4HBT_ARTSP
ID 4HBT_ARTSP Reviewed; 151 AA.
AC Q04416; Q2A653; Q7BUB8; Q9AJQ4;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=4-hydroxybenzoyl-CoA thioesterase {ECO:0000303|PubMed:12732540};
DE Short=4-HBA-CoA thioesterase {ECO:0000303|PubMed:12732540};
DE EC=3.1.2.23;
GN Name=fcbC {ECO:0000312|EMBL:CAJ77823.1};
GN Synonyms=fcbC1 {ECO:0000312|EMBL:AAC80224.1};
OS Arthrobacter sp.
OG Plasmid pASU1 {ECO:0000312|EMBL:AAC80224.1}.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=1667;
RN [1] {ECO:0000312|EMBL:AAC80224.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 20407 / SU {ECO:0000312|EMBL:AAC80224.1}; PLASMID=pASU1;
RX PubMed=1476446; DOI=10.1128/aem.58.12.4068-4071.1992;
RA Schmitz A., Gartemann K.H., Fiedler J., Grund E., Eichenlaub R.;
RT "Cloning and sequence analysis of genes for dehalogenation of 4-
RT chlorobenzoate from Arthrobacter sp. strain SU.";
RL Appl. Environ. Microbiol. 58:4068-4071(1992).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF76242.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCIB 12013 / TM1 {ECO:0000312|EMBL:AAF76242.1};
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 [3] {ECO:0000312|EMBL:CAJ77823.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FG1 {ECO:0000269|PubMed:17384944};
RX PubMed=17384944; DOI=10.1007/s00253-007-0906-z;
RA Radice F., Orlandi V., Massa V., Battini V., Bertoni G., Reineke W.,
RA Barbieri P.;
RT "Cloning of the Arthrobacter sp. FG1 dehalogenase genes and construction of
RT hybrid pathways in Pseudomonas putida strains.";
RL Appl. Microbiol. Biotechnol. 75:1111-1118(2007).
RN [4] {ECO:0000312|EMBL:BAB40578.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FHP1 {ECO:0000312|EMBL:BAB40578.1};
RA Miyashita K., Ogawa N., Tsumori Y.;
RT "4-chlorobenzoate dehalogenase genes are tandemly duplicated in
RT Arthrobacter sp. FHP1.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MASS SPECTROMETRY.
RC STRAIN=DSM 20407 / SU {ECO:0000269|PubMed:12732540};
RX PubMed=12732540; DOI=10.1128/aem.69.5.2707-2711.2003;
RA Zhuang Z., Gartemann K.H., Eichenlaub R., Dunaway-Mariano D.;
RT "Characterization of the 4-hydroxybenzoyl-coenzyme A thioesterase from
RT Arthrobacter sp. strain SU.";
RL Appl. Environ. Microbiol. 69:2707-2711(2003).
RN [6] {ECO:0000312|PDB:1Q4T}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND
RP IN COMPLEX WITH PRODUCT, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF GLU-73.
RC STRAIN=DSM 20407 / SU {ECO:0000269|PubMed:12907670};
RX PubMed=12907670; DOI=10.1074/jbc.m308198200;
RA Thoden J.B., Zhuang Z., Dunaway-Mariano D., Holden H.M.;
RT "The structure of 4-hydroxybenzoyl-CoA thioesterase from arthrobacter sp.
RT strain SU.";
RL J. Biol. Chem. 278:43709-43716(2003).
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:0000269|PubMed:12732540};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=243 uM for benzoyl-CoA {ECO:0000269|PubMed:12732540};
CC KM=1.24 uM for 4-hydroxybenzoyl-CoA {ECO:0000269|PubMed:12732540};
CC KM=22 uM for 3-hydroxybenzoyl-CoA {ECO:0000269|PubMed:12732540};
CC KM=29 uM for 2,5-dihydroxybenzoyl-CoA {ECO:0000269|PubMed:12732540};
CC KM=113 uM for 4-chlorobenzoyl-CoA {ECO:0000269|PubMed:12732540};
CC KM=140 uM for phenylacetyl-CoA {ECO:0000269|PubMed:12732540};
CC KM=2200 uM for acetyl-CoA {ECO:0000269|PubMed:12732540};
CC KM=1100 uM for propionyl-CoA {ECO:0000269|PubMed:12732540};
CC KM=930 uM for butyryl-CoA {ECO:0000269|PubMed:12732540};
CC KM=810 uM for crotonyl-CoA {ECO:0000269|PubMed:12732540};
CC pH dependence:
CC Optimum pH is 4.6-9.6. {ECO:0000269|PubMed:12732540};
CC -!- PATHWAY: Xenobiotic degradation; 4-chlorobenzoate degradation; 4-
CC hydroxybenzoate from 4-chlorobenzoate: step 3/3.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12907670}.
CC -!- MASS SPECTROMETRY: Mass=16394.40; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12732540};
CC -!- SIMILARITY: Belongs to the thioesterase PaaI family. {ECO:0000305}.
