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Database: UniProt
Entry: V6IA01_9LEPT
LinkDB: V6IA01_9LEPT
Original site: V6IA01_9LEPT 
ID   V6IA01_9LEPT            Unreviewed;       344 AA.
AC   V6IA01;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 51.
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   ECO:0000313|EMBL:EQA64709.1};
GN   ORFNames=LEP1GSC062_3955 {ECO:0000313|EMBL:EQA64709.1};
OS   Leptospira alexanderi serovar Manhao 3 str. L 60.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1049759 {ECO:0000313|EMBL:EQA64709.1, ECO:0000313|Proteomes:UP000018747};
RN   [1] {ECO:0000313|EMBL:EQA64709.1, ECO:0000313|Proteomes:UP000018747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L 60 {ECO:0000313|EMBL:EQA64709.1,
RC   ECO:0000313|Proteomes:UP000018747};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA   van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA   Fouts D.E.;
RL   Submitted (MAY-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EQA64709.1}.
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DR   EMBL; AHMT02000002; EQA64709.1; -; Genomic_DNA.
DR   RefSeq; WP_010577257.1; NZ_AHMT02000002.1.
DR   AlphaFoldDB; V6IA01; -.
DR   STRING; 100053.GCA_002009845_00996; -.
DR   OrthoDB; 9781491at2; -.
DR   UniPathway; UPA00061; UER00516.
DR   Proteomes; UP000018747; 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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00230}.
FT   ACT_SITE        311
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00230"
SQ   SEQUENCE   344 AA;  37070 MW;  7773F7D4EA17FA40 CRC64;
     MNPNELIVKL QSKIDLKTKP PGSLGTLESL ALQIGLIQNT DSPELKNPHI LVFAGDHGLA
     DSGVSAYPKE VTYQMVFNFL NGGAAINAFC KQNSIRLKVV DAGVDFSFSD GSASLHPDFI
     DAKVGFGTKN ILMESAMTKE ECNQALEKGA LISAKEISSN CNVIGFGEMG IGNTSSASLI
     TASVLQKDLR EVTGKGTGLN EQKFQKKIAI LEECLRKYQS SLRTPFEVLQ TFGGFETAMM
     IGAMIDSAKK GRIILVDGFI ATSAFLIAHK MEPTILKNAV FCHKSVEPGH MYLLEEWNAK
     PLLDLGLRLG EGTGCAIAFP ILLSAIAFLN DMASFESAKV DQKL
//
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