Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

4-hydroxybenzoyl-CoA thioesterase

Gene

fcbC

Organism
Arthrobacter sp.
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

4-hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA.1 Publication

Kineticsi

  1. KM=243 µM for benzoyl-CoA1 Publication
  2. KM=1.24 µM for 4-hydroxybenzoyl-CoA1 Publication
  3. KM=22 µM for 3-hydroxybenzoyl-CoA1 Publication
  4. KM=29 µM for 2,5-dihydroxybenzoyl-CoA1 Publication
  5. KM=113 µM for 4-chlorobenzoyl-CoA1 Publication
  6. KM=140 µM for phenylacetyl-CoA1 Publication
  7. KM=2200 µM for acetyl-CoA1 Publication
  8. KM=1100 µM for propionyl-CoA1 Publication
  9. KM=930 µM for butyryl-CoA1 Publication
  10. KM=810 µM for crotonyl-CoA1 Publication

    pH dependencei

    Optimum pH is 4.6-9.6.1 Publication

    Pathwayi: 4-chlorobenzoate degradation

    This protein is involved in step 3 of the subpathway that synthesizes 4-hydroxybenzoate from 4-chlorobenzoate.
    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-2 (fcbB2), 4-chlorobenzoyl coenzyme A dehalogenase-1 (fcbB1), 4-chlorobenzoate--CoA ligase (fcbA1), 4-chlorobenzoate--CoA ligase (fcbA2)
    3. 4-hydroxybenzoyl-CoA thioesterase (fcbC)
    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 sitei73 – 7311 Publication

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    SABIO-RKQ04416.
    UniPathwayiUPA01011; UER01022.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-hydroxybenzoyl-CoA thioesterase1 Publication (EC:3.1.2.23)
    Short name:
    4-HBA-CoA thioesterase1 Publication
    Gene namesi
    Name:fcbCImported
    Synonyms:fcbC1Imported
    Encoded oniPlasmid pASU1Imported
    OrganismiArthrobacter sp.
    Taxonomic identifieri1667 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaeArthrobacter

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi73 – 731E → A: Drastically reduces catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 1511514-hydroxybenzoyl-CoA thioesterasePRO_0000400829Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Structurei

    Secondary structure

    1
    151
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi12 – 143Combined sources
    Helixi26 – 283Combined sources
    Helixi30 – 345Combined sources
    Beta strandi37 – 415Combined sources
    Beta strandi43 – 519Combined sources
    Helixi54 – 563Combined sources
    Beta strandi61 – 633Combined sources
    Helixi65 – 8420Combined sources
    Helixi85 – 873Combined sources
    Beta strandi89 – 10214Combined sources
    Beta strandi106 – 11813Combined sources
    Beta strandi120 – 13011Combined sources
    Beta strandi136 – 14813Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Q4SX-ray1.95A/B1-151[»]
    1Q4TX-ray1.60A/B1-151[»]
    1Q4UX-ray1.60A/B1-151[»]
    3R32X-ray1.80A/B1-151[»]
    3R34X-ray1.80A/B1-151[»]
    3R35X-ray1.80A/B1-151[»]
    3R36X-ray1.95A/B1-151[»]
    3R37X-ray1.80A/B1-151[»]
    3R3AX-ray1.80A/B1-151[»]
    3R3BX-ray1.80A/B1-151[»]
    3R3CX-ray1.80A/B1-151[»]
    3R3DX-ray1.75A/B1-151[»]
    3R3FX-ray1.75A/B1-151[»]
    3TEAX-ray1.80A/B1-151[»]
    ProteinModelPortaliQ04416.
    SMRiQ04416. Positions 10-151.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04416.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni100 – 1023Substrate binding

    Sequence similaritiesi

    Belongs to the thioesterase PaaI family.Curated

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    InterProiIPR029069. HotDog_dom.
    IPR003736. PAAI_dom.
    IPR006683. Thioestr_dom.
    [Graphical view]
    PfamiPF03061. 4HBT. 1 hit.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 1 hit.
    TIGRFAMsiTIGR00369. unchar_dom_1. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q04416-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MHRTSNGSHA TGGNLPDVAS HYPVAYEQTL DGTVGFVIDE MTPERATASV
    60 70 80 90 100
    EVTDTLRQRW GLVHGGAYCA LAEMLATEAT VAVVHEKGMM AVGQSNHTSF
    110 120 130 140 150
    FRPVKEGHVR AEAVRIHAGS TTWFWDVSLR DDAGRLCAVS SMSIAVRPRR

