COBT_DEIRA
ID COBT_DEIRA Reviewed; 365 AA.
AC Q9RYR8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 132.
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=cobT; OrderedLocusNames=DR_A0240;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
CC -!- FUNCTION: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from
CC nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
CC {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the CobT family. {ECO:0000305}.
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DR EMBL; AE001825; AAF12397.1; -; Genomic_DNA.
DR PIR; A75577; A75577.
DR RefSeq; NP_285563.1; NC_001264.1.
DR RefSeq; WP_010889499.1; NZ_CP015082.1.
DR AlphaFoldDB; Q9RYR8; -.
DR SMR; Q9RYR8; -.
DR STRING; 243230.DR_A0240; -.
DR EnsemblBacteria; AAF12397; AAF12397; DR_A0240.
DR KEGG; dra:DR_A0240; -.
DR PATRIC; fig|243230.17.peg.3130; -.
DR eggNOG; COG2038; Bacteria.
DR HOGENOM; CLU_002982_0_0_0; -.
DR InParanoid; Q9RYR8; -.
DR OMA; AWMRKCA; -.
DR OrthoDB; 1765140at2; -.
DR UniPathway; UPA00061; UER00516.
DR Proteomes; UP000002524; Chromosome II.
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; Reference proteome;
KW Transferase.
FT CHAIN 1..365
FT /note="Nicotinate-nucleotide--dimethylbenzimidazole
FT phosphoribosyltransferase"
FT /id="PRO_0000167047"
FT ACT_SITE 330
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 365 AA; 37266 MW; 81A37D3194F2EC7D CRC64;
MAMDTGRDSS ALTDLLGRLQ PADAEAMARA RERQAQLTKP AGALGDLEEL SVRLAGVFGT
ERPEPRGAAV LVAAGDHGVA AEGVSAYPPE VTPAMVANFL ADTPAGPGGA AVSALARTLG
AEVYVMDAGV NADLPEHPAL TRAARRRGTR NLRREAAMTR EETVALMLAG AALADRAMDA
GADFIIPGEM GIGNTTPAAA LTARLLGVDP ADVTGRGTGV DDERLAHKVD VVREALARTA
VTDPLDVLAE FGGFEIAAML GMMLAAAARR RAVILDGFVE GSAALVGVAL APALRDFLFP
AGECAERGHA AQLADLGLKP MFNLGLRLGE GTGGVLALPL LRGAAATLRE MRTFEEAAVP
GGGAA