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CLCD_RHOOP
ID   CLCD_RHOOP              Reviewed;         252 AA.
AC   O67988;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Carboxymethylenebutenolidase;
DE            EC=3.1.1.45;
DE   AltName: Full=Dienelactone hydrolase;
DE            Short=DLH;
GN   Name=clcD;
OS   Rhodococcus opacus (Nocardia opaca).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=37919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1CP;
RX   PubMed=9495745; DOI=10.1128/jb.180.5.1082-1094.1998;
RA   Eulberg D., Kourbatova E.M., Golovleva L.A., Schloemann M.;
RT   "Evolutionary relationship between chlorocatechol catabolic enzymes from
RT   Rhodococcus opacus 1CP and their counterparts in proteobacteria: sequence
RT   divergence and functional convergence.";
RL   J. Bacteriol. 180:1082-1094(1998).
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   -!- SIMILARITY: Belongs to the dienelactone hydrolase family.
CC       {ECO:0000305}.
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DR   EMBL; AF003948; AAC38252.1; -; Genomic_DNA.
DR   RefSeq; WP_065493673.1; NZ_CP009112.1.
DR   AlphaFoldDB; O67988; -.
DR   SMR; O67988; -.
DR   ESTHER; rhoop-clcd; Dienelactone_hydrolase.
DR   GeneID; 66790433; -.
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; Serine esterase.
FT   CHAIN           1..252
FT                   /note="Carboxymethylenebutenolidase"
FT                   /id="PRO_0000161572"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        183
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        214
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   252 AA;  27304 MW;  E7E73E7743CE7E9C CRC64;
     MCHNKSSAPP TPAHISIQQN RTPGTDPVPY LHASSDTGSG DTIVLLTDIF GVTPFYRHLA
     AMLAEKGHDV VIPDVFHRVG HATDPGRDAA LARRRQLDDR LAIEDIERTV AHTVDDQQTF
     GVLGFCLGGS FALLTAAAHP NQVTATYYAF PKGAPGAKVP VKPPLEAADA IDGPVLCHWG
     RDDYIDHEEI DQLEQILASA PGPSEIRWYD NAGHSFLAGL TEPNHPSTAA AHDSWQRTVE
     FFERYLTVGS AN
 
 
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