COBT_CERSK
ID COBT_CERSK Reviewed; 338 AA.
AC B9KQ95;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 72.
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};
GN OrderedLocusNames=RSKD131_0742;
OS Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=557760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KD131 / KCTC 12085;
RX PubMed=19028901; DOI=10.1128/jb.01565-08;
RA Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL J. Bacteriol. 191:1118-1119(2009).
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; CP001150; ACM00602.1; -; Genomic_DNA.
DR RefSeq; WP_012643930.1; NC_011963.1.
DR AlphaFoldDB; B9KQ95; -.
DR SMR; B9KQ95; -.
DR EnsemblBacteria; ACM00602; ACM00602; RSKD131_0742.
DR GeneID; 67446188; -.
DR KEGG; rsk:RSKD131_0742; -.
DR HOGENOM; CLU_002982_0_1_5; -.
DR OMA; AIWYAGW; -.
DR UniPathway; UPA00061; UER00516.
DR Proteomes; UP000001597; Chromosome 1.
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..338
FT /note="Nicotinate-nucleotide--dimethylbenzimidazole
FT phosphoribosyltransferase"
FT /id="PRO_1000125112"
FT ACT_SITE 306
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00230"
SQ SEQUENCE 338 AA; 34277 MW; E98B1875BCD9B9B7 CRC64;
MKAPFTSLAG FRAVFETLPQ VDAEAVEAAT ARNETLTKPK GALGRLEDLA IWYAGWIGDG
RPALERPQVA IFAGNHGIAA RGVSAFPPEV TVQMVANYRA GGAAVNQLCH VAGASMTVTE
LELDRPTLDF TVSPAMTEDE LVAALAAGWE AVDDESDLLV VGEMGIGNTT AAAAIAAALF
GGTAAEWTGR GSGVAGSALE AKTRVVAEGL ERHGDALSDP LEVLRCLGGR EIAAMAGAIA
RARVGRTPVI LDGFICTSAA AVLHALTPSA LDHAIAGHVS AEGAHPAALA RIGKEPLLDL
GMRLGEGTGA IVAINILRSA VACLSGMATF AEAGVSGG
