ID   TFDE1_CUPPJ             Reviewed;         234 AA.
AC   P27136; Q46M68;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Carboxymethylenebutenolidase 1;
DE            EC=3.1.1.45;
DE   AltName: Full=Carboxymethylenebutenolidase I;
DE   AltName: Full=Dienelactone hydrolase I;
DE            Short=DLH I;
GN   Name=tfdEI; Synonyms=tfdE; OrderedLocusNames=Reut_D6464;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OG   Plasmid pJP4, and Plasmid pPJ4.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pJP4;
RX   PubMed=2185214; DOI=10.1128/jb.172.5.2351-2359.1990;
RA   Perkins E.J., Gordon M.P., Caceres O., Lurquin P.F.;
RT   "Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase
RT   and dichlorocatechol oxidative operons of plasmid pJP4.";
RL   J. Bacteriol. 172:2351-2359(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pJP4;
RX   PubMed=15186344; DOI=10.1111/j.1462-2920.2004.00596.x;
RA   Trefault N., De la Iglesia R., Molina A.M., Manzano M., Ledger T.,
RA   Perez-Pantoja D., Sanchez M.A., Stuardo M., Gonzalez B.;
RT   "Genetic organization of the catabolic plasmid pJP4 from Ralstonia eutropha
RT   JMP134 (pJP4) reveals mechanisms of adaptation to chloroaromatic pollutants
RT   and evolution of specialized chloroaromatic degradation pathways.";
RL   Environ. Microbiol. 6:655-668(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197; PLASMID=pPJ4;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
CC   -!- FUNCTION: Ring cleavage of cyclic ester dienelactone to produce
CC       maleylacetate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(5-oxo-2,5-dihydrofuran-2-ylidene)acetate + H2O = 4-oxohex-
CC         2-enedioate + H(+); Xref=Rhea:RHEA:12372, ChEBI:CHEBI:12040,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57263; EC=3.1.1.45;
CC   -!- PATHWAY: Aromatic compound metabolism; 3-chlorocatechol degradation.
CC   -!- SUBUNIT: Monomer.
CC   -!- MISCELLANEOUS: Carboxymethylenebutenolidase is specific for
CC       dienelactone and has no activity toward enol-lactones.
CC   -!- SIMILARITY: Belongs to the dienelactone hydrolase family.
CC       {ECO:0000305}.
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DR   EMBL; M35097; AAA98264.1; -; Genomic_DNA.
DR   EMBL; AY365053; AAR31037.1; -; Genomic_DNA.
DR   EMBL; CP000093; AAZ65762.1; -; Genomic_DNA.
DR   PIR; C35255; C35255.
DR   RefSeq; WP_011178384.1; NZ_AY365053.1.
DR   AlphaFoldDB; P27136; -.
DR   SMR; P27136; -.
DR   ESTHER; alceu-tfe1; Dienelactone_hydrolase.
DR   EnsemblBacteria; AAZ65762; AAZ65762; Reut_D6464.
DR   GeneID; 55536836; -.
DR   KEGG; reu:Reut_D6464; -.
DR   HOGENOM; CLU_054590_7_3_4; -.
DR   OMA; VSAFSYP; -.
DR   OrthoDB; 1889569at2; -.
DR   BioCyc; MetaCyc:MON-14412; -.
DR   UniPathway; UPA00083; -.
DR   GO; GO:0008806; F:carboxymethylenebutenolidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002925; Dienelactn_hydro.
DR   Pfam; PF01738; DLH; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Hydrolase; Plasmid; Serine esterase.
FT   CHAIN           1..234
FT                   /note="Carboxymethylenebutenolidase 1"
FT                   /id="PRO_0000161574"
FT   ACT_SITE        123
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        201
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   234 AA;  25428 MW;  1D0658C527CA87BA CRC64;
     MLSDGVEITS RSGGRFGAYL GKPTTDSAPI VVIAQEIFGI TPFIRETVEW LVGAGFGCVC
     PDLYWRQAPN IELDANVPSE REQALALFRD FDMEAGVNDL SCAIEYARAL PFSNGRVAVV
     GYCLGGALAF DVAARSLADC SIGYYGVGLE KKVSLVPAIT RPAMFHMGTK DHYVTEEARS
     ILEEHFGRNK NLSLHWYPVG HSFARSSSPN FDQAATTVAN ARTLELLAML KDPS