ID   THIA_CANTR              Reviewed;         403 AA.
AC   Q12598;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Acetyl-CoA acetyltransferase IA;
DE            EC=2.3.1.9;
DE   AltName: Full=Peroxisomal acetoacetyl-CoA thiolase;
DE   AltName: Full=Thiolase IA;
GN   Name=PACTA;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-17; 209-233
RP   AND 280-290.
RC   STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX   PubMed=1362382; DOI=10.1111/j.1432-1033.1992.tb17505.x;
RA   Kurihara T., Ueda M., Kanayama N., Kondo J., Teranishi Y., Tanaka A.;
RT   "Peroxisomal acetoacetyl-CoA thiolase of an n-alkane-utilizing yeast,
RT   Candida tropicalis.";
RL   Eur. J. Biochem. 210:999-1005(1992).
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   -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC       biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
CC   -!- SUBUNIT: Multimeric. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D13470; BAA02715.1; -; Genomic_DNA.
DR   PIR; S28144; S28144.
DR   AlphaFoldDB; Q12598; -.
DR   SMR; Q12598; -.
DR   VEuPathDB; FungiDB:CTMYA2_016100; -.
DR   VEuPathDB; FungiDB:CTRG_01584; -.
DR   BRENDA; 2.3.1.9; 1146.
DR   SABIO-RK; Q12598; -.
DR   UniPathway; UPA00058; UER00101.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006696; P:ergosterol biosynthetic process; IEA:EnsemblFungi.
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   1: Evidence at protein level;
KW   Acyltransferase; Direct protein sequencing; Peroxisome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1362382"
FT   CHAIN           2..403
FT                   /note="Acetyl-CoA acetyltransferase IA"
FT                   /id="PRO_0000206413"
FT   MOTIF           401..403
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        91
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        353
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT   ACT_SITE        383
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
SQ   SEQUENCE   403 AA;  41898 MW;  63800913AF4E7873 CRC64;
     MALPPVYIVS TARTPIGSFQ GSLSSLTYSD LGAHAVKAAL AKVPQIKPQD VDEIVFGGVL
     QANVGQAPAR QVALKAGLPD SIVASTINKV CASGMKAVII GAQNIICGTS DIVVVGGAES
     MSNTPYYLPS ARSGARYGDA IMVDGVQKDG LLDVYEEKLM GVAAEKCAKD HGFSREDQDN
     FAINSYKKAG KALSEGKFKS EIAPVTIKGF RGKPDTVIEN DEEIGKFNEE RLKSARTVFQ
     KENGTVTAPN ASKLNDGGAA LVLVSEAKLK QLGLKPLAKI SGWGEAARTP FDFTIAPALA
     VPKAVKHAGL TVDRVDFFEL NEAFSVVGLA NAELVNIPLE KLNVYGGAVA MGHPLGCSGA
     RIIVTLLSVL TQEGGRFGVA GVCNGGGGAS AVVIEKIDAD AKL