CBAD2_ARTSP
ID CBAD2_ARTSP Reviewed; 276 AA.
AC Q9LCU3;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=4-chlorobenzoyl coenzyme A dehalogenase-2;
DE Short=4-CBA-CoA dehalogenase-2;
DE Short=4-CBCoA dehalogenase-2 {ECO:0000303|PubMed:15068371};
DE Short=4-chlorobenzoyl-CoA dehalogenase-2;
DE EC=3.8.1.7;
GN Name=fcbB2 {ECO:0000312|EMBL:AAF78820.1};
OS Arthrobacter sp.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=1667;
RN [1] {ECO:0000312|EMBL:AAF78820.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCIB 12013 / TM1 {ECO:0000312|EMBL:AAF78820.1};
RX PubMed=11371537; DOI=10.1128/jb.183.12.3729-3736.2001;
RA Gartemann K.H., Eichenlaub R.;
RT "Isolation and characterization of IS1409, an insertion element of 4-
RT chlorobenzoate-degrading Arthrobacter sp. strain TM1, and development of a
RT system for transposon mutagenesis.";
RL J. Bacteriol. 183:3729-3736(2001).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-25, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=4-CB1 {ECO:0000269|PubMed:7918379};
RX PubMed=7918379; DOI=10.1021/bi00204a028;
RA Crooks G.P., Copley S.D.;
RT "Purification and characterization of 4-chlorobenzoyl CoA dehalogenase from
RT Arthrobacter sp. strain 4-CB1.";
RL Biochemistry 33:11645-11649(1994).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-21, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=NCIB 12013 / TM1 {ECO:0000269|PubMed:15068371};
RX PubMed=15068371; DOI=10.1023/b:biod.0000015614.94615.34;
RA Zhou L., Marks T.S., Poh R.P., Smith R.J., Chowdhry B.Z., Smith A.R.;
RT "The purification and characterisation of 4-chlorobenzoate:CoA ligase and
RT 4-chlorobenzoyl CoA dehalogenase from Arthrobacter sp. strain TM-1.";
RL Biodegradation 15:97-109(2004).
RN [4] {ECO:0000305}
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=NCIB 12013 / TM1 {ECO:0000269|PubMed:17431803};
RX PubMed=17431803; DOI=10.1007/s10532-007-9115-9;
RA Zhou L., Poh R.P., Marks T.S., Chowdhry B.Z., Smith A.R.;
RT "Structure and denaturation of 4-chlorobenzoyl coenzyme A dehalogenase from
RT Arthrobacter sp. strain TM-1.";
RL Biodegradation 19:65-75(2008).
CC -!- FUNCTION: Dehalogenates 4-chlorobenzoyl-CoA, 4-iodobenzoyl-CoA, 4-
CC bromobenzoyl-CoA and, at a slower rate, 4-fluorobenzoyl-CoA. Does not
CC dehalogenate 2-chlorobenzoyl-CoA or 3-chlorobenzoyl-CoA.
CC {ECO:0000269|PubMed:7918379}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl-CoA + chloride +
CC H(+); Xref=Rhea:RHEA:14853, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:57354, ChEBI:CHEBI:57356; EC=3.8.1.7;
CC Evidence={ECO:0000269|PubMed:15068371, ECO:0000269|PubMed:7918379};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 uM for 4-iodobenzoyl-CoA (at 30 degrees Celsius, in 20 mM
CC phosphate buffer, pH 7.2) {ECO:0000269|PubMed:15068371,
CC ECO:0000269|PubMed:17431803, ECO:0000269|PubMed:7918379};
CC KM=36 uM for 4-bromobenzoyl-CoA (at 30 degrees Celsius, in 20 mM
CC phosphate buffer, pH 7.2) {ECO:0000269|PubMed:15068371,
CC ECO:0000269|PubMed:17431803, ECO:0000269|PubMed:7918379};
CC KM=34 uM for 4-chlorobenzoyl-CoA (at 30 degrees Celsius, in 20 mM
CC phosphate buffer, pH 7.2) {ECO:0000269|PubMed:15068371,
CC ECO:0000269|PubMed:17431803, ECO:0000269|PubMed:7918379};
CC KM=75 uM for 4-fluorobenzoyl-CoA (at 30 degrees Celsius, in 20 mM
CC phosphate buffer, pH 7.2) {ECO:0000269|PubMed:15068371,
CC ECO:0000269|PubMed:17431803, ECO:0000269|PubMed:7918379};
CC KM=9 uM for 4-chlorobenzoyl-CoA (at 30 degrees Celsius, in 50 mM
CC phosphate buffer, pH 7.5) {ECO:0000269|PubMed:15068371,
CC ECO:0000269|PubMed:17431803, ECO:0000269|PubMed:7918379};
CC pH dependence:
CC Optimum pH is 8.0 in MOPS buffer at 30 degrees Celsius, 7.5 in 0.1 M
CC potassium phosphate buffer at 30 degrees Celsius, and 7.4 in 20 mM
CC potassium phosphate/2 mM DTT buffer at 30 degrees Celsius. Retains
CC full activity in MOPS buffer between pH 6.5 and 10.0. Is irreversibly
CC damaged below pH 6.5 in MOPS buffer, enzyme treated at pH 6.0 in MOPS
CC buffer only regains 40% of its original activity after re-
CC equilibration at pH 7.2. When treated at pH 5.2 or 10.1 in 20 mM
CC potassium phosphate/2 mM DTT buffer activity is lost completely, but
CC is recovered within 17 minutes following readjustment to pH 7.4.
CC {ECO:0000269|PubMed:15068371, ECO:0000269|PubMed:17431803,
CC ECO:0000269|PubMed:7918379};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius. Activity is lost after 5
CC minutes incubation at 60 degrees Celsius, but one-fifth of this
CC activity is restored after cooling to 45 degrees Celsius.
CC {ECO:0000269|PubMed:15068371, ECO:0000269|PubMed:17431803,
CC ECO:0000269|PubMed:7918379};
CC -!- PATHWAY: Xenobiotic degradation; 4-chlorobenzoate degradation; 4-
CC hydroxybenzoate from 4-chlorobenzoate: step 2/3.
CC {ECO:0000250|UniProtKB:A5JTM5}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15068371,
CC ECO:0000269|PubMed:7918379}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000255}.
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DR EMBL; AF042490; AAF78820.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9LCU3; -.
DR SMR; Q9LCU3; -.
DR UniPathway; UPA01011; UER01021.
DR GO; GO:0018787; F:4-chlorobenzoyl-CoA dehalogenase activity; IDA:UniProtKB.
DR GO; GO:0015936; P:coenzyme A metabolic process; IDA:UniProtKB.
DR Gene3D; 1.10.12.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15068371,
FT ECO:0000269|PubMed:7918379"
FT CHAIN 2..276
FT /note="4-chlorobenzoyl coenzyme A dehalogenase-2"
FT /evidence="ECO:0000269|PubMed:15068371,
FT ECO:0000269|PubMed:7918379"
FT /id="PRO_0000401146"
FT ACT_SITE 93
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A5JTM5"
FT ACT_SITE 148
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:A5JTM5"
FT BINDING 66..71
FT /ligand="substrate"
FT /ligand_note="ligand shared between two oligomeric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="substrate"
FT /ligand_note="ligand shared between two oligomeric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="substrate"
FT /ligand_note="ligand shared between two oligomeric
FT partners"
FT /evidence="ECO:0000250"
SQ 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
