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Protein

4-chlorobenzoyl coenzyme A dehalogenase

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

Dehalogenates 4-chlorobenzoyl-CoA, 4-iodobenzoyl-CoA and 4-bromobenzoyl-CoA, but not 4-fluorobenzoyl-CoA. Inactive towards crotonyl-CoA, alpha-methylcrotonyl-CoA and beta-methylcrotonyl-CoA.2 Publications

Catalytic activityi

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

Enzyme regulationi

Inactivated by 1 mM Ag+ and by 5 mM Cu2+. Partially inhibited by 5 mM Zn2+, Mn2+, Co2+, Fe2+ and Ni2+. Unaffected by 10 mM Na+, K+ and Li+ and by 0.5 mM Mg2+, Mn2+, Fe2+, Ca2+, Co2+ and Zn2+. Inhibited by the sulfhydryl blocking agent 5,5'-dithio-bis-(2-nitrobenzoate), SDS and N-bromosuccinimide. Unaffected by sodium azide and EDTA. Inactivated following treatment with diethyl pyrocarbonate; this inactivation is reversible by treatment with hydroxylamine.3 Publications

Kineticsi

  1. KM=3.7 µM for 4-chlorobenzoyl-CoA8 Publications
  2. KM=4.2 µM for 4-bromobenzoyl-CoA8 Publications
  3. KM=6.5 µM for 4-iodobenzoyl-CoA8 Publications
  4. KM=10.4 µM for 2,4-dichlorobenzoyl-CoA8 Publications
  5. KM=42 µM for 3,4-dichlorobenzoyl-CoA8 Publications
  6. KM=30 µM for 4-chloro-2-nitrobenzoyl-CoA8 Publications
  7. KM=5.5 µM for 4-chloro-3-nitrobenzoyl-CoA8 Publications
  1. Vmax=2.2 µmol/min/mg enzyme with 4-chlorobenzoyl-CoA as substrate8 Publications

pH dependencei

Optimum pH is 10.0. Half maximum activity remains at pH 9.0 and 11.5. Stable from pH 6.5 to 11.0, activity is lost following 10 minutes incubation at pH 4.5 or 12.0.8 Publications

Temperature dependencei

Optimum temperature is 60 degrees Celsius. Retains 60% of maximum activity at 30 degrees Celsius and 65 degrees Celsius. After 15 minutes preincubation at 60 degrees Celsius 70% of the initial activity remains, 15 minutes preincubation at 65 degrees Celsius results in a total loss of activity.8 Publications

Pathwayi: 4-chlorobenzoate degradation

This protein is involved in step 2 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)DescriptionActionsGraphical viewLength
Binding sitei24Substrate1 Publication1
Active sitei90Proton acceptor2 Publications1
Binding sitei114Substrate; via amide nitrogen1
Active sitei145Nucleophile2 Publications1
Binding sitei257Substrate; shared with oligomeric partner1

GO - Molecular functioni

  • 4-chlorobenzoyl-CoA dehalogenase activity Source: UniProtKB

GO - Biological processi

  • coenzyme A metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14753.
BRENDAi3.8.1.7. 5085.
SABIO-RKA5JTM5.
UniPathwayiUPA01011; UER01021.

Names & Taxonomyi

Protein namesi
Recommended name:
4-chlorobenzoyl coenzyme A dehalogenase1 Publication (EC:3.8.1.7)
Short name:
4-CBA-CoA dehalogenaseImported
Short name:
4-CBCoA dehalogenaseBy similarity
Short name:
4-chlorobenzoyl-CoA dehalogenase2 Publications
OrganismiPseudomonas sp. (strain CBS-3)
Taxonomic identifieri72586 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi24R → K or L: Does not strongly affect catalytic activity, but reduces substrate CoA binding. 1 Publication1
Mutagenesisi34E → T: Forms inclusion bodies. 1 Publication1
Mutagenesisi43E → A: No effect on catalytic activity. 1 Publication1
Mutagenesisi45D → A: No effect on catalytic activity. 1 Publication1
Mutagenesisi46D → A: No effect on catalytic activity. 1 Publication1
Mutagenesisi63G → A, I or P: Yields insoluble protein. 1 Publication1
Mutagenesisi64F → A: 30-fold reduction in catalytic activity, substrate benzoyl group binding is unaffected. 3 Publications1
Mutagenesisi64F → L: Retains catalytic activity, but substrate benzoyl group binding is decreased. 3 Publications1
Mutagenesisi64F → P: Severely reduces catalytic activity. Arylated intermediate does not accumulate. 3 Publications1
Mutagenesisi65Y → D: Catalytic activity is almost as efficient as wild type. 1 Publication1
Mutagenesisi67R → K: Reduces substrate CoA binding. 1 Publication1
Mutagenesisi67R → L: Forms inclusion bodies. 1 Publication1
Mutagenesisi68E → T: No effect on catalytic activity. 1 Publication1
Mutagenesisi81H → Q: Loss of catalytic activity, substrate benzoyl group binding is not affected. 2 Publications1
Mutagenesisi82F → L: Retains catalytic activity, but substrate benzoyl group binding is decreased. 1 Publication1
Mutagenesisi89W → F: Retains catalytic activity, but substrate benzoyl group binding is decreased. 1 Publication1
Mutagenesisi89W → Y: Reduced activity and substrate benzoyl group binding. 1 Publication1
Mutagenesisi90H → Q: Complete loss of catalytic activity (PubMed:8718880 and PubMed:9063883). Significantly reduced activity (PubMed:11695894). Substrate binding is not significantly affected. Reduced arylated intermediate formation. 3 Publications1
Mutagenesisi94H → Q: No effect on catalytic activity. 1 Publication1
Mutagenesisi112A → G: Yields insoluble protein. 1 Publication1
Mutagenesisi112A → S: Protein precipitates upon purification. 1 Publication1
Mutagenesisi112A → V: Catalytic activity is almost as efficient as wild type. 1 Publication1
Mutagenesisi113G → A: Strongly reduced catalytic activity and substrate benzoyl group binding. Arylated intermediate does not accumulate. 2 Publications1
Mutagenesisi113G → N or S: Strongly reduced catalytic activity. Arylated intermediate does not accumulate. 2 Publications1
Mutagenesisi113G → V: Protein precipitates upon purification. 2 Publications1
Mutagenesisi114G → A: Strongly reduced catalytic activity and substrate benzoyl group binding. 2 Publications1
Mutagenesisi114G → P: Unstable. 2 Publications1
Mutagenesisi115G → L, N, S or V: Yields insoluble protein. 1 Publication1
Mutagenesisi123D → T: No effect on catalytic activity. 1 Publication1
Mutagenesisi129D → T: No effect on catalytic activity. 1 Publication1
Mutagenesisi137W → F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883). 2 Publications1
Mutagenesisi145D → A: Complete loss of catalytic activity, but not substrate binding. 1 Publication1
Mutagenesisi163E → T: No effect on catalytic activity. 1 Publication1
Mutagenesisi175E → D: No effect on catalytic activity. 1 Publication1
Mutagenesisi179W → F: No effect on catalytic activity. 1 Publication1
Mutagenesisi208H → Q: No effect on catalytic activity. 1 Publication1
Mutagenesisi216R → E, K or L: Yields insoluble protein. 1 Publication1
Mutagenesisi232E → A, N, Q or R: Yields insoluble protein. 1 Publication1
Mutagenesisi232E → D: Reduced catalytic activity, increased substrate binding. 1 Publication1
Mutagenesisi257R → K: Retains catalytic activity and substrate CoA binding. 1 Publication1
Mutagenesisi257R → L: Significantly reduces catalytic activity and substrate CoA binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004011471 – 2694-chlorobenzoyl coenzyme A dehalogenaseAdd BLAST269

