LPDB_LACPL
ID LPDB_LACPL Reviewed; 187 AA.
AC F9UT67;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Flavin prenyltransferase LpdB {ECO:0000305};
DE EC=2.5.1.129 {ECO:0000250|UniProtKB:Q9HX08};
DE AltName: Full=Gallate decarboxylase subunit B {ECO:0000303|PubMed:23645198};
GN Name=lpdB {ECO:0000303|PubMed:23645198};
GN OrderedLocusNames=lp_0271 {ECO:0000312|EMBL:CCC77798.1};
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1
RC {ECO:0000312|Proteomes:UP000000432};
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1
RC {ECO:0000312|Proteomes:UP000000432};
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
RN [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=23645198; DOI=10.1128/aem.00840-13;
RA Jimenez N., Curiel J.A., Reveron I., de Las Rivas B., Munoz R.;
RT "Uncovering the Lactobacillus plantarum WCFS1 gallate decarboxylase
RT involved in tannin degradation.";
RL Appl. Environ. Microbiol. 79:4253-4263(2013).
CC -!- FUNCTION: Involved in tannin degradation. Flavin prenyltransferase that
CC catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for
CC gallate decarboxylase LpdC. The prenyltransferase is metal-independent
CC and links a dimethylallyl moiety from dimethylallyl monophosphate
CC (DMAP) to the flavin N5 and C6 atoms of FMN.
CC {ECO:0000305|PubMed:23645198}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl phosphate + FMNH2 = phosphate + prenyl-FMNH2;
CC Xref=Rhea:RHEA:37743, ChEBI:CHEBI:43474, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:87467, ChEBI:CHEBI:88052; EC=2.5.1.129;
CC Evidence={ECO:0000250|UniProtKB:Q9HX08};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to
CC decarboxylate gallic acid and protocatechuic acid.
CC {ECO:0000269|PubMed:23645198}.
CC -!- MISCELLANEOUS: Gallate decarboxylase does not form a complex composed
CC of Lpdc, LpdB and LpdD. The term subunit has been used in reference to
CC the three-gene operon. Gallate decarboxylase LpdC is the only protein
CC required to yield the gallate decarboxylase activity.
CC {ECO:0000269|PubMed:23645198}.
CC -!- SIMILARITY: Belongs to the UbiX/PAD1 family. {ECO:0000305}.
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DR EMBL; AL935263; CCC77798.1; -; Genomic_DNA.
DR RefSeq; WP_003643707.1; NC_004567.2.
DR RefSeq; YP_004888312.1; NC_004567.2.
DR AlphaFoldDB; F9UT67; -.
DR SMR; F9UT67; -.
DR STRING; 220668.lp_0271; -.
DR EnsemblBacteria; CCC77798; CCC77798; lp_0271.
DR GeneID; 57027085; -.
DR KEGG; lpl:lp_0271; -.
DR PATRIC; fig|220668.9.peg.225; -.
DR eggNOG; COG0163; Bacteria.
DR HOGENOM; CLU_074522_0_1_9; -.
DR OMA; GATHIQD; -.
DR PhylomeDB; F9UT67; -.
DR BioCyc; LPLA220668:G1GW0-220-MON; -.
DR BioCyc; MetaCyc:MON-19903; -.
DR Proteomes; UP000000432; Chromosome.
DR GO; GO:0106141; F:flavin prenyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1950; -; 1.
DR HAMAP; MF_01984; ubiX_pad; 1.
DR InterPro; IPR036551; Flavin_trans-like.
DR InterPro; IPR003382; Flavoprotein.
DR InterPro; IPR004507; UbiX-like.
DR PANTHER; PTHR43374; PTHR43374; 2.
DR Pfam; PF02441; Flavoprotein; 1.
DR SUPFAM; SSF52507; SSF52507; 1.
DR TIGRFAMs; TIGR00421; ubiX_pad; 1.
PE 2: Evidence at transcript level;
KW Flavoprotein; FMN; Prenyltransferase; Reference proteome; Transferase.
FT CHAIN 1..187
FT /note="Flavin prenyltransferase LpdB"
FT /id="PRO_0000444000"
FT BINDING 10..12
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9HX08"
FT BINDING 37
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9HX08"
FT BINDING 88..91
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9HX08"
FT BINDING 123
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9HX08"
FT BINDING 153
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000250|UniProtKB:Q9HX08"
FT BINDING 169
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000250|UniProtKB:Q9HX08"
SQ SEQUENCE 187 AA; 20565 MW; 0E33014C231E60BE CRC64;
MKRIVVGITG ASGTIYAVDL LEKLHQRPDV EVHLVMSAWA KKNLELETDY SLAQLTALAD
ATYRANDQGA AIASGSFLND GMVIVPASMK TVAGIAYGFG DNLISRAADV TIKEQRKLVI
VPRETPLSVI HLENLTKLAK LGAQIIPPIP AFYNHPQSIQ DLVNHQTMKI LDAFHIHNET
DRRWEGD
