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Protein

Carboxymethylenebutenolidase

Gene

clcD

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Ring cleavage of cyclic ester dienelactone to produce maleylacetate.

Catalytic activityi

4-carboxymethylenebut-2-en-4-olide + H2O = 4-oxohex-2-enedioate.

Pathway:i3-chlorocatechol degradation

This protein is involved in the pathway 3-chlorocatechol degradation, which is part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the pathway 3-chlorocatechol degradation and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei123 – 1231
Active sitei171 – 1711
Active sitei202 – 2021

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Enzyme and pathway databases

UniPathwayiUPA00083.

Protein family/group databases

ESTHERipsepu-clcd1. Dienelactone_hydrolase.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxymethylenebutenolidase (EC:3.1.1.45)
Alternative name(s):
Dienelactone hydrolase
Short name:
DLH
Gene namesi
Name:clcD
Encoded oniPlasmid pAC270 Publication
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 236236CarboxymethylenebutenolidasePRO_0000161570Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
236
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 214Combined sources
Beta strandi27 – 348Combined sources
Helixi42 – 5312Combined sources
Beta strandi57 – 615Combined sources
Helixi63 – 664Combined sources
Helixi78 – 9013Combined sources
Helixi93 – 10715Combined sources
Beta strandi113 – 12210Combined sources
Helixi124 – 13411Combined sources
Beta strandi138 – 1458Combined sources
Helixi149 – 1513Combined sources
Helixi153 – 1586Combined sources
Beta strandi163 – 1686Combined sources
Beta strandi172 – 1743Combined sources
Helixi176 – 18611Combined sources
Beta strandi192 – 1976Combined sources
Turni202 – 2054Combined sources
Helixi214 – 22815Combined sources
Helixi229 – 2313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4P92X-ray1.65A1-236[»]
ProteinModelPortaliP0A114.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A114.

Family & Domainsi

Sequence similaritiesi

Belongs to the dienelactone hydrolase family.Curated

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002925. Dienelactn_hydro.
[Graphical view]
PfamiPF01738. DLH. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A114-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTEGISIQS YDGHTFGALV GSPAKAPAPV IVIAQEIFGV NAFMRETVSW
60 70 80 90 100
LVDQGYAAVC PDLYARQAPG TALDPQDERQ REQAYKLWQA FDMEAGVGDL
110 120 130 140 150
EAAIRYARHQ PYSNGKVGLV GYCLGGALAF LVAAKGYVDR AVGYYGVGLE
160 170 180 190 200
KQLKKVPEVK HPALFHMGGQ DHFVPAPSRQ LITEGFGANP LLQVHWYEEA
210 220 230
GHSFARTSSS GYVASAAALA NERRLDFLAP LQSKKP
Length:236
Mass (Da):25,555
Last modified:March 1, 2005 - v1
Checksum:iF630F3D2793730D4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16964 Genomic DNA. Translation: AAA98284.1.
PIRiC27058.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16964 Genomic DNA. Translation: AAA98284.1.
PIRiC27058.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4P92X-ray1.65A1-236[»]
ProteinModelPortaliP0A114.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERipsepu-clcd1. Dienelactone_hydrolase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00083.

Miscellaneous databases

EvolutionaryTraceiP0A114.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002925. Dienelactn_hydro.
[Graphical view]
PfamiPF01738. DLH. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiCLCD_PSEPU
AccessioniPrimary (citable) accession number: P0A114
Secondary accession number(s): P11453
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: June 24, 2015
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Carboxymethylenebutenolidase is specific for dienelactone and has no activity toward enol-lactones.

Keywords - Technical termi

3D-structure, Plasmid

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.