ID   THIM_RAT                Reviewed;         397 AA.
AC   P13437;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   08-NOV-2023, entry version 152.
DE   RecName: Full=3-ketoacyl-CoA thiolase, mitochondrial {ECO:0000305};
DE            EC=2.3.1.16 {ECO:0000269|PubMed:16476568};
DE   AltName: Full=Acetyl-CoA acetyltransferase {ECO:0000305};
DE            EC=2.3.1.9 {ECO:0000269|PubMed:16476568};
DE   AltName: Full=Acetyl-CoA acyltransferase;
DE   AltName: Full=Acyl-CoA hydrolase, mitochondrial {ECO:0000305};
DE            EC=3.1.2.- {ECO:0000269|PubMed:16476568};
DE            EC=3.1.2.1 {ECO:0000269|PubMed:16476568};
DE            EC=3.1.2.2 {ECO:0000269|PubMed:16476568};
DE   AltName: Full=Beta-ketothiolase;
DE   AltName: Full=Mitochondrial 3-oxoacyl-CoA thiolase;
GN   Name=Acaa2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=3038520; DOI=10.1002/j.1460-2075.1987.tb02376.x;
RA   Arakawa H., Takiguchi M., Amaya Y., Nagata S., Hayashi H., Mori M.;
RT   "cDNA-derived amino acid sequence of rat mitochondrial 3-oxoacyl-CoA
RT   thiolase with no transient presequence: structural relationship with
RT   peroxisomal isozyme.";
RL   EMBO J. 6:1361-1366(1987).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   INDUCTION BY DEHP.
RX   PubMed=16476568; DOI=10.1016/j.bbalip.2006.01.001;
RA   Yamashita H., Itsuki A., Kimoto M., Hiemori M., Tsuji H.;
RT   "Acetate generation in rat liver mitochondria; acetyl-CoA hydrolase
RT   activity is demonstrated by 3-ketoacyl-CoA thiolase.";
RL   Biochim. Biophys. Acta 1761:17-23(2006).
CC   -!- FUNCTION: In the production of energy from fats, this is one of the
CC       enzymes that catalyzes the last step of the mitochondrial beta-
CC       oxidation pathway, an aerobic process breaking down fatty acids into
CC       acetyl-CoA (Probable). Using free coenzyme A/CoA, catalyzes the
CC       thiolytic cleavage of medium- to long-chain unbranched 3-oxoacyl-CoAs
CC       into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms
CC       (Probable). Also catalyzes the condensation of two acetyl-CoA molecules
CC       into acetoacetyl-CoA and could be involved in the production of ketone
CC       bodies (Probable). Also displays hydrolase activity on various fatty
CC       acyl-CoAs (PubMed:16476568). Thereby, could be responsible for the
CC       production of acetate in a side reaction to beta-oxidation (Probable).
CC       Abolishes BNIP3-mediated apoptosis and mitochondrial damage (By
CC       similarity). {ECO:0000250|UniProtKB:P42765,
CC       ECO:0000269|PubMed:16476568, ECO:0000305|PubMed:16476568}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC         Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC         Evidence={ECO:0000269|PubMed:16476568};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21565;
CC         Evidence={ECO:0000305|PubMed:16476568};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566;
CC         Evidence={ECO:0000305|PubMed:16476568};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036,
CC         ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9;
CC         Evidence={ECO:0000269|PubMed:16476568};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21037;
CC         Evidence={ECO:0000305|PubMed:16476568};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21038;
CC         Evidence={ECO:0000305|PubMed:16476568};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + H2O = acetate + CoA + H(+); Xref=Rhea:RHEA:20289,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=3.1.2.1;
CC         Evidence={ECO:0000269|PubMed:16476568};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20290;
CC         Evidence={ECO:0000305|PubMed:16476568};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + propanoyl-CoA = CoA + H(+) + propanoate;
CC         Xref=Rhea:RHEA:40103, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17272, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392;
CC         Evidence={ECO:0000269|PubMed:16476568};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40104;
CC         Evidence={ECO:0000305|PubMed:16476568};
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:16476568};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112;
CC         Evidence={ECO:0000305|PubMed:16476568};
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:16476568};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116;
CC         Evidence={ECO:0000305|PubMed:16476568};
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:0000250|UniProtKB:P42765};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144;
CC         Evidence={ECO:0000250|UniProtKB:P42765};
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:0000250|UniProtKB:P42765};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC         Evidence={ECO:0000250|UniProtKB:P42765};
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:16476568};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC         Evidence={ECO:0000305|PubMed:16476568};
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:0000250|UniProtKB:P42765};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC         Evidence={ECO:0000250|UniProtKB:P42765};
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; EC=3.1.2.2;
CC         Evidence={ECO:0000269|PubMed:16476568};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC         Evidence={ECO:0000305|PubMed:16476568};
CC   -!- ACTIVITY REGULATION: The 3-oxoacetyl-CoA thiolase activity is inhibited
CC       by acetyl-CoA while the acetyl-CoA hydrolase activity is inhibited by
CC       acetoacetyl-CoA. {ECO:0000269|PubMed:16476568}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=11.4 uM for acetoacetyl-CoA {ECO:0000269|PubMed:16476568};
CC         KM=0.71 mM for acetyl-CoA {ECO:0000269|PubMed:16476568};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000269|PubMed:16476568}.
