P0A114 (CLCD_PSEPU) Reviewed, UniProtKB/Swiss-Prot

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 pAC27

Organism

Pseudomonas putida (Arthrobacter siderocapsulatus)

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas putida group

Protein attributes

Sequence length	236 AA.
Sequence status	Complete.
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	carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW 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_0000161570

Sites

Active site

123

1

Active site

171

1

Active site

202

1

Secondary structure

1

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236

Helix Strand Turn

Details...

Beta strand

18 – 21

4

Beta strand

27 – 34

8

Helix

42 – 53

12

Beta strand

57 – 61

5

Helix

63 – 66

4

Helix

78 – 90

13

Helix

93 – 107

15

Beta strand

113 – 122

10

Helix

124 – 134

11

Beta strand

138 – 145

8

Helix

149 – 151

3

Helix

153 – 158

6

Beta strand

163 – 168

6

Beta strand

172 – 174

3

Helix

176 – 186

11

Beta strand

192 – 197

6

Turn

202 – 205

4

Helix

214 – 228

15

Helix

229 – 231

3

Sequences

	Sequence		Length	Mass (Da)
	P0A114 [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]	"Organization and nucleotide sequence determination of a gene cluster involved in 3-chlorocatechol degradation." Frantz B., Chakrabarty A.M. Proc. Natl. Acad. Sci. U.S.A. 84:4460-4464(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: AC859.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M16964 Genomic DNA. Translation: AAA98284.1.

PIR

C27058.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GGV	X-ray	2.50	A	1-232	[»]
1ZI6	X-ray	1.70	A	1-236	[»]
1ZI8	X-ray	1.40	A	1-236	[»]
1ZI9	X-ray	1.50	A	1-236	[»]
1ZIC	X-ray	1.70	A	1-236	[»]
1ZIX	X-ray	1.80	A	1-236	[»]
1ZIY	X-ray	1.90	A	1-236	[»]
1ZJ4	X-ray	1.70	A	1-236	[»]
1ZJ5	X-ray	1.70	A	1-236	[»]

ProteinModelPortal

P0A114.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

UniPathway

UPA00083.

Family and domain databases

InterPro

IPR002925. Dienelactn_hydro.
[Graphical view]

Pfam

PF01738. DLH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A114.

Entry information

Entry name

CLCD_PSEPU

Accession

Primary (citable) accession number: P0A114
Secondary accession number(s): P11453

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	March 1, 2005
Last modified:	April 3, 2013
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program