CBADH_PSEUC
ID CBADH_PSEUC Reviewed; 269 AA.
AC A5JTM5;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=4-chlorobenzoyl coenzyme A dehalogenase {ECO:0000303|PubMed:7579994};
DE Short=4-CBA-CoA dehalogenase {ECO:0000312|EMBL:ABQ44578.1};
DE Short=4-CBCoA dehalogenase {ECO:0000250|UniProtKB:O85078};
DE Short=4-chlorobenzoyl-CoA dehalogenase {ECO:0000303|PubMed:1610806, ECO:0000303|PubMed:7579994};
DE EC=3.8.1.7;
OS Pseudomonas sp. (strain CBS-3).
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=72586;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1351742; DOI=10.1021/bi00139a024;
RA Babbitt P.C., Kenyon G.L., Martin B.M., Charest H., Slyvestre M.,
RA Scholten J.D., Chang K.H., Liang P.H., Dunaway-Mariano D.;
RT "Ancestry of the 4-chlorobenzoate dehalogenase: analysis of amino acid
RT sequence identities among families of acyl:adenyl ligases, enoyl-CoA
RT hydratases/isomerases, and acyl-CoA thioesterases.";
RL Biochemistry 31:5594-5604(1992).
RN [2] {ECO:0000312|EMBL:ABQ44578.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CBS-3;
RA Zhang W., Dunaway-Mariano D.;
RT "The nucleotide sequence upstream and downstream of 4-CBA-CoA ORFs in 9.5
RT kb Pseudomonas sp. strain CBS 3 chromosomal DNA.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-40, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INDUCTION.
RC STRAIN=CBS-3;
RX PubMed=7579994; DOI=10.1007/bf00700458;
RA Loffler F., Lingens F., Muller R.;
RT "Dehalogenation of 4-chlorobenzoate. Characterisation of 4-chlorobenzoyl-
RT coenzyme A dehalogenase from Pseudomonas sp. CBS3.";
RL Biodegradation 6:203-212(1995).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, AND SUBUNIT.
RC STRAIN=CBS-3;
RX PubMed=1610806; DOI=10.1021/bi00139a025;
RA Chang K.H., Liang P.H., Beck W., Scholten J.D., Dunaway-Mariano D.;
RT "Isolation and characterization of the three polypeptide components of 4-
RT chlorobenzoate dehalogenase from Pseudomonas sp. strain CBS-3.";
RL Biochemistry 31:5605-5610(1992).
RN [5] {ECO:0000305}
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8218302; DOI=10.1021/bi00096a038;
RA Liang P.H., Yang G., Dunaway-Mariano D.;
RT "Specificity of 4-chlorobenzoyl coenzyme A dehalogenase catalyzed
RT dehalogenation of halogenated aromatics.";
RL Biochemistry 32:12245-12250(1993).
RN [6] {ECO:0000305}
RP ACTIVITY REGULATION, ACTIVE SITES, AND MUTAGENESIS OF GLU-34; GLU-43;
RP ASP-45; ASP-46; GLU-68; HIS-90; HIS-94; ASP-123; ASP-129; TRP-137; GLU-163;
RP GLU-175; TRP-179 AND HIS-208.
RX PubMed=8718880; DOI=10.1021/bi9609533;
RA Yang G., Liu R.Q., Taylor K.L., Xiang H., Price J., Dunaway-Mariano D.;
RT "Identification of active site residues essential to 4-chlorobenzoyl-
RT coenzyme A dehalogenase catalysis by chemical modification and site
RT directed mutagenesis.";
RL Biochemistry 35:10879-10885(1996).
RN [7] {ECO:0000305}
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF PHE-64; HIS-81; PHE-82;
RP TRP-89; HIS-90; GLY-114; TRP-137 AND ASP-145.
RX PubMed=9063883; DOI=10.1021/bi962765i;
RA Taylor K.L., Xiang H., Liu R.Q., Yang G., Dunaway-Mariano D.;
RT "Investigation of substrate activation by 4-chlorobenzoyl-coenzyme A
RT dehalogenase.";
RL Biochemistry 36:1349-1361(1997).
RN [8] {ECO:0000305}
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-24; PHE-64; ARG-67;
RP GLY-113; GLY-114 AND ARG-257.