CC   -!- SUBUNIT: Homotetramer. Interacts with BNIP3 (By similarity).
CC       {ECO:0000250|UniProtKB:P42765}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16476568}.
CC   -!- TISSUE SPECIFICITY: Expressed in liver, brown adipose tissue and heart
CC       (at protein level). {ECO:0000269|PubMed:16476568}.
CC   -!- INDUCTION: Up-regulated in liver, brown adipose tissue, heart,
CC       intestine and kidney by DEHP/bis(2-ethylhexyl)phthalate (at protein
CC       level). {ECO:0000269|PubMed:16476568}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
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DR   EMBL; X05341; CAA28952.1; -; mRNA.
DR   PIR; A29452; XURT.
DR   RefSeq; NP_569117.1; NM_130433.1.
DR   AlphaFoldDB; P13437; -.
DR   SMR; P13437; -.
DR   BioGRID; 250910; 3.
DR   IntAct; P13437; 2.
DR   STRING; 10116.ENSRNOP00000060140; -.
DR   SwissLipids; SLP:000001412; -.
DR   CarbonylDB; P13437; -.
DR   GlyGen; P13437; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; P13437; -.
DR   PhosphoSitePlus; P13437; -.
DR   SwissPalm; P13437; -.
DR   jPOST; P13437; -.
DR   PaxDb; 10116-ENSRNOP00000060140; -.
DR   GeneID; 170465; -.
DR   KEGG; rno:170465; -.
DR   AGR; RGD:620482; -.
DR   CTD; 10449; -.
DR   RGD; 620482; Acaa2.
DR   eggNOG; KOG1391; Eukaryota.
DR   InParanoid; P13437; -.
DR   OrthoDB; 5481312at2759; -.
DR   PhylomeDB; P13437; -.
DR   Reactome; R-RNO-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR   SABIO-RK; P13437; -.
DR   UniPathway; UPA00659; -.
DR   PRO; PR:P13437; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:RGD.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; ISO:RGD.
DR   GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IDA:RGD.
DR   GO; GO:0003986; F:acetyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IDA:RGD.
DR   GO; GO:0071456; P:cellular response to hypoxia; ISO:RGD.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IDA:RGD.
DR   GO; GO:1902109; P:negative regulation of mitochondrial membrane permeability involved in apoptotic process; ISO:RGD.
DR   GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; ISS:UniProtKB.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR   InterPro; IPR020610; Thiolase_AS.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020613; Thiolase_CS.
DR   InterPro; IPR020616; Thiolase_N.
DR   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   PANTHER; PTHR18919:SF107; 3-KETOACYL-COA THIOLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00737; THIOLASE_2; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Acyltransferase; Fatty acid metabolism; Hydrolase;
KW   Lipid metabolism; Mitochondrion; Phosphoprotein; Reference proteome;
KW   Transferase; Transit peptide.
FT   CHAIN           1..397
FT                   /note="3-ketoacyl-CoA thiolase, mitochondrial"
FT                   /id="PRO_0000223301"
FT   TRANSIT         1..16
FT                   /note="Mitochondrion; not cleaved"
FT   ACT_SITE        92
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P42765"
FT   ACT_SITE        382
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT   BINDING         224
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:P42765"
FT   BINDING         227
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:P42765"
FT   BINDING         251
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:P42765"
FT   SITE            352
FT                   /note="Increases nucleophilicity of active site Cys"
FT                   /evidence="ECO:0000250|UniProtKB:P42765"
FT   MOD_RES         25
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         25
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         45
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         119
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P42765"
FT   MOD_RES         121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42765"
FT   MOD_RES         127
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P42765"
FT   MOD_RES         136
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         137
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         137
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         143
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         143
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         158
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         158
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         171
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         171
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         191
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         191
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         209
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         209
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         211
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         212
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         214
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         240
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         241
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         269
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         270
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         305
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         305
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         310
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         312
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         312
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         333
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42765"
FT   MOD_RES         340
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         344
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT   MOD_RES         375
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWT1"
SQ   SEQUENCE   397 AA;  41871 MW;  8344FB7271C3E2E1 CRC64;
     MALLRGVFIV AAKRTPFGAY GGLLKDFTAT DLTEFAARAA LSAGKVPPET IDSVIVGNVM
     QSSSDAAYLA RHVGLRVGVP TETGALTLNR LCGSGFQSIV SGCQEICSKD AEVVLCGGTE
     SMSQSPYSVR NVRFGTKFGL DLKLEDTLWA GLTDQHVKLP MGMTAENLAA KYNISREDCD
     RYALQSQQRW KAANEAGYFN EEMAPIEVKT KKGKQTMQVD EHARPQTTLE QLQNLPPVFK
     KEGTVTAGNA SGMSDGAGVV IIASEDAVKK HNFTPLARVV GYFVSGCDPA IMGIGPVPAI
     TGALKKAGLS LKDMDLIDVN EAFAPQFLAV QKSLDLDPSK TNVSGGAIAL GHPLGGSGSR
     ITAHLVHELR RRGGKYAVGS ACIGGGQGIS LIIQNTA
//