THIB_CANTR
ID THIB_CANTR Reviewed; 403 AA.
AC Q04677;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Acetyl-CoA acetyltransferase IB;
DE EC=2.3.1.9;
DE AltName: Full=Peroxisomal acetoacetyl-CoA thiolase;
DE AltName: Full=Thiolase IB;
GN Name=PACTB;
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; D13471; BAA02716.1; -; Genomic_DNA.
DR AlphaFoldDB; Q04677; -.
DR SMR; Q04677; -.
DR PRIDE; Q04677; -.
DR VEuPathDB; FungiDB:CTMYA2_016100; -.
DR VEuPathDB; FungiDB:CTRG_01584; -.
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 IB"
FT /id="PRO_0000206414"
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; 41930 MW; 42647747B663D47F CRC64;
MTLPPVYIVS TARTPIGSFQ GSLSSLTYSD LGAHAVKAAL AKVPQIKPQD VDEIVFGGVL
QANVGQAPAR QVALKAGLPD SIIASTINKV CASGMKAVII GAQNIICGTS DIVVVGGAES
MSNTPYYLPS ARSGARYGDA VMVDGVQKDG LLDVYEEKLM GVAAEKCAKD HGFSREDQDN
FAINSYKKAG KALSEGKFKS EIAPVTIKGF RGKPDTVIEN DEEIGKFNED RLKSARTVFQ
KENGTVTAPN ASKLNDGGAA LVLVSEAKLK QLGLKPLAKI SGWGEAARTP FDFTIAPALA
VPKAVKHAGL TVDRVDFFEL NEAFSVVGLA NAELVKIPLE KLNVYGGAVA MGHPLGCSGA
RIIVTLLSVL TQEGGRFGAA GVCNGGGGAS AIVIEKIDSD AKL
