LPDC_LACPL
ID LPDC_LACPL Reviewed; 490 AA.
AC F9US27;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Gallate decarboxylase {ECO:0000303|PubMed:23645198};
DE EC=4.1.1.59 {ECO:0000269|PubMed:23645198};
DE AltName: Full=Gallate decarboxylase catalytic subunit {ECO:0000303|PubMed:23645198};
DE AltName: Full=Protocatechuate decarboxylase {ECO:0000303|PubMed:23645198};
DE EC=4.1.1.63 {ECO:0000269|PubMed:23645198};
GN Name=lpdC {ECO:0000303|PubMed:23645198};
GN Synonyms=ubiD {ECO:0000312|EMBL:CCC80016.1};
GN OrderedLocusNames=lp_2945 {ECO:0000312|EMBL:CCC80016.1};
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;
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, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND INDUCTION.
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. Catalyzes the decarboxylation
CC of gallic acid and protocatechuic acid to pyrogallol and catechol,
CC respectively. {ECO:0000269|PubMed:23645198}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4,5-trihydroxybenzoate + H(+) = 1,2,3-trihydroxybenzene +
CC CO2; Xref=Rhea:RHEA:12749, ChEBI:CHEBI:15378, ChEBI:CHEBI:16164,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16918; EC=4.1.1.59;
CC Evidence={ECO:0000269|PubMed:23645198};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxybenzoate + H(+) = catechol + CO2;
CC Xref=Rhea:RHEA:22416, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:18135, ChEBI:CHEBI:36241; EC=4.1.1.63;
CC Evidence={ECO:0000269|PubMed:23645198};
CC -!- COFACTOR:
CC Name=prenyl-FMN; Xref=ChEBI:CHEBI:87746;
CC Evidence={ECO:0000250|UniProtKB:P0AAB4};
CC Note=Binds 1 prenylated FMN (prenyl-FMN) per subunit.
CC {ECO:0000250|UniProtKB:P0AAB4};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P0AAB4};
CC -!- INDUCTION: By gallic acid. {ECO:0000305|PubMed:23645198}.
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 UbiD family. {ECO:0000305}.
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DR EMBL; AL935263; CCC80016.1; -; Genomic_DNA.
DR RefSeq; WP_003644796.1; NC_004567.2.
DR RefSeq; YP_004890530.1; NC_004567.2.
DR AlphaFoldDB; F9US27; -.
DR SMR; F9US27; -.
DR STRING; 220668.lp_2945; -.
DR EnsemblBacteria; CCC80016; CCC80016; lp_2945.
DR GeneID; 57026287; -.
DR GeneID; 66450552; -.
DR KEGG; lpl:lp_2945; -.
DR PATRIC; fig|220668.9.peg.2459; -.
DR eggNOG; COG0043; Bacteria.
DR HOGENOM; CLU_023348_5_1_9; -.
DR OMA; TEGGCCW; -.
DR PhylomeDB; F9US27; -.
DR BioCyc; LPLA220668:G1GW0-2512-MON; -.
DR BioCyc; MetaCyc:MON-19902; -.
DR Proteomes; UP000000432; Chromosome.
DR GO; GO:0018798; F:gallate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050223; F:protocatechuate decarboxylase activity; IEA:UniProtKB-EC.
DR InterPro; IPR002830; UbiD.
DR PANTHER; PTHR30108; PTHR30108; 1.
DR Pfam; PF01977; UbiD; 1.
PE 1: Evidence at protein level;
KW Decarboxylase; Flavoprotein; FMN; Lyase; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..490
FT /note="Gallate decarboxylase"
FT /id="PRO_0000444026"
FT ACT_SITE 289
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AAB4"
FT BINDING 165
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P0AAB4"
FT BINDING 168..170
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000250|UniProtKB:P0AAB4"
FT BINDING 187
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000250|UniProtKB:P0AAB4"
FT BINDING 233
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P0AAB4"
SQ SEQUENCE 490 AA; 54259 MW; 266E54023E02B8AD CRC64;
MAEQPWDLRR VLDEIKDDPK NYHETDVEVD PNAELSGVYR YIGAGGTVQR PTQEGPAMMF
NNVKGFPDTR VLTGLMASRR RVGKMFHHDY QTLGQYLNEA VSNPVAPETV AEADAPAHDV
VYKATDEGFD IRKLVAAPTN TPQDAGPYIT VGVVFGSSMD KSKSDVTIHR MVLEDKDKLG
IYIMPGGRHI GAFAEEYEKA NKPMPITINI GLDPAITIGA TFEPPTTPFG YNELGVAGAI
RNQAVQLVDG VTVDEKAIAR SEYTLEGYIM PNERIQEDIN THTGKAMPEF PGYDGDANPA
LQVIKVTAVT HRKNAIMQSV IGPSEEHVSM AGIPTEASIL QLVNRAIPGK VTNVYNPPAG
GGKLMTIMQI HKDNEADEGI QRQAALLAFS AFKELKTVIL VDEDVDIFDM NDVIWTMNTR
FQADQDLMVL SGMRNHPLDP SERPQYDPKS IRFRGMSSKL VIDGTVPFDM KDQFERAQFM
KVADWEKYLK