RX PubMed=11747444; DOI=10.1021/bi011536f;
RA Luo L., Taylor K.L., Xiang H., Wei Y., Zhang W., Dunaway-Mariano D.;
RT "Role of active site binding interactions in 4-chlorobenzoyl-coenzyme A
RT dehalogenase catalysis.";
RL Biochemistry 40:15684-15692(2001).
RN [9] {ECO:0000305}
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLY-63; PHE-64; TYR-65;
RP ALA-112; GLY-113 AND GLY-115.
RX PubMed=12899635; DOI=10.1021/bi0347656;
RA Dong J., Lu X., Wei Y., Luo L., Dunaway-Mariano D., Carey P.R.;
RT "The strength of dehalogenase-substrate hydrogen bonding correlates with
RT the rate of Meisenheimer intermediate formation.";
RL Biochemistry 42:9482-9490(2003).
RN [10] {ECO:0000305}
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-216 AND GLU-232.
RX PubMed=16388585; DOI=10.1021/bi051477w;
RA Wu J., Xu D., Lu X., Wang C., Guo H., Dunaway-Mariano D.;
RT "Contributions of long-range electrostatic interactions to 4-chlorobenzoyl-
RT CoA dehalogenase catalysis: a combined theoretical and experimental
RT study.";
RL Biochemistry 45:102-112(2006).
RN [11] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF MUTANT GLN-90 IN COMPLEX WITH
RP 4-HYDROXYBENZOYL COENZYME A, SUBUNIT, ACTIVE SITE, AND SUBSTRATE-BINDING
RP SITES.
RC STRAIN=CBS-3;
RX PubMed=8679561; DOI=10.1021/bi960768p;
RA Benning M.M., Taylor K.L., Liu R.-Q., Yang G., Xiang H., Wesenberg G.,
RA Dunaway-Mariano D., Holden H.M.;
RT "Structure of 4-chlorobenzoyl coenzyme A dehalogenase determined to 1.8 A
RT resolution: an enzyme catalyst generated via adaptive mutation.";
RL Biochemistry 35:8103-8109(1996).
RN [12] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANT GLN-90 IN COMPLEX WITH
RP 4-HYDROXYBENZOYL COENZYME A, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS
RP OF HIS-90.
RX PubMed=11695894; DOI=10.1021/bi0114426;
RA Zhang W., Wei Y., Luo L., Taylor K.L., Yang G., Dunaway-Mariano D.,
RA Benning M.M., Holden H.M.;
RT "Histidine 90 function in 4-chlorobenzoyl-coenzyme a dehalogenase
RT catalysis.";
RL Biochemistry 40:13474-13482(2001).
CC -!- FUNCTION: Dehalogenates 4-chlorobenzoyl-CoA, 4-iodobenzoyl-CoA and 4-
CC bromobenzoyl-CoA, but not 4-fluorobenzoyl-CoA. Inactive towards
CC crotonyl-CoA, alpha-methylcrotonyl-CoA and beta-methylcrotonyl-CoA.
CC {ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:7579994}.
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:1610806, ECO:0000269|PubMed:7579994};
CC -!- ACTIVITY REGULATION: Inactivated by 1 mM Ag(+) and by 5 mM Cu(2+).
CC Partially inhibited by 5 mM Zn(2+), Mn(2+), Co(2+), Fe(2+) and Ni(2+).
CC Unaffected by 10 mM Na(+), K(+) and Li(+) and by 0.5 mM Mg(2+), Mn(2+),
CC Fe(2+), Ca(2+), Co(2+) and Zn(2+). Inhibited by the sulfhydryl blocking
CC agent 5,5'-dithio-bis-(2-nitrobenzoate), SDS and N-bromosuccinimide.
