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