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P0A114 (CLCD_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carboxymethylenebutenolidase

EC=3.1.1.45
Alternative name(s):
Dienelactone hydrolase
Short name=DLH
Gene names
Name:clcD
Encoded onPlasmid pAC27
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length236 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processAromatic hydrocarbons catabolism
   Molecular functionHydrolase
Serine esterase
   Technical term3D-structure
Plasmid
Gene Ontology (GO)
   Biological_processaromatic compound catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncarboxymethylenebutenolidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 236236Carboxymethylenebutenolidase
PRO_0000161570

Sites

Active site1231
Active site1711
Active site2021

Secondary structure

...................................... 236
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A114 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: F630F3D2793730D4

FASTA23625,555
        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 

« Hide

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.
PIRC27058.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GGVX-ray2.50A1-232[»]
1ZI6X-ray1.70A1-236[»]
1ZI8X-ray1.40A1-236[»]
1ZI9X-ray1.50A1-236[»]
1ZICX-ray1.70A1-236[»]
1ZIXX-ray1.80A1-236[»]
1ZIYX-ray1.90A1-236[»]
1ZJ4X-ray1.70A1-236[»]
1ZJ5X-ray1.70A1-236[»]
ProteinModelPortalP0A114.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00083.

Family and domain databases

InterProIPR002925. Dienelactn_hydro.
[Graphical view]
PfamPF01738. DLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A114.

Entry information

Entry nameCLCD_PSEPU
AccessionPrimary (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: January 22, 2014
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways