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P0A114

- CLCD_PSEPU

UniProt

P0A114 - CLCD_PSEPU

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Protein
Carboxymethylenebutenolidase
Gene
clcD
Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - 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

Sites

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

GO - Molecular functioni

  1. carboxymethylenebutenolidase activity Source: UniProtKB-EC

GO - Biological processi

  1. aromatic compound catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Enzyme and pathway databases

UniPathwayiUPA00083.

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 – 236236Carboxymethylenebutenolidase
PRO_0000161570Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortaliP0A114.

Miscellaneous databases

EvolutionaryTraceiP0A114.

Family & Domainsi

Sequence similaritiesi

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

MLTEGISIQS YDGHTFGALV GSPAKAPAPV IVIAQEIFGV NAFMRETVSW    50
LVDQGYAAVC PDLYARQAPG TALDPQDERQ REQAYKLWQA FDMEAGVGDL 100
EAAIRYARHQ PYSNGKVGLV GYCLGGALAF LVAAKGYVDR AVGYYGVGLE 150
KQLKKVPEVK HPALFHMGGQ DHFVPAPSRQ LITEGFGANP LLQVHWYEEA 200
GHSFARTSSS GYVASAAALA NERRLDFLAP LQSKKP 236
Length:236
Mass (Da):25,555
Last modified:March 1, 2005 - v1
Checksum:iF630F3D2793730D4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M16964 Genomic DNA. Translation: AAA98284.1.
PIRiC27058.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M16964 Genomic DNA. Translation: AAA98284.1 .
PIRi C27058.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P0A114.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00083 .

Miscellaneous databases

EvolutionaryTracei P0A114.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR002925. Dienelactn_hydro.
[Graphical view ]
Pfami PF01738. DLH. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

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 11, 2014
This is version 34 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

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