4HBT_PSEUC
ID 4HBT_PSEUC Reviewed; 141 AA.
AC P56653; A5JTM7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=4-hydroxybenzoyl-CoA thioesterase;
DE EC=3.1.2.23;
OS Pseudomonas sp. (strain CBS-3).
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=72586;
RN [1]
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, AND SUBUNIT.
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 [4]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-17; ARG-88; ARG-89;
RP LYS-90; ARG-126 AND ARG-128.
RX PubMed=12220180; DOI=10.1021/bi0262303;
RA Zhuang Z., Song F., Zhang W., Taylor K., Archambault A.,
RA Dunaway-Mariano D., Dong J., Carey P.R.;
RT "Kinetic, Raman, NMR, and site-directed mutagenesis studies of the
RT Pseudomonas sp. strain CBS3 4-hydroxybenzoyl-CoA thioesterase active
RT site.";
RL Biochemistry 41:11152-11160(2002).
RN [5]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-32.
RX PubMed=16962159; DOI=10.1016/j.bioorg.2006.07.002;
RA Song F., Zhuang Z., Dunaway-Mariano D.;
RT "Structure-activity analysis of base and enzyme-catalyzed 4-hydroxybenzoyl
RT coenzyme A hydrolysis.";
RL Bioorg. Chem. 35:1-10(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
RX PubMed=9837940; DOI=10.1074/jbc.273.50.33572;
RA Benning M.M., Wesenberg G., Liu R., Taylor K.L., Dunaway-Mariano D.,
RA Holden H.M.;
RT "The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from
RT Pseudomonas sp. strain CBS-3.";
RL J. Biol. Chem. 273:33572-33579(1998).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF WILD-TYPE IN COMPLEX WITH
RP INHIBITOR AND MUTANT ASN-17 IN COMPLEX WITH SUBSTRATE, SUBUNIT, AND ACTIVE
RP SITE.
RX PubMed=11997398; DOI=10.1074/jbc.m203904200;
RA Thoden J.B., Holden H.M., Zhuang Z., Dunaway-Mariano D.;
RT "X-ray crystallographic analyses of inhibitor and substrate complexes of
RT wild-type and mutant 4-hydroxybenzoyl-CoA thioesterase.";
RL J. Biol. Chem. 277:27468-27476(2002).
CC -!- FUNCTION: Hydrolyzes 4-hydroxybenzoate-CoA, and to a lesser extent
CC benzoyl-CoA and 4-chlorobenzoate-CoA. Not active against aliphatic
CC acyl-CoA thioesters, including palmitoyl-CoA, hexanoyl-CoA and acetyl-
CC CoA. {ECO:0000269|PubMed:1610806}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA + H(+);
CC Xref=Rhea:RHEA:11948, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17879, ChEBI:CHEBI:57287, ChEBI:CHEBI:57356; EC=3.1.2.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10041,
CC ECO:0000269|PubMed:1610806};
CC -!- ACTIVITY REGULATION: Unaffected by EDTA, Mg(2+), Mn(2+), Fe(2+),
CC Ca(2+), Co(2+) and Zn(2+). {ECO:0000269|PubMed:1610806}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 uM for 4-hydroxybenzoyl-CoA {ECO:0000269|PubMed:12220180,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16962159};
CC KM=550 uM for 4-chlorobenzoyl-CoA {ECO:0000269|PubMed:12220180,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16962159};
CC KM=200 uM for benzoyl-CoA {ECO:0000269|PubMed:12220180,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16962159};
CC KM=270 uM for 4-hydroxybenzoyl-pantetheine
CC {ECO:0000269|PubMed:12220180, ECO:0000269|PubMed:1610806,
CC ECO:0000269|PubMed:16962159};
CC KM=56 uM for 4-methoxybenzoyl-CoA {ECO:0000269|PubMed:12220180,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16962159};
CC KM=230 uM for 4-methylbenzoyl-CoA {ECO:0000269|PubMed:12220180,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16962159};
CC KM=510 uM for benzoyl-CoA {ECO:0000269|PubMed:12220180,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16962159};
CC KM=520 uM for 4-fluorobenzoyl-CoA {ECO:0000269|PubMed:12220180,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16962159};
CC KM=300 uM for 4-trifluorobenzoyl-CoA {ECO:0000269|PubMed:12220180,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:16962159};
CC -!- PATHWAY: Xenobiotic degradation; 4-chlorobenzoate degradation; 4-
CC hydroxybenzoate from 4-chlorobenzoate: step 3/3.
CC {ECO:0000269|PubMed:1610806}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11997398,
CC ECO:0000269|PubMed:1610806, ECO:0000269|PubMed:9837940}.