CC Unaffected by sodium azide and EDTA. Inactivated following treatment
CC with diethyl pyrocarbonate; this inactivation is reversible by
CC treatment with hydroxylamine. {ECO:0000269|PubMed:1610806,
CC ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8718880}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.7 uM for 4-chlorobenzoyl-CoA {ECO:0000269|PubMed:11695894,
CC ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585,
CC ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302,
CC ECO:0000269|PubMed:9063883};
CC KM=4.2 uM for 4-bromobenzoyl-CoA {ECO:0000269|PubMed:11695894,
CC ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585,
CC ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302,
CC ECO:0000269|PubMed:9063883};
CC KM=6.5 uM for 4-iodobenzoyl-CoA {ECO:0000269|PubMed:11695894,
CC ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585,
CC ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302,
CC ECO:0000269|PubMed:9063883};
CC KM=10.4 uM for 2,4-dichlorobenzoyl-CoA {ECO:0000269|PubMed:11695894,
CC ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585,
CC ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302,
CC ECO:0000269|PubMed:9063883};
CC KM=42 uM for 3,4-dichlorobenzoyl-CoA {ECO:0000269|PubMed:11695894,
CC ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585,
CC ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302,
CC ECO:0000269|PubMed:9063883};
CC KM=30 uM for 4-chloro-2-nitrobenzoyl-CoA
CC {ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444,
CC ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806,
CC ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994,
CC ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883};
CC KM=5.5 uM for 4-chloro-3-nitrobenzoyl-CoA
CC {ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444,
CC ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806,
CC ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994,
CC ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883};
CC Vmax=2.2 umol/min/mg enzyme with 4-chlorobenzoyl-CoA as substrate
CC {ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:11747444,
CC ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:1610806,
CC ECO:0000269|PubMed:16388585, ECO:0000269|PubMed:7579994,
CC ECO:0000269|PubMed:8218302, ECO:0000269|PubMed:9063883};
CC pH dependence:
CC Optimum pH is 10.0. Half maximum activity remains at pH 9.0 and 11.5.
CC Stable from pH 6.5 to 11.0, activity is lost following 10 minutes
CC incubation at pH 4.5 or 12.0. {ECO:0000269|PubMed:11695894,
CC ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585,
CC ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302,
CC ECO:0000269|PubMed:9063883};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. Retains 60% of maximum
CC activity at 30 degrees Celsius and 65 degrees Celsius. After 15
CC minutes preincubation at 60 degrees Celsius 70% of the initial
CC activity remains, 15 minutes preincubation at 65 degrees Celsius
CC results in a total loss of activity. {ECO:0000269|PubMed:11695894,
CC ECO:0000269|PubMed:11747444, ECO:0000269|PubMed:12899635,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16388585,
CC ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8218302,
CC ECO:0000269|PubMed:9063883};
CC -!- PATHWAY: Xenobiotic degradation; 4-chlorobenzoate degradation; 4-
CC hydroxybenzoate from 4-chlorobenzoate: step 2/3.
CC {ECO:0000269|PubMed:1610806}.
CC -!- SUBUNIT: Homotetramer (PubMed:1610806). Homotetramer, homooctamer and
CC larger multimers (PubMed:7579994). Homotrimer (PubMed:8679561).
CC {ECO:0000269|PubMed:11695894, ECO:0000269|PubMed:1610806,
CC ECO:0000269|PubMed:7579994, ECO:0000269|PubMed:8679561}.
CC -!- INDUCTION: By 4-chlorobenzoyl-CoA, 4-iodobenzoyl-CoA or 4-bromobenzoyl-
CC CoA. {ECO:0000269|PubMed:7579994}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000255}.
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DR EMBL; EF569604; ABQ44578.1; -; Genomic_DNA.
DR PDB; 1JXZ; X-ray; 1.90 A; A/B/C=1-269.
DR PDB; 1NZY; X-ray; 1.80 A; A/B/C=1-269.
DR PDBsum; 1JXZ; -.
DR PDBsum; 1NZY; -.
DR AlphaFoldDB; A5JTM5; -.
DR SMR; A5JTM5; -.
DR KEGG; ag:ABQ44578; -.
DR BioCyc; MetaCyc:MON-14753; -.
DR BRENDA; 3.8.1.7; 5085.
DR SABIO-RK; A5JTM5; -.
DR UniPathway; UPA01011; UER01021.
DR EvolutionaryTrace; A5JTM5; -.
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 3D-structure; Direct protein sequencing; Hydrolase.
FT CHAIN 1..269
FT /note="4-chlorobenzoyl coenzyme A dehalogenase"
FT /id="PRO_0000401147"
FT ACT_SITE 90
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:8679561,
FT ECO:0000269|PubMed:8718880"
FT ACT_SITE 145
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:8679561,
FT ECO:0000269|PubMed:8718880"
FT BINDING 24
FT /ligand="substrate"
FT /ligand_note="ligand shared between two oligomeric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:8679561"
FT BINDING 62..67
FT /ligand="substrate"
FT /ligand_note="ligand shared between two oligomeric
FT partners"
FT /note="in other chain"
FT BINDING 114
FT /ligand="substrate"
FT /ligand_note="ligand shared between two oligomeric
FT partners"
FT /note="in other chain"
FT BINDING 257
FT /ligand="substrate"
FT /ligand_note="ligand shared between two oligomeric
FT partners"
FT MUTAGEN 24
FT /note="R->K,L: Does not strongly affect catalytic activity,
FT but reduces substrate CoA binding."
