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P0A114

- CLCD_PSEPU

UniProt

P0A114 - CLCD_PSEPU

Protein

Carboxymethylenebutenolidase

Gene

clcD

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 35 (01 Oct 2014)
      Sequence version 1 (01 Mar 2005)
      Previous versions | rss
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    • Comment

    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

    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 – 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 – 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.
    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

    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: October 1, 2014
    This is version 35 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