TESB_ECOLI
ID TESB_ECOLI Reviewed; 286 AA.
AC P0AGG2; P23911; Q2MBX4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Acyl-CoA thioesterase 2;
DE EC=3.1.2.20 {ECO:0000269|PubMed:10876240, ECO:0000269|PubMed:14707139, ECO:0000269|PubMed:1645722, ECO:0000269|PubMed:18702504, ECO:0000269|PubMed:20547355, ECO:0000269|PubMed:24271180};
DE AltName: Full=Thioesterase II {ECO:0000303|PubMed:1645722};
DE Short=TEII {ECO:0000303|PubMed:10876240};
GN Name=tesB {ECO:0000303|PubMed:1645722}; OrderedLocusNames=b0452, JW0442;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-7 AND 56-63,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND ACTIVITY REGULATION.
RC STRAIN=K12;
RX PubMed=1645722; DOI=10.1016/s0021-9258(18)99125-8;
RA Naggert J., Narasimhan M.L., Deveaux L., Cho H., Randhawa Z.I.,
RA Cronan J.E. Jr., Green B.N., Smith S.;
RT "Cloning, sequencing, and characterization of Escherichia coli thioesterase
RT II.";
RL J. Biol. Chem. 266:11044-11050(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14707139; DOI=10.1074/jbc.m310032200;
RA Ren Y., Aguirre J., Ntamack A.G., Chu C., Schulz H.;
RT "An alternative pathway of oleate beta-oxidation in Escherichia coli
RT involving the hydrolysis of a dead end intermediate by a thioesterase.";
RL J. Biol. Chem. 279:11042-11050(2004).
RN [6]
RP CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
RX PubMed=17609944; DOI=10.1007/s00253-007-1063-0;
RA Liu Q., Ouyang S.P., Chung A., Wu Q., Chen G.Q.;
RT "Microbial production of R-3-hydroxybutyric acid by recombinant E. coli
RT harboring genes of phbA, phbB, and tesB.";
RL Appl. Microbiol. Biotechnol. 76:811-818(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18702504; DOI=10.1021/bi801074e;
RA Nie L., Ren Y., Janakiraman A., Smith S., Schulz H.;
RT "A novel paradigm of fatty acid beta-oxidation exemplified by the
RT thioesterase-dependent partial degradation of conjugated linoleic acid that
RT fully supports growth of Escherichia coli.";
RL Biochemistry 47:9618-9626(2008).
RN [8]
RP CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
RX PubMed=19304817; DOI=10.1128/aem.02667-08;
RA Tseng H.C., Martin C.H., Nielsen D.R., Prather K.L.;
RT "Metabolic engineering of Escherichia coli for enhanced production of
RT (R)- and (S)-3-hydroxybutyrate.";
RL Appl. Environ. Microbiol. 75:3137-3145(2009).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20547355; DOI=10.1016/j.jbiosc.2010.05.004;
RA Seto Y., Kang J., Ming L., Habu N., Nihei K., Ueda S., Maeda I.;
RT "Genetic replacement of tesB with PTE1 affects chain-length proportions of
RT 3-hydroxyalkanoic acids produced through beta-oxidation of oleic acid in
RT Escherichia coli.";
RL J. Biosci. Bioeng. 110:392-396(2010).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=24271180; DOI=10.1128/aem.03303-13;
RA McMahon M.D., Prather K.L.;
RT "Functional screening and in vitro analysis reveal thioesterases with
RT enhanced substrate specificity profiles that improve short-chain fatty acid
RT production in Escherichia coli.";
RL Appl. Environ. Microbiol. 80:1042-1050(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, REACTION MECHANISM, AND
RP MUTAGENESIS OF SER-107; ASP-204 AND GLU-279.
RX PubMed=10876240; DOI=10.1038/76776;
RA Li J., Derewenda U., Dauter Z., Smith S., Derewenda Z.S.;
RT "Crystal structure of the Escherichia coli thioesterase II, a homolog of
RT the human Nef binding enzyme.";
RL Nat. Struct. Biol. 7:555-559(2000).