    D
    Length:151
    Mass (Da):16,394
    Last modified:November 1, 1996 - v1
    Checksum:i95738A4BBD241A7E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 371V → I in BAB40578 (Ref. 4) Curated
    Sequence conflicti67 – 671A → T in BAB40578 (Ref. 4) Curated
    Sequence conflicti114 – 1141V → I in BAB40578 (Ref. 4) Curated
    Sequence conflicti126 – 1261D → N in BAB40578 (Ref. 4) Curated

    Mass spectrometryi

    Molecular mass is 16394.40 Da from positions 1 - 151. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M93187 Genomic DNA. Translation: AAC80224.1.
    AF042490 Genomic DNA. Translation: AAF76242.1.
    AM231748 Genomic DNA. Translation: CAJ77823.1.
    AB041030 Genomic DNA. Translation: BAB40578.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M93187 Genomic DNA. Translation: AAC80224.1.
    AF042490 Genomic DNA. Translation: AAF76242.1.
    AM231748 Genomic DNA. Translation: CAJ77823.1.
    AB041030 Genomic DNA. Translation: BAB40578.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Q4SX-ray1.95A/B1-151[»]
    1Q4TX-ray1.60A/B1-151[»]
    1Q4UX-ray1.60A/B1-151[»]
    3R32X-ray1.80A/B1-151[»]
    3R34X-ray1.80A/B1-151[»]
    3R35X-ray1.80A/B1-151[»]
    3R36X-ray1.95A/B1-151[»]
    3R37X-ray1.80A/B1-151[»]
    3R3AX-ray1.80A/B1-151[»]
    3R3BX-ray1.80A/B1-151[»]
    3R3CX-ray1.80A/B1-151[»]
    3R3DX-ray1.75A/B1-151[»]
    3R3FX-ray1.75A/B1-151[»]
    3TEAX-ray1.80A/B1-151[»]
    ProteinModelPortaliQ04416.
    SMRiQ04416. Positions 10-151.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA01011; UER01022.
    SABIO-RKQ04416.

    Miscellaneous databases

    EvolutionaryTraceiQ04416.

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    InterProiIPR029069. HotDog_dom.
    IPR003736. PAAI_dom.
    IPR006683. Thioestr_dom.
    [Graphical view]
    PfamiPF03061. 4HBT. 1 hit.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 1 hit.
    TIGRFAMsiTIGR00369. unchar_dom_1. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "Cloning and sequence analysis of genes for dehalogenation of 4-chlorobenzoate from Arthrobacter sp. strain SU."
      Schmitz A., Gartemann K.H., Fiedler J., Grund E., Eichenlaub R.
      Appl. Environ. Microbiol. 58:4068-4071(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DSM 20407 / SUImported.
      Plasmid: pASU1
    2. "Isolation and characterization of IS1409, an insertion element of 4-chlorobenzoate-degrading Arthrobacter sp. strain TM1, and development of a system for transposon mutagenesis."
      Gartemann K.H., Eichenlaub R.
      J. Bacteriol. 183:3729-3736(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: NCIB 12013 / TM1Imported.
    3. "Cloning of the Arthrobacter sp. FG1 dehalogenase genes and construction of hybrid pathways in Pseudomonas putida strains."
      Radice F., Orlandi V., Massa V., Battini V., Bertoni G., Reineke W., Barbieri P.
      Appl. Microbiol. Biotechnol. 75:1111-1118(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: FG11 Publication.
    4. "4-chlorobenzoate dehalogenase genes are tandemly duplicated in Arthrobacter sp. FHP1."
      Miyashita K., Ogawa N., Tsumori Y.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: FHP1Imported.
    5. "Characterization of the 4-hydroxybenzoyl-coenzyme A thioesterase from Arthrobacter sp. strain SU."
      Zhuang Z., Gartemann K.H., Eichenlaub R., Dunaway-Mariano D.
      Appl. Environ. Microbiol. 69:2707-2711(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY.
      Strain: DSM 20407 / SU1 Publication.
    6. "The structure of 4-hydroxybenzoyl-CoA thioesterase from arthrobacter sp. strain SU."
      Thoden J.B., Zhuang Z., Dunaway-Mariano D., Holden H.M.
      J. Biol. Chem. 278:43709-43716(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND IN COMPLEX WITH PRODUCT, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF GLU-73.
      Strain: DSM 20407 / SU1 Publication.

    Entry informationi

    Entry namei4HBT_ARTSP
    AccessioniPrimary (citable) accession number: Q04416
    Secondary accession number(s): Q2A653, Q7BUB8, Q9AJQ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 2, 2010
    Last sequence update: November 1, 1996
    Last modified: March 16, 2016
    This is version 56 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, 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.