FT /evidence="ECO:0000269|PubMed:11747444"
FT MUTAGEN 34
FT /note="E->T: Forms inclusion bodies."
FT /evidence="ECO:0000269|PubMed:8718880"
FT MUTAGEN 43
FT /note="E->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:8718880"
FT MUTAGEN 45
FT /note="D->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:8718880"
FT MUTAGEN 46
FT /note="D->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:8718880"
FT MUTAGEN 63
FT /note="G->A,I,P: Yields insoluble protein."
FT /evidence="ECO:0000269|PubMed:12899635"
FT MUTAGEN 64
FT /note="F->A: 30-fold reduction in catalytic activity,
FT substrate benzoyl group binding is unaffected."
FT /evidence="ECO:0000269|PubMed:11747444,
FT ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:9063883"
FT MUTAGEN 64
FT /note="F->L: Retains catalytic activity, but substrate
FT benzoyl group binding is decreased."
FT /evidence="ECO:0000269|PubMed:11747444,
FT ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:9063883"
FT MUTAGEN 64
FT /note="F->P: Severely reduces catalytic activity. Arylated
FT intermediate does not accumulate."
FT /evidence="ECO:0000269|PubMed:11747444,
FT ECO:0000269|PubMed:12899635, ECO:0000269|PubMed:9063883"
FT MUTAGEN 65
FT /note="Y->D: Catalytic activity is almost as efficient as
FT wild type."
FT /evidence="ECO:0000269|PubMed:12899635"
FT MUTAGEN 67
FT /note="R->K: Reduces substrate CoA binding."
FT /evidence="ECO:0000269|PubMed:11747444"
FT MUTAGEN 67
FT /note="R->L: Forms inclusion bodies."
FT /evidence="ECO:0000269|PubMed:11747444"
FT MUTAGEN 68
FT /note="E->T: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:8718880"
FT MUTAGEN 81
FT /note="H->Q: Loss of catalytic activity, substrate benzoyl
FT group binding is not affected."
FT /evidence="ECO:0000269|PubMed:8718880,
FT ECO:0000269|PubMed:9063883"
FT MUTAGEN 82
FT /note="F->L: Retains catalytic activity, but substrate
FT benzoyl group binding is decreased."
FT /evidence="ECO:0000269|PubMed:9063883"
FT MUTAGEN 89
FT /note="W->F: Retains catalytic activity, but substrate
FT benzoyl group binding is decreased."
FT /evidence="ECO:0000269|PubMed:9063883"
FT MUTAGEN 89
FT /note="W->Y: Reduced activity and substrate benzoyl group
FT binding."
FT /evidence="ECO:0000269|PubMed:9063883"
FT MUTAGEN 90
FT /note="H->Q: Complete loss of catalytic activity
FT (PubMed:8718880 and PubMed:9063883). Significantly reduced
FT activity (PubMed:11695894). Substrate binding is not
FT significantly affected. Reduced arylated intermediate
FT formation."
FT /evidence="ECO:0000269|PubMed:11695894,
FT ECO:0000269|PubMed:8718880, ECO:0000269|PubMed:9063883"
FT MUTAGEN 94
FT /note="H->Q: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:8718880"
FT MUTAGEN 112
FT /note="A->G: Yields insoluble protein."
FT /evidence="ECO:0000269|PubMed:12899635"
FT MUTAGEN 112
FT /note="A->S: Protein precipitates upon purification."
FT /evidence="ECO:0000269|PubMed:12899635"
FT MUTAGEN 112
FT /note="A->V: Catalytic activity is almost as efficient as
FT wild type."
FT /evidence="ECO:0000269|PubMed:12899635"
FT MUTAGEN 113
FT /note="G->A: Strongly reduced catalytic activity and
FT substrate benzoyl group binding. Arylated intermediate does
FT not accumulate."
FT /evidence="ECO:0000269|PubMed:11747444,
FT ECO:0000269|PubMed:12899635"
FT MUTAGEN 113
FT /note="G->N,S: Strongly reduced catalytic activity.
