THIM_BOVIN
ID THIM_BOVIN Reviewed; 397 AA.
AC Q3T0R7; B4X9P2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=3-ketoacyl-CoA thiolase, mitochondrial {ECO:0000305};
DE EC=2.3.1.16 {ECO:0000250|UniProtKB:P42765};
DE AltName: Full=Acetyl-CoA acetyltransferase {ECO:0000305};
DE EC=2.3.1.9 {ECO:0000255|PROSITE-ProRule:PRU10020};
DE AltName: Full=Acetyl-CoA acyltransferase;
DE AltName: Full=Acyl-CoA hydrolase, mitochondrial {ECO:0000305};
DE EC=3.1.2.- {ECO:0000250|UniProtKB:P42765};
DE EC=3.1.2.1 {ECO:0000250|UniProtKB:P42765};
DE EC=3.1.2.2 {ECO:0000250|UniProtKB:P13437};
DE AltName: Full=Beta-ketothiolase;
DE AltName: Full=Mitochondrial 3-oxoacyl-CoA thiolase;
GN Name=ACAA2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Li H., Xu S., Gao X.;
RT "Association analysis of bovine ACAA2 and economic traits.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. Using free coenzyme A/CoA, catalyzes the thiolytic cleavage
CC of medium- to long-chain unbranched 3-oxoacyl-CoAs into acetyl-CoA and
CC a fatty acyl-CoA shortened by two carbon atoms. Also catalyzes the
CC condensation of two acetyl-CoA molecules into acetoacetyl-CoA and could
CC be involved in the production of ketone bodies. Also displays hydrolase
CC activity on various fatty acyl-CoAs (By similarity). Thereby, could be
CC responsible for the production of acetate in a side reaction to beta-
CC oxidation (By similarity). Abolishes BNIP3-mediated apoptosis and
CC mitochondrial damage (By similarity). {ECO:0000250|UniProtKB:P13437,
CC ECO:0000250|UniProtKB:P42765}.
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:0000250|UniProtKB:P42765};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21565;
CC Evidence={ECO:0000250|UniProtKB:P42765};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566;
CC Evidence={ECO:0000250|UniProtKB:P42765};
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:0000255|PROSITE-ProRule:PRU10020};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21037;
CC Evidence={ECO:0000250|UniProtKB:P42765};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21038;
CC Evidence={ECO:0000250|UniProtKB:P42765};
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:0000250|UniProtKB:P42765};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20290;
CC Evidence={ECO:0000250|UniProtKB:P42765};
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:0000250|UniProtKB:P42765};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40104;
CC Evidence={ECO:0000250|UniProtKB:P42765};
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:0000250|UniProtKB:P42765};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112;
CC Evidence={ECO:0000250|UniProtKB:P42765};
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:0000250|UniProtKB:P42765};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116;
CC Evidence={ECO:0000250|UniProtKB:P42765};
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:0000250|UniProtKB:P42765};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000250|UniProtKB:P42765};
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:0000250|UniProtKB:P13437};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000250|UniProtKB:P42765};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:P42765}.
CC -!- SUBUNIT: Homotetramer. Interacts with BNIP3.
CC {ECO:0000250|UniProtKB:P42765}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P42765}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; EF583004; ABU62844.1; -; mRNA.
DR EMBL; EF583005; ABU62845.1; -; Genomic_DNA.
DR EMBL; BT025480; ABF57436.1; -; mRNA.
DR EMBL; BC102287; AAI02288.1; -; mRNA.
DR RefSeq; NP_001030419.1; NM_001035342.2.
DR AlphaFoldDB; Q3T0R7; -.
DR SMR; Q3T0R7; -.
DR IntAct; Q3T0R7; 1.
DR STRING; 9913.ENSBTAP00000003716; -.
DR PaxDb; Q3T0R7; -.
DR PeptideAtlas; Q3T0R7; -.
DR PRIDE; Q3T0R7; -.
DR Ensembl; ENSBTAT00000003716; ENSBTAP00000003716; ENSBTAG00000002863.
DR GeneID; 522006; -.
DR KEGG; bta:522006; -.
DR CTD; 10449; -.
DR VEuPathDB; HostDB:ENSBTAG00000002863; -.
DR VGNC; VGNC:25518; ACAA2.
DR eggNOG; KOG1391; Eukaryota.
DR GeneTree; ENSGT01030000234626; -.
DR HOGENOM; CLU_031026_0_0_1; -.
DR InParanoid; Q3T0R7; -.
DR OMA; GIWEINE; -.
DR OrthoDB; 1129049at2759; -.
DR TreeFam; TF105696; -.
DR SABIO-RK; Q3T0R7; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000002863; Expressed in liver and 104 other tissues.
DR ExpressionAtlas; Q3T0R7; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; ISS: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:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
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; -; 1.
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 Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 2: Evidence at transcript 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_0000270498"
FT TRANSIT 1..16
FT /note="Mitochondrion; not cleaved"
FT /evidence="ECO:0000250"
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:0000250|UniProtKB:P42765"
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 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 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42765"
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 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 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 234
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
FT MOD_RES 234
FT /note="N6-succinyllysine; alternate"
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 375
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT1"
SQ SEQUENCE 397 AA; 42131 MW; D1AFAAA509594E11 CRC64;
MALLRGVFIV AAKRTPFGAY GGLLKDFTPT DMAEFAARAA LSAGRVSPET VDSVVVGNVM
QSSSDAIYLA RHVGLRVGIP KETPAITINR LCGSGFQSIV SGCQEICSRD SEVVLCGGTE
SMSQAPYCVR NIRFGTKLGS ELKLEDTLWT GLTDTHVQMP MAITAENLAV KHQISREDCD
RYALQSQQRW KTANDAGYFD NEMAPVEVKT RKGKQTMQVD EHPRPQTTME QLNKLPPVFK
KEGTVTAGNA SGVSDGAGAV IIASEDAVKK HNFTPLARIV GYFVSGCDPT IMGIGPVPAI
SGALKKTGLS LKDMDLVEVN EAFAPQYLAV EKSLNLDPSK TNVNGGAIAL GHPLAGSGSR
ITAHLVHELR RRGGKYAVGS ACIGGGQGIA VIIENTA
