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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

Pathwayi

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

  1. 4-chlorobenzoyl-CoA dehalogenase activity Source: UniProtKB-EC
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 lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

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: October 1, 2014
This is version 49 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.