CC -!- FUNCTION: Thioesterase that has relatively broad substrate specificity,
CC hydrolyzing primarily medium- and long-chain acyl-CoA substrates to
CC free fatty acids and CoA (PubMed:1645722, PubMed:24271180,
CC PubMed:20547355). Functions in the thioesterase-dependent pathway of
CC beta-oxidation of oleate and conjugated linoleate ((9Z,11E)-
CC octadecadienoate or CLA), which provides all energy and carbon
CC precursors required for the growth of E.coli. Thus, supports growth on
CC oleate or conjugated linoleate as the sole source of carbon by
CC hydrolyzing 3,5-tetradecadienoyl-CoA, the terminal metabolite of oleate
CC beta-oxidation via the alternative thioesterase-dependent pathway, and
CC 3,5-dodecadienoyl-CoA, the end product of CLA beta-oxidation,
CC respectively (PubMed:18702504, PubMed:14707139). Seems to be involved
CC in 3-hydroxyalkanoate production in E.coli (PubMed:20547355).
CC {ECO:0000269|PubMed:14707139, ECO:0000269|PubMed:1645722,
CC ECO:0000269|PubMed:18702504, ECO:0000269|PubMed:20547355,
CC ECO:0000269|PubMed:24271180}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+);
CC Xref=Rhea:RHEA:16781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; EC=3.1.2.20;
CC Evidence={ECO:0000269|PubMed:10876240, ECO:0000269|PubMed:14707139,
CC ECO:0000269|PubMed:1645722, ECO:0000269|PubMed:18702504,
CC ECO:0000269|PubMed:20547355, ECO:0000269|PubMed:24271180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16782;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385;
CC Evidence={ECO:0000269|PubMed:18702504, ECO:0000269|PubMed:24271180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000305|PubMed:18702504};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E,5Z)-tetradecadienoyl-CoA + H2O = (3E,5Z)-tetradecadienoate
CC + CoA + H(+); Xref=Rhea:RHEA:55044, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:71586,
CC ChEBI:CHEBI:71590; Evidence={ECO:0000269|PubMed:14707139,
CC ECO:0000269|PubMed:18702504};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55045;
CC Evidence={ECO:0000305|PubMed:14707139, ECO:0000305|PubMed:18702504};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+);
CC Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375;
CC Evidence={ECO:0000269|PubMed:18702504, ECO:0000269|PubMed:20547355,
CC ECO:0000269|PubMed:24271180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000305|PubMed:18702504, ECO:0000305|PubMed:20547355};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3Z,5E)-dodecadienoyl-CoA + H2O = (3Z,5E)-dodecadienoate + CoA
CC + H(+); Xref=Rhea:RHEA:65172, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:156333, ChEBI:CHEBI:156334;
CC Evidence={ECO:0000269|PubMed:18702504};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65173;
CC Evidence={ECO:0000269|PubMed:18702504};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+);
CC Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430;
CC Evidence={ECO:0000269|PubMed:10876240, ECO:0000269|PubMed:1645722,
CC ECO:0000269|PubMed:18702504, ECO:0000269|PubMed:24271180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC Evidence={ECO:0000305|PubMed:1645722, ECO:0000305|PubMed:18702504};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octanoyl-CoA = CoA + H(+) + octanoate;
CC Xref=Rhea:RHEA:30143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25646, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386;
CC Evidence={ECO:0000269|PubMed:18702504, ECO:0000269|PubMed:24271180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144;
CC Evidence={ECO:0000305|PubMed:18702504};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanoyl-CoA = CoA + H(+) + hexanoate;
CC Xref=Rhea:RHEA:40115, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000269|PubMed:24271180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116;
CC Evidence={ECO:0000305|PubMed:24271180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + pentanoyl-CoA = CoA + H(+) + pentanoate;
