THIL_PIG
ID THIL_PIG Reviewed; 26 AA.
AC P14610;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Acetyl-CoA acetyltransferase;
DE EC=2.3.1.9;
DE AltName: Full=Acetoacetyl-CoA thiolase;
DE Flags: Fragment;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Heart;
RX PubMed=5477295; DOI=10.1111/j.1432-1033.1970.tb01108.x;
RA Gehring U., Harris J.I.;
RT "The active site cysteines of thiolase.";
RL Eur. J. Biochem. 16:492-498(1970).
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 -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- PTM: Succinylation, adjacent to a coenzyme A binding site.
CC Desuccinylated by SIRT5 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P14610; -.
DR SMR; P14610; -.
DR PeptideAtlas; P14610; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
PE 1: Evidence at protein level;
KW Acyltransferase; Direct protein sequencing; Mitochondrion;
KW Reference proteome; Transferase.
FT CHAIN <1..>26
FT /note="Acetyl-CoA acetyltransferase"
FT /id="PRO_0000206408"
FT ACT_SITE 21
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 26
SQ SEQUENCE 26 AA; 2561 MW; 7A4D306BC9BE35CE CRC64;
QAVLGAGLPC NTTTSPIIKV CASGMK