ID   LIGI_COMTE              Reviewed;         305 AA.
AC   Q93PS7;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=2-pyrone-4,6-dicarbaxylate hydrolase {ECO:0000303|PubMed:11495993, ECO:0000303|PubMed:7142106};
DE            Short=PDC hydrolase {ECO:0000303|PubMed:7142106};
DE            EC=3.1.1.57 {ECO:0000269|PubMed:7142106};
DE   AltName: Full=2-pyrone-4,6-dicarboxylate lactonase;
GN   Name=pmdD {ECO:0000303|PubMed:11495993};
OS   Comamonas testosteroni (Pseudomonas testosteroni).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=BR6020;
RX   PubMed=11495993; DOI=10.1099/00221287-147-8-2157;
RA   Providenti M.A., Mampel J., MacSween S., Cook A.M., Wyndham R.C.;
RT   "Comamonas testosteroni BR6020 possesses a single genetic locus for
RT   extradiol cleavage of protocatechuate.";
RL   Microbiology 147:2157-2167(2001).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND INDUCTION.
RX   PubMed=7142106; DOI=10.1128/jb.152.3.1154-1162.1982;
RA   Kersten P.J., Dagley S., Whittaker J.W., Arciero D.M., Lipscomb J.D.;
RT   "2-pyrone-4,6-dicarboxylic acid, a catabolite of gallic acids in
RT   Pseudomonas species.";
RL   J. Bacteriol. 152:1154-1162(1982).
CC   -!- FUNCTION: Involved in the degradation of aromatic compounds via the
CC       protocatechuate 4,5-cleavage pathway (PubMed:11495993). Catalyzes the
CC       hydrolysis of 2-pyrone-4,6-dicarboxylate (PDC) to oxalomesaconate (OMA)
CC       (PubMed:7142106). Also catalyzes the reverse reaction (PubMed:7142106).
CC       {ECO:0000269|PubMed:11495993, ECO:0000269|PubMed:7142106}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxo-2H-pyran-4,6-dicarboxylate + H2O = (1E)-4-oxobut-1-ene-
CC         1,2,4-tricarboxylate + H(+); Xref=Rhea:RHEA:10644, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57471, ChEBI:CHEBI:58304; EC=3.1.1.57;
CC         Evidence={ECO:0000269|PubMed:7142106};
CC   -!- ACTIVITY REGULATION: Strongly inhibited by 1 mM Zn(2+), Cu(2+), Mn(2+)
CC       and Co(2+) ions. Also inhibited by 5,5'-dithiobis(2-nitrobenzoic acid)
CC       (Ellman reagent) in vitro. {ECO:0000269|PubMed:7142106}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=90 uM for 2-pyrone-4,6-dicarboxylate {ECO:0000269|PubMed:7142106};
CC       pH dependence:
CC         Optimum pH is 8.4-8.8 for the hydrolysis of 2-pyrone-4,6-
CC         dicarboxylate. {ECO:0000269|PubMed:7142106};
CC   -!- INDUCTION: Induced by 4-hydroxybenzoate. {ECO:0000269|PubMed:7142106}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of this gene results in a strain
CC       unable to grow on protocatechuate and a variety of aromatic substrates
CC       funnelled through this compound (m- and p-hydroxybenzoate, p-
CC       sulfobenzoate, phthalate, isophthalate, terephthalate, vanillate,
CC       isovanillate and veratrate). Growth on benzoate and o-aminobenzoate
CC       (anthranilate) is not affected in the mutant strain, indicating that
CC       these substrates are metabolized via a different lower pathway.
CC       {ECO:0000269|PubMed:11495993}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       PDC hydrolase family. {ECO:0000305}.
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DR   EMBL; AF305325; AAK73571.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q93PS7; -.
DR   SMR; Q93PS7; -.
DR   BioCyc; MetaCyc:MON-3463; -.
DR   GO; GO:0047554; F:2-pyrone-4,6-dicarboxylate lactonase activity; ISS:UniProtKB.
DR   GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IDA:UniProtKB.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF04909; Amidohydro_2; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Hydrolase.
FT   CHAIN           1..305
FT                   /note="2-pyrone-4,6-dicarbaxylate hydrolase"
FT                   /id="PRO_0000422784"
FT   ACT_SITE        258
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O87170"
FT   BINDING         32..34
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O87170"
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O87170"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O87170"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O87170"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O87170"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O87170"
FT   BINDING         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O87170"
FT   BINDING         263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O87170"
SQ   SEQUENCE   305 AA;  34451 MW;  2167B504424FDDDF CRC64;
     MSQFEKTPGW LDWYANPSKP QFKLPAGAVD AHCHVFGPGN EFPFAPERKY TPCDASKAQL
     YALRDHLGFA RNVVVQATCH GADNRAMVDA CKSSGGKARG VATVKRSISD AELQQLHDAG
     VRGVRFNFVK RLVDFTPKDE LMEIAGRIAK LGWHVVIYFE AVDLPELWDF FTALPTTVVV
     DHMGRPDVTK GVDSEEFALF LKFMREHQNV WSKVSCPERL SVTGPKALNG EQNAYRDVVP
     FARRVVEEFP DRVLWGTDWP HPNLKDHMPD DGLLVDFIPH IAPTAELQQK LLVDNPMRLY
     WPEEV