Expressioni

Inductioni

By 4-chlorobenzoyl-CoA, 4-iodobenzoyl-CoA or 4-bromobenzoyl-CoA.1 Publication

Interactioni

Subunit structurei

Homotetramer (PubMed:1610806). Homotetramer, homooctamer and larger multimers (PubMed:7579994). Homotrimer (PubMed:8679561).4 Publications

Structurei

Secondary structure

1269
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 10Combined sources8
Beta strandi13 – 18Combined sources6
Helixi21 – 23Combined sources3
Helixi29 – 44Combined sources16
Beta strandi50 – 56Combined sources7
Beta strandi59 – 61Combined sources3
Helixi66 – 68Combined sources3
Beta strandi71 – 73Combined sources3
Helixi74 – 98Combined sources25
Beta strandi99 – 101Combined sources3
Beta strandi103 – 107Combined sources5
Beta strandi109 – 112Combined sources4
Helixi114 – 121Combined sources8
Beta strandi122 – 128Combined sources7
Beta strandi132 – 134Combined sources3
Helixi137 – 140Combined sources4
Helixi148 – 167Combined sources20
Helixi173 – 178Combined sources6
Beta strandi183 – 186Combined sources4
Helixi188 – 204Combined sources17
Helixi207 – 220Combined sources14
Helixi225 – 241Combined sources17
Helixi245 – 253Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JXZX-ray1.90A/B/C1-269[»]
1NZYX-ray1.80A/B/C1-269[»]
ProteinModelPortaliA5JTM5.
SMRiA5JTM5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA5JTM5.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni62 – 67Substrate binding6

Sequence similaritiesi

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

Phylogenomic databases

KOiK14418.

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. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A5JTM5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYEAIGHRVE DGVAEITIKL PRHRNALSVK AMQEVTDALN RAEEDDSVGA
60 70 80 90 100
VMITGAEDAF CAGFYLREIP LDKGVAGVRD HFRIGALWWH QMIHKIIRVK
110 120 130 140 150
RPVLAAINGV AAGGGLGISL ASDMAICADS AKFVCAWHTI GIGNDTATSY
160 170 180 190 200
SLARIVGMRR AMELMLTNRT LYPEEAKDWG LVSRVYPKDD FREVAWKVAR
210 220 230 240 250
ELAAAPTHLQ VMAKERFHAG WMQPVEECTE FEIQNVIASV THPHFMPCLT
260
EFLDGHRADR PQVELPAGV
Length:269
Mass (Da):29,802
Last modified:June 26, 2007 - v1
Checksum:iEC165E9063C70B07
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF569604 Genomic DNA. Translation: ABQ44578.1.

Genome annotation databases

KEGGiag:ABQ44578.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF569604 Genomic DNA. Translation: ABQ44578.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JXZX-ray1.90A/B/C1-269[»]
1NZYX-ray1.80A/B/C1-269[»]
ProteinModelPortaliA5JTM5.
SMRiA5JTM5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:ABQ44578.

Phylogenomic databases

KOiK14418.

Enzyme and pathway databases

UniPathwayiUPA01011; UER01021.
BioCyciMetaCyc:MONOMER-14753.
BRENDAi3.8.1.7. 5085.
SABIO-RKA5JTM5.

Miscellaneous databases

EvolutionaryTraceiA5JTM5.

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. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCBADH_PSEUC
AccessioniPrimary (citable) accession number: A5JTM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: June 26, 2007
Last modified: November 2, 2016
This is version 44 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, Direct protein sequencing

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.