Reviewed, UniProtKB/Swiss-Prot O67988 (CLCD_RHOOP)

Names and origin

Protein names

Recommended name:
    Carboxymethylenebutenolidase
    EC=3.1.1.45
Alternative name(s):
    Dienelactone hydrolase
      Short name=DLH

Gene names

Name:

clcD

Organism

Rhodococcus opacus (Nocardia opaca)

Taxonomic identifier

37919 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length	252 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Ring cleavage of cyclic ester dienelactone to produce maleylacetate.
Catalytic activity	4-carboxymethylenebut-2-en-4-olide + H2O = 4-oxohex-2-enedioate.
Pathway	Aromatic compound metabolism; 3-chlorocatechol degradation.
Sequence similarities	Belongs to the dienelactone hydrolase family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Molecular function	Hydrolase Serine esterase
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	carboxymethylenebutenolidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 252	252	Carboxymethylenebutenolidase		PRO_0000161572
Sites
	Active site	126	1	By similarity
	Active site	183	1	By similarity
	Active site	214	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	O67988-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: E7E73E7743CE7E9C	FASTA	252	27,304
	10 20 30 40 50 60 MCHNKSSAPP TPAHISIQQN RTPGTDPVPY LHASSDTGSG DTIVLLTDIF GVTPFYRHLA 70 80 90 100 110 120 AMLAEKGHDV VIPDVFHRVG HATDPGRDAA LARRRQLDDR LAIEDIERTV AHTVDDQQTF 130 140 150 160 170 180 GVLGFCLGGS FALLTAAAHP NQVTATYYAF PKGAPGAKVP VKPPLEAADA IDGPVLCHWG 190 200 210 220 230 240 RDDYIDHEEI DQLEQILASA PGPSEIRWYD NAGHSFLAGL TEPNHPSTAA AHDSWQRTVE 250 FFERYLTVGS AN

References

[1]

"Evolutionary relationship between chlorocatechol catabolic enzymes from Rhodococcus opacus 1CP and their counterparts in proteobacteria: sequence divergence and functional convergence." Eulberg D., Kourbatova E.M., Golovleva L.A., Schloemann M. J. Bacteriol. 180:1082-1094(1998) [PubMed: 9495745] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 1CP.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF003948 Genomic DNA. Translation: AAC38252.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.1.1.45. 2206.
Family and domain databases
InterPro	IPR002925. Dienelactn_hydro. [Graphical view]
Pfam	PF01738. DLH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CLCD_RHOOP

Accession

Primary (citable) accession number: O67988

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	August 1, 1998
Last modified:	January 20, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)