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O85078 (CBAD1_ARTSP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-chlorobenzoyl coenzyme A dehalogenase-1

Short name=4-CBA-CoA dehalogenase-1
Short name=4-CBCoA dehalogenase-1
Short name=4-chlorobenzoyl-CoA dehalogenase-1
EC=3.8.1.7
Gene names
Name:fcbB1
OrganismArthrobacter sp.
Taxonomic identifier1667 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length276 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2

Catalytic activity

4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl CoA + chloride. Ref.2 Ref.3

Pathway

Xenobiotic degradation; 4-chlorobenzoate degradation; 4-hydroxybenzoate from 4-chlorobenzoate: step 2/3. UniProtKB A5JTM5

Subunit structure

Homotetramer. Ref.2 Ref.3

Sequence similarities

Belongs to the enoyl-CoA hydratase/isomerase family.

Biophysicochemical properties

Kinetic parameters:

KM=14 µM for 4-iodobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2) Ref.2 Ref.3 Ref.4

KM=36 µM for 4-bromobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)

KM=34 µM for 4-chlorobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2) Ref.2

KM=75 µM for 4-fluorobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)

KM=9 µM for 4-chlorobenzoyl-CoA (at 30 degrees Celsius, in 50 mM phosphate buffer, pH 7.5) Ref.3

pH dependence:

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. Ref.2 Ref.3 Ref.4

Temperature dependence:

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. Ref.3 Ref.4

Ontologies

Keywords
   Molecular functionHydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular_function4-chlorobenzoyl-CoA dehalogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.3
Chain2 – 2762754-chlorobenzoyl coenzyme A dehalogenase-1 Ref.2 Ref.3
PRO_0000401145

Regions

Region66 – 716Substrate binding By similarity

Sites

Active site931Proton acceptor By similarity UniProtKB A5JTM5
Active site1481Nucleophile By similarity UniProtKB A5JTM5
Binding site1171Substrate; via amide nitrogen By similarity
Binding site2611Substrate; shared with oligomeric partner By similarity UniProtKB A5JTM5

Sequences

Sequence LengthMass (Da)Tools
O85078 [UniParc].

Last modified October 1, 2000. Version 2.
Checksum: E59F5CF36E8FD305

FASTA27629,899
        10         20         30         40         50         60 
MSSNSDHHIS VEHTDGVATI RFTRPSKHNA ASGQLLLETL EALYRLESDD SVGAIVLTGE 

        70         80         90        100        110        120 
GAVFSAGFDL EEVPMGPASE IQSHFRLKAL YYHAVIHMLA RIEKPTLAAI NGPAVGGGLG 

       130        140        150        160        170        180 
MSLACDLAVC TDRATFLPAW MSIGIANDAS SSFYLPRIVG YRRAMEWLLT NRTLGADEAY 

       190        200        210        220        230        240 
EWGVVNRVFS EADFQSRVGE IARQLAAAPT HLQGLVKNRI QEGSSETLES CTEHEVQNVI 

       250        260        270 
ASVGHPHFAE RLAMFRSKEM RSSALAVDLD AVCGGR 

« Hide

References

[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 / TM1.
[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-CB1.
[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 / TM1.
[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 / TM1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF042490 Genomic DNA. Translation: AAF76241.1.

3D structure databases

ProteinModelPortalO85078.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA01011; UER01021.

Family and domain databases

Gene3D1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamPF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF52096. SSF52096. 1 hit.
PROSITEPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCBAD1_ARTSP
AccessionPrimary (citable) accession number: O85078
Secondary accession number(s): Q04415
Entry history
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 48 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways