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4-chlorobenzoyl coenzyme A dehalogenase-2 (4-CBA-CoA dehalogenase-2) (4-CBCoA dehalogenase-2) (4-chlorobenzoyl-CoA dehalogenase-2) (EC 3.8.1.7)

 CBAD2_ARTSP             Reviewed;         276 AA.
Q9LCU3;
30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
10-MAY-2017, entry version 45.
RecName: Full=4-chlorobenzoyl coenzyme A dehalogenase-2;
Short=4-CBA-CoA dehalogenase-2;
Short=4-CBCoA dehalogenase-2 {ECO:0000303|PubMed:15068371};
Short=4-chlorobenzoyl-CoA dehalogenase-2;
EC=3.8.1.7;
Name=fcbB2 {ECO:0000312|EMBL:AAF78820.1};
Arthrobacter sp.
Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
NCBI_TaxID=1667;
[1] {ECO:0000312|EMBL:AAF78820.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=NCIB 12013 / TM1 {ECO:0000312|EMBL:AAF78820.1};
PubMed=11371537; DOI=10.1128/JB.183.12.3729-3736.2001;
Gartemann K.H., Eichenlaub R.;
"Isolation and characterization of IS1409, an insertion element of 4-
chlorobenzoate-degrading Arthrobacter sp. strain TM1, and development
of a system for transposon mutagenesis.";
J. Bacteriol. 183:3729-3736(2001).
[2] {ECO:0000305}
PROTEIN SEQUENCE OF 2-25, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
STRAIN=4-CB1 {ECO:0000269|PubMed:7918379};
PubMed=7918379; DOI=10.1021/bi00204a028;
Crooks G.P., Copley S.D.;
"Purification and characterization of 4-chlorobenzoyl CoA dehalogenase
from Arthrobacter sp. strain 4-CB1.";
Biochemistry 33:11645-11649(1994).
[3] {ECO:0000305}
PROTEIN SEQUENCE OF 2-21, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, AND SUBUNIT.
STRAIN=NCIB 12013 / TM1 {ECO:0000269|PubMed:15068371};
PubMed=15068371; DOI=10.1023/B:BIOD.0000015614.94615.34;
Zhou L., Marks T.S., Poh R.P., Smith R.J., Chowdhry B.Z., Smith A.R.;
"The purification and characterisation of 4-chlorobenzoate:CoA ligase
and 4-chlorobenzoyl CoA dehalogenase from Arthrobacter sp. strain TM-
1.";
Biodegradation 15:97-109(2004).
[4] {ECO:0000305}
BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=NCIB 12013 / TM1 {ECO:0000269|PubMed:17431803};
PubMed=17431803; DOI=10.1007/s10532-007-9115-9;
Zhou L., Poh R.P., Marks T.S., Chowdhry B.Z., Smith A.R.;
"Structure and denaturation of 4-chlorobenzoyl coenzyme A dehalogenase
from Arthrobacter sp. strain TM-1.";
Biodegradation 19:65-75(2008).
-!- 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.
{ECO:0000269|PubMed:7918379}.
-!- CATALYTIC ACTIVITY: 4-chlorobenzoyl-CoA + H(2)O = 4-hydroxybenzoyl
CoA + chloride. {ECO:0000269|PubMed:15068371,
ECO:0000269|PubMed:7918379}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=14 uM for 4-iodobenzoyl-CoA (at 30 degrees Celsius, in 20 mM
phosphate buffer, pH 7.2) {ECO:0000269|PubMed:15068371,
ECO:0000269|PubMed:17431803, ECO:0000269|PubMed:7918379};
KM=36 uM for 4-bromobenzoyl-CoA (at 30 degrees Celsius, in 20 mM
phosphate buffer, pH 7.2) {ECO:0000269|PubMed:15068371,
ECO:0000269|PubMed:17431803, ECO:0000269|PubMed:7918379};
KM=34 uM for 4-chlorobenzoyl-CoA (at 30 degrees Celsius, in 20
mM phosphate buffer, pH 7.2) {ECO:0000269|PubMed:15068371,
ECO:0000269|PubMed:17431803, ECO:0000269|PubMed:7918379};
KM=75 uM for 4-fluorobenzoyl-CoA (at 30 degrees Celsius, in 20
mM phosphate buffer, pH 7.2) {ECO:0000269|PubMed:15068371,
ECO:0000269|PubMed:17431803, ECO:0000269|PubMed:7918379};
KM=9 uM for 4-chlorobenzoyl-CoA (at 30 degrees Celsius, in 50 mM
phosphate buffer, pH 7.5) {ECO:0000269|PubMed:15068371,
ECO:0000269|PubMed:17431803, ECO:0000269|PubMed:7918379};
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. {ECO:0000269|PubMed:15068371,
ECO:0000269|PubMed:17431803, ECO:0000269|PubMed:7918379};
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. {ECO:0000269|PubMed:15068371,
ECO:0000269|PubMed:17431803, ECO:0000269|PubMed:7918379};
-!- PATHWAY: Xenobiotic degradation; 4-chlorobenzoate degradation; 4-
hydroxybenzoate from 4-chlorobenzoate: step 2/3.
{ECO:0000250|UniProtKB:A5JTM5}.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15068371,
ECO:0000269|PubMed:7918379}.
-!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
{ECO:0000255}.
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EMBL; AF042490; AAF78820.1; -; Genomic_DNA.
ProteinModelPortal; Q9LCU3; -.
SMR; Q9LCU3; -.
UniPathway; UPA01011; UER01021.
GO; GO:0018787; F:4-chlorobenzoyl-CoA dehalogenase activity; IDA:UniProtKB.
GO; GO:0015936; P:coenzyme A metabolic process; IDA:UniProtKB.
Gene3D; 1.10.12.10; -; 1.
InterPro; IPR029045; ClpP/crotonase-like_dom.
InterPro; IPR014748; Crontonase_C.
InterPro; IPR001753; Crotonase_core_superfam.
InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
Pfam; PF00378; ECH_1; 1.
SUPFAM; SSF52096; SSF52096; 1.
PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
1: Evidence at protein level;
Direct protein sequencing; Hydrolase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:15068371,
ECO:0000269|PubMed:7918379}.
CHAIN 2 276 4-chlorobenzoyl coenzyme A dehalogenase-
2. {ECO:0000269|PubMed:15068371,
ECO:0000269|PubMed:7918379}.
/FTId=PRO_0000401146.
REGION 66 71 Substrate binding. {ECO:0000250}.
ACT_SITE 93 93 Proton acceptor.
{ECO:0000250|UniProtKB:A5JTM5}.
ACT_SITE 148 148 Nucleophile.
{ECO:0000250|UniProtKB:A5JTM5}.
BINDING 117 117 Substrate; via amide nitrogen.
{ECO:0000250}.
BINDING 261 261 Substrate; shared with oligomeric
partner. {ECO:0000250}.
SEQUENCE 276 AA; 29913 MW; 459F5CF25CC6F795 CRC64;
MSSNSDHHIS VEHTDGVATI RFTRPSKHNA ASAQLLLETL EALYRLESDD SVGAIVLTGE
GAVFSAGFDL EEVPMGPASE IQSHFRLKAL YYHAVIHMLA RIEKPTLAAI NGPAVGGGLG
MSLACDLAVC TDRATFLPAW MSIGIANDAS SSFYLPRIVG YRRAMEWLLT NRTLGADEAY
EWGVVNRVFS EADFQSRVGE IARQLAAAPT HLQGLVKNRI QEGSSETLES CTEHEVQNVI
ASVGHPHFAE RLAMFRSKEM RSSALAVDLD AVCGGR


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