CC Xref=Rhea:RHEA:55052, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31011, ChEBI:CHEBI:57287, ChEBI:CHEBI:57389;
CC Evidence={ECO:0000269|PubMed:24271180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55053;
CC Evidence={ECO:0000305|PubMed:24271180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + H2O = butanoate + CoA + H(+);
CC Xref=Rhea:RHEA:40111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17968, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371;
CC Evidence={ECO:0000269|PubMed:20547355, ECO:0000269|PubMed:24271180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112;
CC Evidence={ECO:0000305|PubMed:20547355, ECO:0000305|PubMed:24271180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methylpentanoyl-CoA + H2O = 4-methylpentanoate + CoA + H(+);
CC Xref=Rhea:RHEA:55064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:74904, ChEBI:CHEBI:131445;
CC Evidence={ECO:0000269|PubMed:24271180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55065;
CC Evidence={ECO:0000305|PubMed:24271180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-3-hydroxypentanoyl-CoA + H2O = (3R)-3-hydroxypentanoate +
CC CoA + H(+); Xref=Rhea:RHEA:55084, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:138587,
CC ChEBI:CHEBI:138588; Evidence={ECO:0000269|PubMed:24271180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55085;
CC Evidence={ECO:0000305|PubMed:24271180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxypentanoyl-CoA + H2O = (3S)-3-hydroxypentanoate +
CC CoA + H(+); Xref=Rhea:RHEA:55096, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:138607,
CC ChEBI:CHEBI:138608; Evidence={ECO:0000269|PubMed:24271180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55097;
CC Evidence={ECO:0000305|PubMed:24271180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379;
CC Evidence={ECO:0000269|PubMed:18702504};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000305|PubMed:18702504};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate;
CC Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394;
CC Evidence={ECO:0000269|PubMed:18702504};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC Evidence={ECO:0000305|PubMed:18702504};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+);
CC Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387;
CC Evidence={ECO:0000269|PubMed:18702504};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140;
CC Evidence={ECO:0000305|PubMed:18702504};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-3-hydroxybutanoyl-CoA + H2O = (R)-3-hydroxybutanoate +
CC CoA + H(+); Xref=Rhea:RHEA:65204, ChEBI:CHEBI:10983,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57315; Evidence={ECO:0000269|PubMed:17609944,
CC ECO:0000269|PubMed:19304817};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65205;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxybutanoyl-CoA + H2O = (S)-3-hydroxybutanoate +
CC CoA + H(+); Xref=Rhea:RHEA:65208, ChEBI:CHEBI:11047,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57316; Evidence={ECO:0000269|PubMed:19304817};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65209;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-dodecenoyl-CoA + H2O = (2E)-dodecenoate + CoA + H(+);
CC Xref=Rhea:RHEA:65212, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57330, ChEBI:CHEBI:84274;
CC Evidence={ECO:0000269|PubMed:20547355};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65213;
CC Evidence={ECO:0000305|PubMed:20547355};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxododecanoyl-CoA + H2O = 3-oxododecanoate + CoA + H(+);
CC Xref=Rhea:RHEA:65216, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29743, ChEBI:CHEBI:57287, ChEBI:CHEBI:62615;
CC Evidence={ECO:0000269|PubMed:20547355};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65217;
CC Evidence={ECO:0000305|PubMed:20547355};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxydodecanoyl-CoA + H2O = 3-hydroxydodecanoate + CoA +
