ID   TCBE_PSESQ              Reviewed;         238 AA.
AC   P27100;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   28-JAN-2026, entry version 73.
DE   RecName: Full=Carboxymethylenebutenolidase;
DE            EC=3.1.1.45;
DE   AltName: Full=Dienelactone hydrolase;
DE            Short=DLH;
GN   Name=tcbE;
OS   Pseudomonas sp. (strain P51).
OG   Plasmid pP51.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pseudomonadales; Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=65067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2013566; DOI=10.1128/jb.173.8.2425-2434.1991;
RA   van der Meer J.R., Eggen R.I., Zehnder A.J., de Vos W.M.;
RT   "Sequence analysis of the Pseudomonas sp. strain P51 tcb gene cluster,
RT   which encodes metabolism of chlorinated catechols: evidence for
RT   specialization of catechol 1,2-dioxygenases for chlorinated substrates.";
RL   J. Bacteriol. 173:2425-2434(1991).
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; M57629; AAD13628.1; -; Genomic_DNA.
DR   PIR; D43673; D43673.
DR   AlphaFoldDB; P27100; -.
DR   SMR; P27100; -.
DR   ESTHER; alceu-CBNC; Dienelactone_hydrolase.
DR   BioCyc; MetaCyc:MONOMER-14406; -.
DR   UniPathway; UPA00083; -.
DR   GO; GO:0008806; F:carboxymethylenebutenolidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase_fold.
DR   InterPro; IPR002925; Dienelactn_hydro.
DR   InterPro; IPR051049; Dienelactone_hydrolase-like.
DR   PANTHER; PTHR46623:SF6; ALPHA_BETA-HYDROLASES SUPERFAMILY PROTEIN; 1.
DR   PANTHER; PTHR46623; CARBOXYMETHYLENEBUTENOLIDASE-RELATED; 1.
DR   Pfam; PF01738; DLH; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Hydrolase; Plasmid; Serine esterase.
FT   CHAIN           1..238
FT                   /note="Carboxymethylenebutenolidase"
FT                   /id="PRO_0000161573"
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   238 AA;  25812 MW;  DB57EAD5229C03C8 CRC64;
     MLTEGLSIDA KGGGRFGAHL QLPARGRGPV VMVAQEIFGV NPFMTEVLAW LASEGFVGLC
     PDLYWRHGPG IEFDPNDEVQ RARALGMFRD YKLEDGVADL RATVAYAASQ PFCDGGVAVI
     GYCLGGALAY EVAAEGFAQC CVGYYGVGFE KRLERARLVK TPSMFHMGTN DHFVTAEARQ
     LITNAFEANP AIALHWYDAG HSFARASSPN FSPEATRTAN ARTLEMLKRM KPIGTIGQ
//