COBT_THET8
ID COBT_THET8 Reviewed; 335 AA.
AC Q7SIC7; Q53WB4;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 25-MAY-2022, entry version 117.
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=TTHB048;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OG Plasmid pTT27.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of cobT from Thermus thermophilus HB8.";
RL Submitted (JAN-2003) to the PDB data bank.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP008227; BAD71844.1; -; Genomic_DNA.
DR RefSeq; WP_008631396.1; NC_006462.1.
DR RefSeq; YP_145287.1; NC_006462.1.
DR PDB; 1J33; X-ray; 2.00 A; A=1-335.
DR PDB; 1WX1; X-ray; 1.97 A; A/B=1-335.
DR PDBsum; 1J33; -.
DR PDBsum; 1WX1; -.
DR AlphaFoldDB; Q7SIC7; -.
DR SMR; Q7SIC7; -.
DR PRIDE; Q7SIC7; -.
DR EnsemblBacteria; BAD71844; BAD71844; BAD71844.
DR GeneID; 3169236; -.
DR KEGG; ttj:TTHB048; -.
DR PATRIC; fig|300852.9.peg.1992; -.
DR HOGENOM; CLU_002982_0_0_0; -.
DR OMA; AWMRKCA; -.
DR PhylomeDB; Q7SIC7; -.
DR UniPathway; UPA00061; UER00516.
DR EvolutionaryTrace; Q7SIC7; -.
DR Proteomes; UP000000532; Plasmid pTT27.
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 3D-structure; Cobalamin biosynthesis; Glycosyltransferase; Plasmid;
KW Reference proteome; Transferase.
FT CHAIN 1..335
FT /note="Nicotinate-nucleotide--dimethylbenzimidazole
FT phosphoribosyltransferase"
FT /id="PRO_0000167074"
FT ACT_SITE 304
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00230"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:1WX1"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1WX1"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:1WX1"
FT HELIX 24..37
FT /evidence="ECO:0007829|PDB:1WX1"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:1WX1"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:1WX1"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:1WX1"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:1WX1"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:1WX1"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1WX1"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1WX1"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:1WX1"
FT HELIX 133..152
FT /evidence="ECO:0007829|PDB:1WX1"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:1WX1"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:1WX1"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:1WX1"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:1J33"
FT HELIX 195..210
FT /evidence="ECO:0007829|PDB:1WX1"
FT HELIX 218..225
FT /evidence="ECO:0007829|PDB:1WX1"
FT HELIX 228..242
FT /evidence="ECO:0007829|PDB:1WX1"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:1WX1"
FT HELIX 252..264
FT /evidence="ECO:0007829|PDB:1WX1"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:1WX1"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:1WX1"
FT HELIX 282..290
FT /evidence="ECO:0007829|PDB:1WX1"
FT HELIX 306..321
FT /evidence="ECO:0007829|PDB:1WX1"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:1WX1"
SQ SEQUENCE 335 AA; 34747 MW; B05DDF144305C4C6 CRC64;
MDPEVFAQAR LRMDQLTKPP RALGYLEEVA LRLAALQGRV KPELGRGAVV VAAADHGVVA
EGVSAYPQEV TRQMVLNFLR GGAAINQFAL AADCAVYVLD VGVVGELPDH PGLLKRKVRP
GTANLAQGPA MTPEEAERAL LAGREAARRA IAEGATLLAA GDMGIGNTTA AAALTAALLG
LPPEAVVGRG TGVGEEGLRR KRQAVARALA RLHPGMGPLE VAAEVGGLEL VAIAGIYLEG
YEAGLPLVLD GFPVTAGALL AWKMAPGLRD HLFAGHLSRE PGHRHQLEAL GLRPLLDLDL
ALGEGTGAVL AMPLLRAAAR ILHMATFQEA GVSRG