CC H(+); Xref=Rhea:RHEA:65232, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:76616, ChEBI:CHEBI:156383;
CC Evidence={ECO:0000269|PubMed:20547355};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65233;
CC Evidence={ECO:0000305|PubMed:20547355};
CC -!- ACTIVITY REGULATION: Inhibited by iodoacetamide and
CC diethylpyrocarbonate in vitro, but is insensitive to iodoacetate
CC treatment. {ECO:0000269|PubMed:1645722}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13 uM for decanoyl-CoA {ECO:0000269|PubMed:10876240};
CC KM=9 uM for dodecanoyl-CoA {ECO:0000269|PubMed:18702504};
CC KM=6 uM for 3,5-dodecadienoyl-CoA {ECO:0000269|PubMed:18702504};
CC KM=13 uM for tetradecanoyl-CoA {ECO:0000269|PubMed:18702504};
CC KM=7 uM for 3,5-tetradecadienoyl-CoA {ECO:0000269|PubMed:18702504};
CC KM=75 uM for butanoyl-CoA {ECO:0000269|PubMed:20547355};
CC KM=60 uM for (2E)-butenoyl-CoA {ECO:0000269|PubMed:20547355};
CC KM=81 uM for (RS)-3-hydroxybutanoyl-CoA
CC {ECO:0000269|PubMed:20547355};
CC KM=46 uM for 3-oxobutanoyl-CoA {ECO:0000269|PubMed:20547355};
CC KM=23 uM for dodecanoyl-CoA {ECO:0000269|PubMed:20547355};
CC KM=12 uM for (2E)-dodecenoyl-CoA {ECO:0000269|PubMed:20547355};
CC KM=6.3 uM for 3-hydroxydodecanoyl-CoA {ECO:0000269|PubMed:20547355};
CC KM=3.2 uM for 3-oxododecanoyl-CoA {ECO:0000269|PubMed:20547355};
CC Vmax=58 umol/min/mg enzyme with butanoyl-CoA as substrate
CC {ECO:0000269|PubMed:20547355};
CC Vmax=1.9 umol/min/mg enzyme with (2E)-butenoyl-CoA as substrate
CC {ECO:0000269|PubMed:20547355};
CC Vmax=34 umol/min/mg enzyme with (RS)-3-hydroxybutanoyl-CoA as
CC substrate {ECO:0000269|PubMed:20547355};
CC Vmax=21 umol/min/mg enzyme with 3-oxobutanoyl-CoA as substrate
CC {ECO:0000269|PubMed:20547355};
CC Vmax=234 umol/min/mg enzyme with dodecanoyl-CoA as substrate
CC {ECO:0000269|PubMed:20547355};
CC Vmax=36 umol/min/mg enzyme with (2E)-dodecenoyl-CoA as substrate
CC {ECO:0000269|PubMed:20547355};
CC Vmax=29 umol/min/mg enzyme with 3-hydroxydodecanoyl-CoA as substrate
CC {ECO:0000269|PubMed:20547355};
CC Vmax=77 umol/min/mg enzyme with 3-oxododecanoyl-CoA as substrate
CC {ECO:0000269|PubMed:20547355};
CC Note=kcat is 83 sec(-1) with decanoyl-CoA as substrate.
CC {ECO:0000269|PubMed:10876240};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:1645722}.
CC -!- DISRUPTION PHENOTYPE: Deletion of this gene decreases the growth rate
CC of cells on conjugated linoleate but not on palmitate
CC (PubMed:18702504). Deletion of this gene also decreases 3-
CC hydroxybutanoate, 3-hydroxyhexanoate, 3-hydroxyoctanoate, and hexanoate
CC in medium after cultivation with oleate as a sole carbon source
CC (PubMed:20547355). {ECO:0000269|PubMed:18702504,
CC ECO:0000269|PubMed:20547355}.
CC -!- BIOTECHNOLOGY: Has been used in the engineered enzymatic high-level
CC production of enantiomerically pure (R)- and (S)-3-hydroxybutanoate,
CC used as a building block for the synthesis of optically active fine
CC chemicals, such as vitamins, antibiotics, pheromones, and flavor
CC compounds. Chemical synthesis of chiral 3-hydroxybutanoate (3HB) is not
CC economically feasible. {ECO:0000269|PubMed:17609944,
CC ECO:0000269|PubMed:19304817}.
CC -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC {ECO:0000305}.
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DR EMBL; M63308; AAA24665.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40208.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73555.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76232.1; -; Genomic_DNA.
DR PIR; D64775; D64775.
DR RefSeq; NP_414986.1; NC_000913.3.
DR RefSeq; WP_000075876.1; NZ_STEB01000007.1.
DR PDB; 1C8U; X-ray; 1.90 A; A/B=2-286.
DR PDBsum; 1C8U; -.
DR AlphaFoldDB; P0AGG2; -.
DR SMR; P0AGG2; -.
DR BioGRID; 4259857; 17.
DR DIP; DIP-10980N; -.
DR IntAct; P0AGG2; 5.
DR STRING; 511145.b0452; -.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR SwissLipids; SLP:000001819; -.
DR jPOST; P0AGG2; -.
DR PaxDb; P0AGG2; -.
DR PRIDE; P0AGG2; -.
DR EnsemblBacteria; AAC73555; AAC73555; b0452.