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DR EMBL; M93187; AAC80224.1; -; Genomic_DNA.
DR EMBL; AF042490; AAF76242.1; -; Genomic_DNA.
DR EMBL; AM231748; CAJ77823.1; -; Genomic_DNA.
DR EMBL; AB041030; BAB40578.1; -; Genomic_DNA.
DR PDB; 1Q4S; X-ray; 1.95 A; A/B=1-151.
DR PDB; 1Q4T; X-ray; 1.60 A; A/B=1-151.
DR PDB; 1Q4U; X-ray; 1.60 A; A/B=1-151.
DR PDB; 3R32; X-ray; 1.80 A; A/B=1-151.
DR PDB; 3R34; X-ray; 1.80 A; A/B=1-151.
DR PDB; 3R35; X-ray; 1.80 A; A/B=1-151.
DR PDB; 3R36; X-ray; 1.95 A; A/B=1-151.
DR PDB; 3R37; X-ray; 1.80 A; A/B=1-151.
DR PDB; 3R3A; X-ray; 1.80 A; A/B=1-151.
DR PDB; 3R3B; X-ray; 1.80 A; A/B=1-151.
DR PDB; 3R3C; X-ray; 1.80 A; A/B=1-151.
DR PDB; 3R3D; X-ray; 1.75 A; A/B=1-151.
DR PDB; 3R3F; X-ray; 1.75 A; A/B=1-151.
DR PDB; 3TEA; X-ray; 1.80 A; A/B=1-151.
DR PDBsum; 1Q4S; -.
DR PDBsum; 1Q4T; -.
DR PDBsum; 1Q4U; -.
DR PDBsum; 3R32; -.
DR PDBsum; 3R34; -.
DR PDBsum; 3R35; -.
DR PDBsum; 3R36; -.
DR PDBsum; 3R37; -.
DR PDBsum; 3R3A; -.
DR PDBsum; 3R3B; -.
DR PDBsum; 3R3C; -.
DR PDBsum; 3R3D; -.
DR PDBsum; 3R3F; -.
DR PDBsum; 3TEA; -.
DR AlphaFoldDB; Q04416; -.
DR SMR; Q04416; -.
DR DrugBank; DB04242; 4-hydroxybenzoic acid.
DR DrugBank; DB04067; 4-hydroxybenzyl coenzyme A.
DR DrugBank; DB03613; 4-hydroxyphenacyl coenzyme A.
DR DrugBank; DB01992; Coenzyme A.
DR BRENDA; 3.1.2.23; 457.
DR SABIO-RK; Q04416; -.
DR UniPathway; UPA01011; UER01022.
DR EvolutionaryTrace; Q04416; -.
DR GO; GO:0018739; F:4-hydroxybenzoyl-CoA thioesterase activity; IDA:UniProtKB.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR003736; PAAI_dom.
DR InterPro; IPR006683; Thioestr_dom.
DR Pfam; PF03061; 4HBT; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
DR TIGRFAMs; TIGR00369; unchar_dom_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Plasmid.
FT CHAIN 1..151
FT /note="4-hydroxybenzoyl-CoA thioesterase"
FT /id="PRO_0000400829"
FT ACT_SITE 73
FT /evidence="ECO:0000269|PubMed:12907670"
FT BINDING 100..102
FT /ligand="substrate"
FT MUTAGEN 73
FT /note="E->A: Drastically reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:12907670"
FT CONFLICT 37
FT /note="V -> I (in Ref. 4; BAB40578)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="A -> T (in Ref. 4; BAB40578)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="V -> I (in Ref. 4; BAB40578)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="D -> N (in Ref. 4; BAB40578)"
FT /evidence="ECO:0000305"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3R32"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:1Q4T"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:1Q4T"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:1Q4T"
FT STRAND 43..51
FT /evidence="ECO:0007829|PDB:1Q4T"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1Q4T"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1Q4T"
FT HELIX 65..84
FT /evidence="ECO:0007829|PDB:1Q4T"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1Q4T"
FT STRAND 89..102
FT /evidence="ECO:0007829|PDB:1Q4T"
FT STRAND 106..118
FT /evidence="ECO:0007829|PDB:1Q4T"
FT STRAND 120..130
FT /evidence="ECO:0007829|PDB:1Q4T"
FT STRAND 136..148
FT /evidence="ECO:0007829|PDB:1Q4T"
SQ SEQUENCE 151 AA; 16394 MW; 95738A4BBD241A7E CRC64;
MHRTSNGSHA TGGNLPDVAS HYPVAYEQTL DGTVGFVIDE MTPERATASV EVTDTLRQRW
GLVHGGAYCA LAEMLATEAT VAVVHEKGMM AVGQSNHTSF FRPVKEGHVR AEAVRIHAGS
TTWFWDVSLR DDAGRLCAVS SMSIAVRPRR D
