COBT_HERA2
ID COBT_HERA2 Reviewed; 350 AA.
AC A9B732;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=Haur_3263;
OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC Herpetosiphon.
OX NCBI_TaxID=316274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23779 / DSM 785 / 114-95;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL Submitted (OCT-2007) 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; CP000875; ABX05900.1; -; Genomic_DNA.
DR AlphaFoldDB; A9B732; -.
DR SMR; A9B732; -.
DR STRING; 316274.Haur_3263; -.
DR EnsemblBacteria; ABX05900; ABX05900; Haur_3263.
DR KEGG; hau:Haur_3263; -.
DR eggNOG; COG2038; Bacteria.
DR HOGENOM; CLU_002982_0_0_0; -.
DR OMA; AWMRKCA; -.
DR UniPathway; UPA00061; UER00516.
DR Proteomes; UP000000787; 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; Reference proteome;
KW Transferase.
FT CHAIN 1..350
FT /note="Nicotinate-nucleotide--dimethylbenzimidazole
FT phosphoribosyltransferase"
FT /id="PRO_1000100466"
FT ACT_SITE 317
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00230"
SQ SEQUENCE 350 AA; 35908 MW; 61C2C2F274D881CC CRC64;
MNIDDLSATI AELDSAAIQQ AQQRQDQLTK PQGALGLLET LSIQLAGITQ QCPPSVQKPI
IVVAAADHGV AEYGVSAYPS SVTAQMVANF LAGGAAVSVL ARHVGAELLI IDAGVQTAIV
SEAANFRSEW LGAGTHNLAI EPAMSQAQAQ SAFERGIRIA HELADAGHDL IALGEMGIGN
TTAAACLTAI YCQQPAAAVT GHGTGVQAEH YQRKIEVVAQ AVARVGSNVD GLQPLIEVGG
FEIGILAGII VGAAQRRVPI LVDGFITTAA ALVAQALAPK AIDYCIAAHC GAEPGHRIAL
QQLGLRPLLE LDLRLGEGSG AALAIPLVQA ACRILSEMAT FASAHVDTAL