CLCD_PSEKB
ID CLCD_PSEKB Reviewed; 236 AA.
AC P0A115; P11453;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Carboxymethylenebutenolidase;
DE EC=3.1.1.45;
DE AltName: Full=Dienelactone hydrolase;
DE Short=DLH;
GN Name=clcD;
OS Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13).
OG Plasmid pB13.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1301098;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3804974; DOI=10.1128/jb.169.2.704-709.1987;
RA Frantz B., Ngai K.-L., Chatterjee D.K., Ornston L.N., Chakrabarty A.M.;
RT "Nucleotide sequence and expression of clcD, a plasmid-borne dienelactone
RT hydrolase gene from Pseudomonas sp. strain B13.";
RL J. Bacteriol. 169:704-709(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9171435; DOI=10.1128/jb.179.11.3801-3803.1997;
RA Kasberg T., Seibert V., Schlomann M., Reineke W.;
RT "Cloning, characterization, and sequence analysis of the clcE gene encoding
RT the maleylacetate reductase of Pseudomonas sp. strain B13.";
RL J. Bacteriol. 179:3801-3803(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=3221394; DOI=10.1016/0022-2836(88)90587-6;
RA Pathak D., Ngai K.L., Ollis D.;
RT "X-ray crystallographic structure of dienelactone hydrolase at 2.8 A.";
RL J. Mol. Biol. 204:435-445(1988).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=2380986; DOI=10.1016/0022-2836(90)90196-s;
RA Pathak D., Ollis D.;
RT "Refined structure of dienelactone hydrolase at 1.8 A.";
RL J. Mol. Biol. 214:497-525(1990).
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; M15201; AAA25770.1; -; Genomic_DNA.
DR EMBL; AF019038; AAB71539.1; -; Genomic_DNA.
DR PIR; S02022; S02022.
DR PDB; 1DIN; X-ray; 1.80 A; A=1-236.
DR PDB; 4P93; X-ray; 1.85 A; A/B=1-236.
DR PDB; 4U2B; X-ray; 1.70 A; A=1-236.
DR PDB; 4U2C; X-ray; 1.95 A; A=1-236.
DR PDB; 4U2D; X-ray; 1.67 A; A=1-236.
DR PDB; 4U2E; X-ray; 1.70 A; A=1-236.
DR PDB; 4U2F; X-ray; 1.80 A; A=1-236.
DR PDB; 4U2G; X-ray; 1.80 A; A=1-236.
DR PDBsum; 1DIN; -.
DR PDBsum; 4P93; -.
DR PDBsum; 4U2B; -.
DR PDBsum; 4U2C; -.
DR PDBsum; 4U2D; -.
DR PDBsum; 4U2E; -.
DR PDBsum; 4U2F; -.
DR PDBsum; 4U2G; -.
DR AlphaFoldDB; P0A115; -.
DR SMR; P0A115; -.
DR STRING; 1301098.PKB_3276; -.
DR DrugBank; DB02153; 3-sulfino-L-alanine.
DR DrugBank; DB01973; O-Benzylsulfonyl-Serine.
DR ESTHER; psepu-clcd1; Dienelactone_hydrolase.
DR eggNOG; COG0412; Bacteria.
DR BioCyc; MetaCyc:MON-14382; -.
DR BRENDA; 3.1.1.45; 5180.
DR UniPathway; UPA00083; -.
DR EvolutionaryTrace; P0A115; -.
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 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Hydrolase; Plasmid;
KW Serine esterase.
FT CHAIN 1..236
FT /note="Carboxymethylenebutenolidase"
FT /id="PRO_0000161571"
FT ACT_SITE 123
FT ACT_SITE 171
FT ACT_SITE 202
FT MUTAGEN 123
FT /note="C->S: Drastically reduced activity."
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:4U2D"
FT STRAND 24..34
FT /evidence="ECO:0007829|PDB:4U2D"
FT HELIX 42..53
FT /evidence="ECO:0007829|PDB:4U2D"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:4U2D"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:4U2D"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:4U2D"
FT HELIX 93..108
FT /evidence="ECO:0007829|PDB:4U2D"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:4U2D"
FT HELIX 124..135
FT /evidence="ECO:0007829|PDB:4U2D"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:4U2D"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:4U2D"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:4U2D"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:4U2D"
FT HELIX 176..187
FT /evidence="ECO:0007829|PDB:4U2D"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:4U2D"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:4U2D"
FT HELIX 214..228
FT /evidence="ECO:0007829|PDB:4U2D"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:4U2D"
SQ SEQUENCE 236 AA; 25555 MW; F630F3D2793730D4 CRC64;
MLTEGISIQS YDGHTFGALV GSPAKAPAPV IVIAQEIFGV NAFMRETVSW LVDQGYAAVC
PDLYARQAPG TALDPQDERQ REQAYKLWQA FDMEAGVGDL EAAIRYARHQ PYSNGKVGLV
GYCLGGALAF LVAAKGYVDR AVGYYGVGLE KQLKKVPEVK HPALFHMGGQ DHFVPAPSRQ
LITEGFGANP LLQVHWYEEA GHSFARTSSS GYVASAAALA NERRLDFLAP LQSKKP
