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Database: UniProt
Entry: F2LGA2_BURGS
LinkDB: F2LGA2_BURGS
Original site: F2LGA2_BURGS 
ID   F2LGA2_BURGS            Unreviewed;       351 AA.
AC   F2LGA2;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
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   OrderedLocusNames=bgla_1g31450 {ECO:0000313|EMBL:AEA61753.1};
OS   Burkholderia gladioli (strain BSR3).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA61753.1, ECO:0000313|Proteomes:UP000008316};
RN   [1] {ECO:0000313|EMBL:AEA61753.1, ECO:0000313|Proteomes:UP000008316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSR3 {ECO:0000313|EMBL:AEA61753.1,
RC   ECO:0000313|Proteomes:UP000008316};
RX   PubMed=21478339; DOI=10.1128/JB.00420-11;
RA   Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., Choi I.Y.,
RA   Moon J.S., Kim J., Hwang I.;
RT   "Complete genome sequence of Burkholderia gladioli BSR3.";
RL   J. Bacteriol. 193:3149-3149(2011).
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; CP002599; AEA61753.1; -; Genomic_DNA.
DR   RefSeq; WP_013699075.1; NC_015381.1.
DR   AlphaFoldDB; F2LGA2; -.
DR   STRING; 999541.bgla_1g31450; -.
DR   KEGG; bgd:bgla_1g31450; -.
DR   eggNOG; COG2038; Bacteria.
DR   HOGENOM; CLU_002982_0_0_4; -.
DR   UniPathway; UPA00061; UER00516.
DR   Proteomes; UP000008316; 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   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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00230}.
FT   ACT_SITE        316
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00230"
SQ   SEQUENCE   351 AA;  36019 MW;  C1AAD6DCB1CF4664 CRC64;
     MNPTYTVPKL EALDDTLSAT LQHLIDTKTK PPGSLGKLEA LALQLGRIQR STRPRIERPV
     TIVFAADHGI AAEGVSPYPQ AVTAQMVANF LAGGAAINAF SKLAGCELEI VDAGVATPLP
     ASPQLIAAPV AAGTRNFAQE PAMSEAQLHA ALAAGAARVA HHAALGTTVV GFGEMGIANT
     SAAACLMSRL VGLPLAECVG RGTGLDDQGL ARKRAVLEAA LARHPEAQAP LEVLATFGGF
     EIAMMTGAFL AAAQARMAIL VDGFIASSAL LVAAALQPAV LDYCVFSHVS DENGHRRMLQ
     HFGAAPLLAL DLRLGEGTGA ALALPLLRAA TAFLDEMASF EAAGVANRDD A
//
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