Reviewed, UniProtKB/Swiss-Prot P0A115 (CLCD_PSESB)

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

Encoded on

Plasmid pB13

Organism

Pseudomonas sp. (strain B13)

Taxonomic identifier

65741 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	236 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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.
Subunit structure	Monomer.
Miscellaneous	Carboxymethylenebutenolidase is specific for dienelactone and has no activity toward enol-lactones.
Sequence similarities	Belongs to the dienelactone hydrolase family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Molecular function	Hydrolase Serine esterase
Technical term	3D-structure Plasmid
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 – 236

236

Carboxymethylenebutenolidase

PRO_0000161571

Sites

Active site

123

1

Active site

171

1

Active site

202

1

Experimental info

Mutagenesis

123

1

C → S: Drastically reduced activity.

Secondary structure

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236

Helix Strand Turn

Details...

Turn

4 – 5

2

Turn

11 – 12

2

Beta strand

18 – 21

4

Beta strand

28 – 34

7

Turn

37 – 38

2

Helix

42 – 53

12

Turn

54 – 55

2

Beta strand

57 – 61

5

Helix

63 – 66

4

Turn

67

1

Turn

69 – 70

2

Turn

75 – 76

2

Helix

78 – 89

12

Turn

90

1

Helix

93 – 108

16

Turn

109

1

Turn

111 – 112

2

Beta strand

113 – 122

10

Turn

123

1

Helix

124 – 135

12

Turn

136

1

Beta strand

140 – 144

5

Helix

149 – 158

10

Beta strand

163 – 168

6

Turn

169 – 170

2

Turn

172 – 173

2

Helix

176 – 186

11

Turn

187 – 188

2

Turn

190 – 191

2

Beta strand

192 – 197

6

Turn

198 – 199

2

Turn

202 – 205

4

Turn

207 – 208

2

Turn

210 – 211

2

Helix

214 – 228

15

Helix

229 – 231

3

Sequences

	Sequence		Length	Mass (Da)
	P0A115-1 [UniParc]. Last modified March 1, 2005. Version 1. Checksum: F630F3D2793730D4	FASTA	236	25,555
	10 20 30 40 50 60 MLTEGISIQS YDGHTFGALV GSPAKAPAPV IVIAQEIFGV NAFMRETVSW LVDQGYAAVC 70 80 90 100 110 120 PDLYARQAPG TALDPQDERQ REQAYKLWQA FDMEAGVGDL EAAIRYARHQ PYSNGKVGLV 130 140 150 160 170 180 GYCLGGALAF LVAAKGYVDR AVGYYGVGLE KQLKKVPEVK HPALFHMGGQ DHFVPAPSRQ 190 200 210 220 230 LITEGFGANP LLQVHWYEEA GHSFARTSSS GYVASAAALA NERRLDFLAP LQSKKP

References

[1]	"Nucleotide sequence and expression of clcD, a plasmid-borne dienelactone hydrolase gene from Pseudomonas sp. strain B13." Frantz B., Ngai K.-L., Chatterjee D.K., Ornston L.N., Chakrabarty A.M. J. Bacteriol. 169:704-709(1987) [PubMed: 3804974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning, characterization, and sequence analysis of the clcE gene encoding the maleylacetate reductase of Pseudomonas sp. strain B13." Kasberg T., Seibert V., Schlomann M., Reineke W. J. Bacteriol. 179:3801-3803(1997) [PubMed: 9171435] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"X-ray crystallographic structure of dienelactone hydrolase at 2.8 A." Pathak D., Ngai K.L., Ollis D. J. Mol. Biol. 204:435-445(1988) [PubMed: 3221394] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[4]	"Refined structure of dienelactone hydrolase at 1.8 A." Pathak D., Ollis D. J. Mol. Biol. 214:497-525(1990) [PubMed: 2380986] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

M15201 Genomic DNA. Translation: AAA25770.1.
AF019038 Genomic DNA. Translation: AAB71539.1.

PIR

S02022.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DIN	X-ray	1.80	A	1-236	[»]

SMR

P0A115. Positions 1-233.

ModBase

Search...

Family and domain databases

InterPro

IPR002925. Dienelactn_hydro.
[Graphical view]

Pfam

PF01738. DLH. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CLCD_PSESB

Accession

Primary (citable) accession number: P0A115
Secondary accession number(s): P11453

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	March 1, 2005
Last modified:	June 16, 2009
This is version 22 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)