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Database: UniProt
Entry: A0A1H9HVN7_9BURK
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ID   A0A1H9HVN7_9BURK        Unreviewed;       356 AA.
AC   A0A1H9HVN7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00015486, ECO:0000256|HAMAP-Rule:MF_00230};
DE            Short=NN:DBI PRT {ECO:0000256|HAMAP-Rule:MF_00230};
DE            EC=2.4.2.21 {ECO:0000256|ARBA:ARBA00011991, ECO:0000256|HAMAP-Rule:MF_00230};
DE   AltName: Full=N(1)-alpha-phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00030686, ECO:0000256|HAMAP-Rule:MF_00230};
GN   Name=cobT {ECO:0000256|HAMAP-Rule:MF_00230};
GN   ORFNames=SAMN02982919_00933 {ECO:0000313|EMBL:SEQ66338.1};
OS   Giesbergeria anulus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Giesbergeria.
OX   NCBI_TaxID=180197 {ECO:0000313|EMBL:SEQ66338.1, ECO:0000313|Proteomes:UP000199766};
RN   [1] {ECO:0000313|EMBL:SEQ66338.1, ECO:0000313|Proteomes:UP000199766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35958 {ECO:0000313|EMBL:SEQ66338.1,
RC   ECO:0000313|Proteomes:UP000199766};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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:0000256|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:0000256|ARBA:ARBA00001058, ECO:0000256|HAMAP-
CC         Rule:MF_00230};
CC   -!- PATHWAY: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-
CC       ribazole from 5,6-dimethylbenzimidazole: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005049, ECO:0000256|HAMAP-Rule:MF_00230}.
CC   -!- SIMILARITY: Belongs to the CobT family. {ECO:0000256|ARBA:ARBA00007110,
CC       ECO:0000256|HAMAP-Rule:MF_00230}.
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DR   EMBL; FOGD01000002; SEQ66338.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9HVN7; -.
DR   STRING; 180197.SAMN02982919_00933; -.
DR   OrthoDB; 9781491at2; -.
DR   UniPathway; UPA00061; UER00516.
DR   Proteomes; UP000199766; Unassembled WGS sequence.
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   NCBIfam; TIGR03160; cobT_DBIPRT; 1.
DR   PANTHER; PTHR43463; NICOTINATE-NUCLEOTIDE--DIMETHYLBENZIMIDAZOLE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR43463:SF1; NICOTINATE-NUCLEOTIDE--DIMETHYLBENZIMIDAZOLE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF02277; DBI_PRT; 1.
DR   SUPFAM; SSF52733; Nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT); 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW   Rule:MF_00230};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00230}; Reference proteome {ECO:0000313|Proteomes:UP000199766};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00230}.
FT   ACT_SITE        323
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00230"
SQ   SEQUENCE   356 AA;  36357 MW;  AEA00F65E37589E7 CRC64;
     MLLPSELPSL PVVADLADPT LTSALHHLID HKTKPLGALG RLEALALQLG QILGTEQPRL
     EVPQMVVFAG DHGLAAKGVS AYPSDVTWQM VENFLAGGAA VSVLARQHGL ALTVVDCGVA
     RDLTPRQAVA GQPQLLARKV AAGTQDASIG PAMTPAQCAQ AVAHGMEVVR SLPGNVLLLG
     EMGIGNTSVA SLLLARLCGV PLEACTGAGT GLDAAGIARK RQVLEQALQA NAGAVEPLEA
     LAALGGFEVA TMVGAVLQAA SERRVMVVDG FITSAAVLVA SRLEPLVLQR CVFAHNSGEP
     GHALMLAQLR AQPLLDLGLR LGEGSGAALA WPLLVSACAI LREMASFATA GVATKA
//
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