ID CLCD_PSEPU Reviewed; 236 AA. AC P0A114; P11453; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 49. DE RecName: Full=Carboxymethylenebutenolidase; DE EC=3.1.1.45; DE AltName: Full=Dienelactone hydrolase; DE Short=DLH; GN Name=clcD; OS Pseudomonas putida (Arthrobacter siderocapsulatus). OG Plasmid pAC27. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=AC859; RX PubMed=3299368; DOI=10.1073/pnas.84.13.4460; RA Frantz B., Chakrabarty A.M.; RT "Organization and nucleotide sequence determination of a gene cluster RT involved in 3-chlorocatechol degradation."; RL Proc. Natl. Acad. Sci. U.S.A. 84:4460-4464(1987). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M16964; AAA98284.1; -; Genomic_DNA. DR PIR; C27058; C27058. DR PDB; 1GGV; X-ray; 2.50 A; A=1-232. DR PDB; 1ZI6; X-ray; 1.70 A; A=1-236. DR PDB; 1ZI8; X-ray; 1.40 A; A=1-236. DR PDB; 1ZI9; X-ray; 1.50 A; A=1-236. DR PDB; 1ZIC; X-ray; 1.70 A; A=1-236. DR PDB; 1ZIX; X-ray; 1.80 A; A=1-236. DR PDB; 1ZIY; X-ray; 1.90 A; A=1-236. DR PDB; 1ZJ4; X-ray; 1.70 A; A=1-236. DR PDB; 1ZJ5; X-ray; 1.70 A; A=1-236. DR PDB; 4P92; X-ray; 1.65 A; A=1-236. DR PDBsum; 1GGV; -. DR PDBsum; 1ZI6; -. DR PDBsum; 1ZI8; -. DR PDBsum; 1ZI9; -. DR PDBsum; 1ZIC; -. DR PDBsum; 1ZIX; -. DR PDBsum; 1ZIY; -. DR PDBsum; 1ZJ4; -. DR PDBsum; 1ZJ5; -. DR PDBsum; 4P92; -. DR AlphaFoldDB; P0A114; -. DR SMR; P0A114; -. DR ESTHER; psepu-clcd1; Dienelactone_hydrolase. DR UniPathway; UPA00083; -. DR EvolutionaryTrace; P0A114; -. 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; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR002925; Dienelactn_hydro. DR PANTHER; PTHR46623; CARBOXYMETHYLENEBUTENOLIDASE-RELATED; 1. DR PANTHER; PTHR46623:SF11; CARBOXYMETHYLENEBUTENOLIDASE-RELATED; 1. DR Pfam; PF01738; DLH; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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_0000161570" FT ACT_SITE 123 FT ACT_SITE 171 FT ACT_SITE 202 FT STRAND 18..21 FT /evidence="ECO:0007829|PDB:1ZI8" FT STRAND 27..34 FT /evidence="ECO:0007829|PDB:1ZI8" FT HELIX 42..53 FT /evidence="ECO:0007829|PDB:1ZI8" FT STRAND 57..61 FT /evidence="ECO:0007829|PDB:1ZI8" FT HELIX 63..66 FT /evidence="ECO:0007829|PDB:1ZI8" FT HELIX 78..90 FT /evidence="ECO:0007829|PDB:1ZI8" FT HELIX 93..107 FT /evidence="ECO:0007829|PDB:1ZI8" FT STRAND 113..122 FT /evidence="ECO:0007829|PDB:1ZI8" FT HELIX 124..134 FT /evidence="ECO:0007829|PDB:1ZI8" FT STRAND 138..145 FT /evidence="ECO:0007829|PDB:1ZI8" FT HELIX 149..151 FT /evidence="ECO:0007829|PDB:1ZI8" FT HELIX 153..158 FT /evidence="ECO:0007829|PDB:1ZI8" FT STRAND 163..168 FT /evidence="ECO:0007829|PDB:1ZI8" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:1ZJ4" FT HELIX 176..186 FT /evidence="ECO:0007829|PDB:1ZI8" FT STRAND 192..197 FT /evidence="ECO:0007829|PDB:1ZI8" FT TURN 202..205 FT /evidence="ECO:0007829|PDB:1ZI8" FT HELIX 214..228 FT /evidence="ECO:0007829|PDB:1ZI8" FT HELIX 229..231 FT /evidence="ECO:0007829|PDB:1ZI8" 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 //