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 27-MAR-2024, entry version 93.
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}.
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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 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 NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919:SF171; ACETYL-COA ACETYLTRANSFERASE, CYTOSOLIC; 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 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
//