CC -!- SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase family.
CC {ECO:0000305}.
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DR EMBL; EF569604; ABQ44580.1; -; Genomic_DNA.
DR PDB; 1BVQ; X-ray; 2.00 A; A=1-141.
DR PDB; 1LO7; X-ray; 1.50 A; A=1-141.
DR PDB; 1LO8; X-ray; 1.80 A; A=1-141.
DR PDB; 1LO9; X-ray; 2.80 A; A=1-141.
DR PDBsum; 1BVQ; -.
DR PDBsum; 1LO7; -.
DR PDBsum; 1LO8; -.
DR PDBsum; 1LO9; -.
DR AlphaFoldDB; P56653; -.
DR SMR; P56653; -.
DR DrugBank; DB01652; 4-hydroxybenzoyl-CoA.
DR DrugBank; DB04067; 4-hydroxybenzyl coenzyme A.
DR DrugBank; DB03613; 4-hydroxyphenacyl coenzyme A.
DR KEGG; ag:ABQ44580; -.
DR BioCyc; MetaCyc:MON-14754; -.
DR BRENDA; 3.1.2.23; 5085.
DR SABIO-RK; P56653; -.
DR UniPathway; UPA01011; UER01022.
DR EvolutionaryTrace; P56653; -.
DR GO; GO:0018739; F:4-hydroxybenzoyl-CoA thioesterase activity; IDA:UniProtKB.
DR InterPro; IPR008272; HB-CoA_thioesterase_AS.
DR InterPro; IPR029069; HotDog_dom_sf.
DR SUPFAM; SSF54637; SSF54637; 1.
DR PROSITE; PS01328; 4HBCOA_THIOESTERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase.
FT CHAIN 1..141
FT /note="4-hydroxybenzoyl-CoA thioesterase"
FT /id="PRO_0000087760"
FT ACT_SITE 17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10041,
FT ECO:0000269|PubMed:11997398, ECO:0000269|PubMed:9837940"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11997398"
FT BINDING 59..61
FT /ligand="substrate"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11997398"
FT MUTAGEN 17
FT /note="D->E: Reduces catalytic activity. Little effect on
FT substrate binding."
FT /evidence="ECO:0000269|PubMed:12220180"
FT MUTAGEN 17
FT /note="D->N: Drastically reduces catalytic activity. No
FT effect on substrate binding."
FT /evidence="ECO:0000269|PubMed:12220180"
FT MUTAGEN 17
FT /note="D->S: Drastically reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:12220180"
FT MUTAGEN 32
FT /note="D->S: Substrate turnover rate is decreased."
FT /evidence="ECO:0000269|PubMed:16962159"
FT MUTAGEN 88
FT /note="R->A: No significant effect on catalytic activity or
FT substrate binding."
FT /evidence="ECO:0000269|PubMed:12220180"
FT MUTAGEN 89
FT /note="R->L: No significant effect on catalytic activity or
FT substrate binding."
FT /evidence="ECO:0000269|PubMed:12220180"
FT MUTAGEN 90
FT /note="K->A: Decreases substrate binding affinity."
FT /evidence="ECO:0000269|PubMed:12220180"
FT MUTAGEN 126
FT /note="R->L: No significant effect on catalytic activity or
FT substrate binding."
FT /evidence="ECO:0000269|PubMed:12220180"
FT MUTAGEN 128
FT /note="R->A: No significant effect on catalytic activity or
FT substrate binding."
FT /evidence="ECO:0000269|PubMed:12220180"
FT CONFLICT 107
FT /note="V -> L (in Ref. 2; ABQ44580)"
FT /evidence="ECO:0000305"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1LO7"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1LO7"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:1LO7"
FT HELIX 25..41
FT /evidence="ECO:0007829|PDB:1LO7"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:1LO7"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1LO7"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:1LO7"
FT STRAND 77..87
FT /evidence="ECO:0007829|PDB:1LO7"
FT STRAND 89..101
FT /evidence="ECO:0007829|PDB:1LO7"
FT STRAND 107..123
FT /evidence="ECO:0007829|PDB:1LO7"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:1LO7"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:1LO7"
SQ SEQUENCE 141 AA; 16105 MW; 410896EA5CC49F22 CRC64;
MARSITMQQR IEFGDCDPAG IVWFPNYHRW LDAASRNYFI KCGLPPWRQT VVERGIVGTP
IVSCNASFVC TASYDDVLTI ETCIKEWRRK SFVQRHSVSR TTPGGDVQLV MRADEIRVFA
MNDGERLRAI EVPADYIELC S
