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Protein

4-hydroxybenzoyl-CoA thioesterase

Gene
N/A
Organism
Pseudomonas sp. (strain CBS-3)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes 4-hydroxybenzoate-CoA, and to a lesser extent benzoyl-CoA and 4-chlorobenzoate-CoA. Not active against aliphatic acyl-CoA thioesters, including palmitoyl-CoA, hexanoyl-CoA and acetyl-CoA.1 Publication

Catalytic activityi

4-hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA.PROSITE-ProRule annotation1 Publication

Enzyme regulationi

Unaffected by EDTA, Mg2+, Mn2+, Fe2+, Ca2+, Co2+ and Zn2+.1 Publication

Kineticsi

  1. KM=6 µM for 4-hydroxybenzoyl-CoA3 Publications
  2. KM=550 µM for 4-chlorobenzoyl-CoA3 Publications
  3. KM=200 µM for benzoyl-CoA3 Publications
  4. KM=270 µM for 4-hydroxybenzoyl-pantetheine3 Publications
  5. KM=56 µM for 4-methoxybenzoyl-CoA3 Publications
  6. KM=230 µM for 4-methylbenzoyl-CoA3 Publications
  7. KM=510 µM for benzoyl-CoA3 Publications
  8. KM=520 µM for 4-fluorobenzoyl-CoA3 Publications
  9. KM=300 µM for 4-trifluorobenzoyl-CoA3 Publications

    Pathwayi: 4-chlorobenzoate degradation

    This protein is involved in step 3 of the subpathway that synthesizes 4-hydroxybenzoate from 4-chlorobenzoate.1 Publication
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. 4-chlorobenzoyl coenzyme A dehalogenase, 4-chlorobenzoate--CoA ligase
    3. 4-hydroxybenzoyl-CoA thioesterase
    This subpathway is part of the pathway 4-chlorobenzoate degradation, which is itself part of Xenobiotic degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 4-hydroxybenzoate from 4-chlorobenzoate, the pathway 4-chlorobenzoate degradation and in Xenobiotic degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei17 – 171PROSITE-ProRule annotation2 Publications
    Binding sitei47 – 471Substrate1 Publication
    Binding sitei90 – 901Substrate1 Publication

    GO - Molecular functioni

    • 4-hydroxybenzoyl-CoA thioesterase activity Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14754.
    BRENDAi3.1.2.23. 5085.
    SABIO-RKP56653.
    UniPathwayiUPA01011; UER01022.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-hydroxybenzoyl-CoA thioesterase (EC:3.1.2.23)
    OrganismiPseudomonas sp. (strain CBS-3)
    Taxonomic identifieri72586 [NCBI]
    Taxonomic lineageiBacteriaProteobacteria

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi17 – 171D → E: Reduces catalytic activity. Little effect on substrate binding. 1 Publication
    Mutagenesisi17 – 171D → N: Drastically reduces catalytic activity. No effect on substrate binding. 1 Publication
    Mutagenesisi17 – 171D → S: Drastically reduces catalytic activity. 1 Publication
    Mutagenesisi32 – 321D → S: Substrate turnover rate is decreased. 1 Publication
    Mutagenesisi88 – 881R → A: No significant effect on catalytic activity or substrate binding. 1 Publication
    Mutagenesisi89 – 891R → L: No significant effect on catalytic activity or substrate binding. 1 Publication
    Mutagenesisi90 – 901K → A: Decreases substrate binding affinity. 1 Publication
    Mutagenesisi126 – 1261R → L: No significant effect on catalytic activity or substrate binding. 1 Publication
    Mutagenesisi128 – 1281R → A: No significant effect on catalytic activity or substrate binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 1411414-hydroxybenzoyl-CoA thioesterasePRO_0000087760Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.3 Publications

    Structurei

    Secondary structure

    1
    141
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 107Combined sources
    Helixi13 – 153Combined sources
    Beta strandi20 – 223Combined sources
    Helixi25 – 4117Combined sources
    Helixi47 – 548Combined sources
    Beta strandi56 – 583Combined sources
    Beta strandi61 – 688Combined sources
    Beta strandi77 – 8711Combined sources
    Beta strandi89 – 10113Combined sources
    Beta strandi107 – 12317Combined sources
    Beta strandi126 – 1305Combined sources
    Helixi134 – 1407Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BVQX-ray2.00A1-141[»]
    1LO7X-ray1.50A1-141[»]
    1LO8X-ray1.80A1-141[»]
    1LO9X-ray2.80A1-141[»]
    ProteinModelPortaliP56653.
    SMRiP56653. Positions 2-141.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP56653.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni59 – 613Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    KOiK01075.

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    InterProiIPR008272. HB-CoA_thioesterase_AS.
    IPR029069. HotDog_dom.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 1 hit.
    PROSITEiPS01328. 4HBCOA_THIOESTERASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P56653-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MARSITMQQR IEFGDCDPAG IVWFPNYHRW LDAASRNYFI KCGLPPWRQT
    60 70 80 90 100
    VVERGIVGTP IVSCNASFVC TASYDDVLTI ETCIKEWRRK SFVQRHSVSR
    110 120 130 140
    TTPGGDVQLV MRADEIRVFA MNDGERLRAI EVPADYIELC S
    Length:141
    Mass (Da):16,105
    Last modified:July 15, 1999 - v1
    Checksum:i410896EA5CC49F22
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti107 – 1071V → L in ABQ44580 (Ref. 2) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    EF569604 Genomic DNA. Translation: ABQ44580.1.

    Genome annotation databases

    KEGGiag:ABQ44580.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    EF569604 Genomic DNA. Translation: ABQ44580.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BVQX-ray2.00A1-141[»]
    1LO7X-ray1.50A1-141[»]
    1LO8X-ray1.80A1-141[»]
    1LO9X-ray2.80A1-141[»]
    ProteinModelPortaliP56653.
    SMRiP56653. Positions 2-141.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:ABQ44580.

    Phylogenomic databases

    KOiK01075.

    Enzyme and pathway databases

    UniPathwayiUPA01011; UER01022.
    BioCyciMetaCyc:MONOMER-14754.
    BRENDAi3.1.2.23. 5085.
    SABIO-RKP56653.

    Miscellaneous databases

    EvolutionaryTraceiP56653.

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    InterProiIPR008272. HB-CoA_thioesterase_AS.
    IPR029069. HotDog_dom.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 1 hit.
    PROSITEiPS01328. 4HBCOA_THIOESTERASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry namei4HBT_PSEUC
    AccessioniPrimary (citable) accession number: P56653
    Secondary accession number(s): A5JTM7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: July 15, 1999
    Last modified: July 6, 2016
    This is version 59 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    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.