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 27-MAR-2024, entry version 69. 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; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae; OC 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 CC re-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CDD; cd06558; crotonase-like; 1. DR Gene3D; 1.10.12.10; Lyase 2-enoyl-coa Hydratase, Chain A, domain 2; 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 PANTHER; PTHR43684; -; 1. DR PANTHER; PTHR43684:SF4; ENOYL-COA HYDRATASE_ISOMERASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G01890); 1. DR Pfam; PF00378; ECH_1; 1. DR SUPFAM; SSF52096; ClpP/crotonase; 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 //