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-chlorobenzoyl coenzyme A dehalogenase-1

Gene

fcbB1

Organism
Arthrobacter sp.
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Dehalogenates 4-chlorobenzoyl-CoA, 4-iodobenzoyl-CoA, 4-bromobenzoyl-CoA and, at a slower rate, 4-fluorobenzoyl-CoA. Does not dehalogenate 2-chlorobenzoyl-CoA or 3-chlorobenzoyl-CoA.1 Publication

Catalytic activityi

4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride.2 Publications

Kineticsi

  1. KM=14 µM for 4-iodobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)3 Publications
  2. KM=36 µM for 4-bromobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)3 Publications
  3. KM=34 µM for 4-chlorobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)3 Publications
  4. KM=75 µM for 4-fluorobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)3 Publications
  5. KM=9 µM for 4-chlorobenzoyl-CoA (at 30 degrees Celsius, in 50 mM phosphate buffer, pH 7.5)3 Publications

    pH dependencei

    Optimum pH is 8.0 in MOPS buffer at 30 degrees Celsius, 7.5 in 0.1 M potassium phosphate buffer at 30 degrees Celsius, and 7.4 in 20 mM potassium phosphate/2 mM DTT buffer at 30 degrees Celsius. Retains full activity in MOPS buffer between pH 6.5 and 10.0. Is irreversibly damaged below pH 6.5 in MOPS buffer, enzyme treated at pH 6.0 in MOPS buffer only regains 40% of its original activity after re-equilibration at pH 7.2. When treated at pH 5.2 or 10.1 in 20 mM potassium phosphate/2 mM DTT buffer activity is lost completely, but is recovered within 17 minutes following readjustment to pH 7.4.3 Publications

    Temperature dependencei

    Optimum temperature is 45 degrees Celsius. Activity is lost after 5 minutes incubation at 60 degrees Celsius, but one-fifth of this activity is restored after cooling to 45 degrees Celsius.3 Publications

    Pathway:i4-chlorobenzoate degradation

    This protein is involved in step 2 of the subpathway that synthesizes 4-hydroxybenzoate from 4-chlorobenzoate.By similarity
    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 sitei93 – 931Proton acceptorBy similarity
    Binding sitei117 – 1171Substrate; via amide nitrogenBy similarity
    Active sitei148 – 1481NucleophileBy similarity
    Binding sitei261 – 2611Substrate; shared with oligomeric partnerBy similarity

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    UniPathwayiUPA01011; UER01021.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-chlorobenzoyl coenzyme A dehalogenase-1 (EC:3.8.1.7)
    Short name:
    4-CBA-CoA dehalogenase-1
    Short name:
    4-CBCoA dehalogenase-11 Publication
    Short name:
    4-chlorobenzoyl-CoA dehalogenase-1
    Gene namesi
    Name:fcbB1Imported
    OrganismiArthrobacter sp.
    Taxonomic identifieri1667 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaeArthrobacter

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 2762754-chlorobenzoyl coenzyme A dehalogenase-12 PublicationsPRO_0000401145Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Structurei

    3D structure databases

    ProteinModelPortaliO85078.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni66 – 716Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the enoyl-CoA hydratase/isomerase family.Sequence Analysis

    Family and domain databases

    Gene3Di1.10.12.10. 1 hit.
    3.90.226.10. 1 hit.
    InterProiIPR029045. ClpP/crotonase-like_dom.
    IPR014748. Crontonase_C.
    IPR001753. Crotonase_core_superfam.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    [Graphical view]
    PfamiPF00378. ECH. 1 hit.
    [Graphical view]
    SUPFAMiSSF52096. SSF52096. 1 hit.
    PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O85078-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSSNSDHHIS VEHTDGVATI RFTRPSKHNA ASGQLLLETL EALYRLESDD
    60 70 80 90 100
    SVGAIVLTGE GAVFSAGFDL EEVPMGPASE IQSHFRLKAL YYHAVIHMLA
    110 120 130 140 150
    RIEKPTLAAI NGPAVGGGLG MSLACDLAVC TDRATFLPAW MSIGIANDAS
    160 170 180 190 200
    SSFYLPRIVG YRRAMEWLLT NRTLGADEAY EWGVVNRVFS EADFQSRVGE
    210 220 230 240 250
    IARQLAAAPT HLQGLVKNRI QEGSSETLES CTEHEVQNVI ASVGHPHFAE
    260 270
    RLAMFRSKEM RSSALAVDLD AVCGGR
    Length:276
    Mass (Da):29,899
    Last modified:October 1, 2000 - v2
    Checksum:iE59F5CF36E8FD305
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF042490 Genomic DNA. Translation: AAF76241.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF042490 Genomic DNA. Translation: AAF76241.1.

    3D structure databases

    ProteinModelPortaliO85078.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA01011; UER01021.

    Family and domain databases

    Gene3Di1.10.12.10. 1 hit.
    3.90.226.10. 1 hit.
    InterProiIPR029045. ClpP/crotonase-like_dom.
    IPR014748. Crontonase_C.
    IPR001753. Crotonase_core_superfam.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    [Graphical view]
    PfamiPF00378. ECH. 1 hit.
    [Graphical view]
    SUPFAMiSSF52096. SSF52096. 1 hit.
    PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "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.
    2. "Purification and characterization of 4-chlorobenzoyl CoA dehalogenase from Arthrobacter sp. strain 4-CB1."
      Crooks G.P., Copley S.D.
      Biochemistry 33:11645-11649(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-25, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Strain: 4-CB11 Publication.
    3. "The purification and characterisation of 4-chlorobenzoate:CoA ligase and 4-chlorobenzoyl CoA dehalogenase from Arthrobacter sp. strain TM-1."
      Zhou L., Marks T.S., Poh R.P., Smith R.J., Chowdhry B.Z., Smith A.R.
      Biodegradation 15:97-109(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Strain: NCIB 12013 / TM11 Publication.
    4. "Structure and denaturation of 4-chlorobenzoyl coenzyme A dehalogenase from Arthrobacter sp. strain TM-1."
      Zhou L., Poh R.P., Marks T.S., Chowdhry B.Z., Smith A.R.
      Biodegradation 19:65-75(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: NCIB 12013 / TM11 Publication.

    Entry informationi

    Entry nameiCBAD1_ARTSP
    AccessioniPrimary (citable) accession number: O85078
    Secondary accession number(s): Q04415
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 30, 2010
    Last sequence update: October 1, 2000
    Last modified: June 24, 2015
    This is version 50 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.