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CBAD1_ARTSP
ID   CBAD1_ARTSP             Reviewed;         276 AA.
AC   O85078; Q04415;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 2.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=4-chlorobenzoyl coenzyme A dehalogenase-1;
DE            Short=4-CBA-CoA dehalogenase-1;
DE            Short=4-CBCoA dehalogenase-1 {ECO:0000303|PubMed:15068371};
DE            Short=4-chlorobenzoyl-CoA dehalogenase-1;
DE            EC=3.8.1.7;
GN   Name=fcbB1 {ECO:0000312|EMBL:AAF76241.1};
OS   Arthrobacter sp.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=1667;
RN   [1] {ECO:0000312|EMBL:AAF76241.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCIB 12013 / TM1 {ECO:0000312|EMBL:AAF76241.1};
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; AAF76241.1; -; Genomic_DNA.
DR   AlphaFoldDB; O85078; -.
DR   SMR; O85078; -.
DR   UniPathway; UPA01011; UER01021.
DR   GO; GO:0018787; F:4-chlorobenzoyl-CoA dehalogenase activity; IEA:UniProtKB-EC.
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-1"
FT                   /evidence="ECO:0000269|PubMed:15068371,
FT                   ECO:0000269|PubMed:7918379"
FT                   /id="PRO_0000401145"
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;  29899 MW;  E59F5CF36E8FD305 CRC64;
     MSSNSDHHIS VEHTDGVATI RFTRPSKHNA ASGQLLLETL 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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