DR EnsemblBacteria; BAE76232; BAE76232; BAE76232.
DR GeneID; 66671246; -.
DR GeneID; 945074; -.
DR KEGG; ecj:JW0442; -.
DR KEGG; eco:b0452; -.
DR PATRIC; fig|1411691.4.peg.1823; -.
DR EchoBASE; EB0988; -.
DR eggNOG; COG1946; Bacteria.
DR HOGENOM; CLU_032690_0_0_6; -.
DR InParanoid; P0AGG2; -.
DR OMA; SQVWFRT; -.
DR PhylomeDB; P0AGG2; -.
DR BioCyc; EcoCyc:THIOESTERII-MON; -.
DR BioCyc; MetaCyc:THIOESTERII-MON; -.
DR BRENDA; 3.1.2.2; 2026.
DR BRENDA; 3.1.2.20; 2026.
DR EvolutionaryTrace; P0AGG2; -.
DR PRO; PR:P0AGG2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:RHEA.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:RHEA.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0009062; P:fatty acid catabolic process; IMP:EcoCyc.
DR Gene3D; 2.40.160.210; -; 1.
DR InterPro; IPR042171; Acyl-CoA_hotdog.
DR InterPro; IPR003703; Acyl_CoA_thio.
DR InterPro; IPR029069; HotDog_dom_sf.
DR PANTHER; PTHR11066; PTHR11066; 1.
DR SUPFAM; SSF54637; SSF54637; 2.
DR TIGRFAMs; TIGR00189; tesB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Lipid metabolism;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1645722"
FT CHAIN 2..286
FT /note="Acyl-CoA thioesterase 2"
FT /id="PRO_0000202144"
FT ACT_SITE 204
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:10876240"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:10876240"
FT ACT_SITE 278
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:10876240"
FT MUTAGEN 107
FT /note="S->C: 2-fold reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:10876240"
FT MUTAGEN 204
FT /note="D->N,A: 1000-fold reduction in catalytic activity.
FT No significant change in substrate affinity."
FT /evidence="ECO:0000269|PubMed:10876240"
FT MUTAGEN 279
FT /note="E->Q: 4-fold reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:10876240"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:1C8U"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:1C8U"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1C8U"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:1C8U"
FT STRAND 56..64
FT /evidence="ECO:0007829|PDB:1C8U"
FT STRAND 74..83
FT /evidence="ECO:0007829|PDB:1C8U"
FT STRAND 85..96
FT /evidence="ECO:0007829|PDB:1C8U"
FT STRAND 99..109
FT /evidence="ECO:0007829|PDB:1C8U"
FT HELIX 133..140
FT /evidence="ECO:0007829|PDB:1C8U"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:1C8U"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:1C8U"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:1C8U"
FT STRAND 176..186
FT /evidence="ECO:0007829|PDB:1C8U"
FT HELIX 192..202
FT /evidence="ECO:0007829|PDB:1C8U"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:1C8U"
FT HELIX 208..215
FT /evidence="ECO:0007829|PDB:1C8U"
FT STRAND 224..235
FT /evidence="ECO:0007829|PDB:1C8U"
FT STRAND 245..255
FT /evidence="ECO:0007829|PDB:1C8U"
FT STRAND 258..267
FT /evidence="ECO:0007829|PDB:1C8U"
FT STRAND 272..284
FT /evidence="ECO:0007829|PDB:1C8U"
SQ SEQUENCE 286 AA; 31966 MW; 8E7C4A4BCF73CA4B CRC64;
MSQALKNLLT LLNLEKIEEG LFRGQSEDLG LRQVFGGQVV GQALYAAKET VPEERLVHSF
HSYFLRPGDS KKPIIYDVET LRDGNSFSAR RVAAIQNGKP IFYMTASFQA PEAGFEHQKT
MPSAPAPDGL PSETQIAQSL AHLLPPVLKD KFICDRPLEV RPVEFHNPLK GHVAEPHRQV
WIRANGSVPD DLRVHQYLLG YASDLNFLPV ALQPHGIGFL EPGIQIATID HSMWFHRPFN
LNEWLLYSVE STSASSARGF VRGEFYTQDG VLVASTVQEG VMRNHN
