ID   THIL_PARDE              Reviewed;         391 AA.
AC   P54810;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Acetyl-CoA acetyltransferase;
DE            EC=2.3.1.9;
DE   AltName: Full=Acetoacetyl-CoA thiolase;
GN   Name=phaA;
OS   Paracoccus denitrificans.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=266;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8566717; DOI=10.1111/j.1574-6968.1995.tb07865.x;
RA   Yabutani T., Maehara A., Ueda S., Yamane T.;
RT   "Analysis of beta-ketothiolase and acetoacetyl-CoA reductase genes of a
RT   methylotrophic bacterium, Paracoccus denitrificans, and their expression in
RT   Escherichia coli.";
RL   FEMS Microbiol. Lett. 133:85-90(1995).
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: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
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DR   EMBL; D49362; BAA08357.1; -; Genomic_DNA.
DR   AlphaFoldDB; P54810; -.
DR   SMR; P54810; -.
DR   UniPathway; UPA00058; UER00101.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042619; P:poly-hydroxybutyrate biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
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   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; PHB biosynthesis; Transferase.
FT   CHAIN           1..391
FT                   /note="Acetyl-CoA acetyltransferase"
FT                   /id="PRO_0000206460"
FT   ACT_SITE        88
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        347
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT   ACT_SITE        377
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
SQ   SEQUENCE   391 AA;  40745 MW;  A6278FD632EC697B CRC64;
     MTKAVIVSAA RTPVGSFLGS FANLPAHELG AIVLKAVVER AGIDPSEVSE TILGQVLTAA
     QGQNPARQAH IKVGLPRESA AWVINQVCGS GLRTVALAAQ QVLLGDARIV VAGGQESMSL
     APHAAYIAPG QKMGDMKMLD TMIKDGLWDA FNDYHMGTTA ENVAGKWEIS RAEQDQFAVA
     SQNKAEAAQK AGKFADEIVP VTIKSRKGET VVDADEYIRH GATLEAMENV RPAFSKEGTV
     TAGNASGLND GAAAVLVMTE DEAARRGLTP LARIASYATA GVDPQIMGTG PIPASRKALE
     KAGWSVGDLD LVEANEAFAA QAIAVNRDMG WDPSIVNVNG GAIAIGHPIG ASGCRILNTL
     LFEMQRRDAK KGLATLCIGG GMGVALCLER P