GTAEEWVGPG TGSEGEVLKR KIAAVEKAVA LHRDHLSDPL ELMRRLGGRE IAAMAGAILA
ARVQKVPVII DGYVATAAAS ILKAANPSAL DHCLIGHVSG EPGHLRAIEK LGKTPLLALG
MRLGEGTGAA LAAGIVKAAA ACHSGMATFA QAGVSNKE