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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.

Pathwayi: 3-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)DescriptionActionsGraphical viewLength
Active sitei1231
Active sitei1711
Active sitei2021

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001615701 – 236CarboxymethylenebutenolidaseAdd BLAST236

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1236
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi18 – 21Combined sources4
Beta strandi27 – 34Combined sources8
Helixi42 – 53Combined sources12
Beta strandi57 – 61Combined sources5
Helixi63 – 66Combined sources4
Helixi78 – 90Combined sources13
Helixi93 – 107Combined sources15
Beta strandi113 – 122Combined sources10
Helixi124 – 134Combined sources11
Beta strandi138 – 145Combined sources8
Helixi149 – 151Combined sources3
Helixi153 – 158Combined sources6
Beta strandi163 – 168Combined sources6
Beta strandi172 – 174Combined sources3
Helixi176 – 186Combined sources11
Beta strandi192 – 197Combined sources6
Turni202 – 205Combined sources4
Helixi214 – 228Combined sources15
Helixi229 – 231Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiP0A114.
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
PDB 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.
SMRiP0A114.
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...

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: November 2, 2016
This is version 39 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

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 one 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.