FT Arylated intermediate does not accumulate."
FT /evidence="ECO:0000269|PubMed:11747444,
FT ECO:0000269|PubMed:12899635"
FT MUTAGEN 113
FT /note="G->V: Protein precipitates upon purification."
FT /evidence="ECO:0000269|PubMed:11747444,
FT ECO:0000269|PubMed:12899635"
FT MUTAGEN 114
FT /note="G->A: Strongly reduced catalytic activity and
FT substrate benzoyl group binding."
FT /evidence="ECO:0000269|PubMed:11747444,
FT ECO:0000269|PubMed:9063883"
FT MUTAGEN 114
FT /note="G->P: Unstable."
FT /evidence="ECO:0000269|PubMed:11747444,
FT ECO:0000269|PubMed:9063883"
FT MUTAGEN 115
FT /note="G->L,N,S,V: Yields insoluble protein."
FT /evidence="ECO:0000269|PubMed:12899635"
FT MUTAGEN 123
FT /note="D->T: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:8718880"
FT MUTAGEN 129
FT /note="D->T: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:8718880"
FT MUTAGEN 137
FT /note="W->F: Low catalytic activity, but KM unaffected
FT (PubMed:8718880). Retains catalytic activity, but substrate
FT benzoyl group binding is decreased (PubMed:9063883)."
FT /evidence="ECO:0000269|PubMed:8718880,
FT ECO:0000269|PubMed:9063883"
FT MUTAGEN 145
FT /note="D->A: Complete loss of catalytic activity, but not
FT substrate binding."
FT /evidence="ECO:0000269|PubMed:9063883"
FT MUTAGEN 163
FT /note="E->T: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:8718880"
FT MUTAGEN 175
FT /note="E->D: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:8718880"
FT MUTAGEN 179
FT /note="W->F: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:8718880"
FT MUTAGEN 208
FT /note="H->Q: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:8718880"
FT MUTAGEN 216
FT /note="R->E,K,L: Yields insoluble protein."
FT /evidence="ECO:0000269|PubMed:16388585"
FT MUTAGEN 232
FT /note="E->A,N,Q,R: Yields insoluble protein."
FT /evidence="ECO:0000269|PubMed:16388585"
FT MUTAGEN 232
FT /note="E->D: Reduced catalytic activity, increased
FT substrate binding."
FT /evidence="ECO:0000269|PubMed:16388585"
FT MUTAGEN 257
FT /note="R->K: Retains catalytic activity and substrate CoA
FT binding."
FT /evidence="ECO:0000269|PubMed:11747444"
FT MUTAGEN 257
FT /note="R->L: Significantly reduces catalytic activity and
FT substrate CoA binding."
FT /evidence="ECO:0000269|PubMed:11747444"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:1NZY"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:1NZY"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1NZY"
FT HELIX 29..44
FT /evidence="ECO:0007829|PDB:1NZY"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:1NZY"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1NZY"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1NZY"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1NZY"
FT HELIX 74..98
FT /evidence="ECO:0007829|PDB:1NZY"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1NZY"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:1NZY"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:1NZY"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:1NZY"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:1NZY"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:1NZY"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:1NZY"
FT HELIX 148..167
FT /evidence="ECO:0007829|PDB:1NZY"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:1NZY"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:1NZY"
FT HELIX 188..204
FT /evidence="ECO:0007829|PDB:1NZY"
FT HELIX 207..220
FT /evidence="ECO:0007829|PDB:1NZY"
FT HELIX 225..241
FT /evidence="ECO:0007829|PDB:1NZY"
FT HELIX 245..253
FT /evidence="ECO:0007829|PDB:1NZY"
SQ SEQUENCE 269 AA; 29802 MW; EC165E9063C70B07 CRC64;
MYEAIGHRVE DGVAEITIKL PRHRNALSVK AMQEVTDALN RAEEDDSVGA VMITGAEDAF
CAGFYLREIP LDKGVAGVRD HFRIGALWWH QMIHKIIRVK RPVLAAINGV AAGGGLGISL
ASDMAICADS AKFVCAWHTI GIGNDTATSY SLARIVGMRR AMELMLTNRT LYPEEAKDWG
LVSRVYPKDD FREVAWKVAR ELAAAPTHLQ VMAKERFHAG WMQPVEECTE FEIQNVIASV
THPHFMPCLT EFLDGHRADR PQVELPAGV
