ID   THIL_THIVI              Reviewed;         394 AA.
AC   P45363;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Acetyl-CoA acetyltransferase;
DE            EC=2.3.1.9;
DE   AltName: Full=Acetoacetyl-CoA thiolase;
DE   AltName: Full=Beta-ketothiolase {ECO:0000303|PubMed:7763384};
GN   Name=phaA {ECO:0000303|PubMed:1476773};
GN   Synonyms=phbA {ECO:0000303|PubMed:7763384};
OS   Thiocystis violacea.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiocystis.
OX   NCBI_TaxID=13725;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC   STRAIN=2311 / DSM 208;
RX   PubMed=7763384; DOI=10.1007/bf00242944;
RA   Liebergesell M., Steinbuechel A.;
RT   "Cloning and molecular analysis of the poly(3-hydroxybutyric acid)
RT   biosynthetic genes of Thiocystis violacea.";
RL   Appl. Microbiol. Biotechnol. 38:493-501(1993).
RN   [2]
RP   GENE NAME.
RX   PubMed=1476773; DOI=10.1111/j.1574-6968.1992.tb05841.x;
RA   Steinbuechel A., Hustede E., Liebergesell M., Pieper U., Timm A.,
RA   Valentin H.;
RT   "Molecular basis for biosynthesis and accumulation of polyhydroxyalkanoic
RT   acids in bacteria.";
RL   FEMS Microbiol. Rev. 9:217-230(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: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
CC       biosynthesis. {ECO:0000269|PubMed:7763384}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC       biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P14611}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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; L01113; AAB02860.1; -; Genomic_DNA.
DR   EMBL; S54369; AAC60428.2; -; Genomic_DNA.
DR   PIR; B48376; B48376.
DR   AlphaFoldDB; P45363; -.
DR   SMR; P45363; -.
DR   UniPathway; UPA00058; UER00101.
DR   UniPathway; UPA00917; -.
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..394
FT                   /note="Acetyl-CoA acetyltransferase"
FT                   /id="PRO_0000206462"
FT   ACT_SITE        89
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        350
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT   ACT_SITE        380
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
SQ   SEQUENCE   394 AA;  40897 MW;  D51EAAE97F55E3F2 CRC64;
     MSDTIVIVDA GRTAIGTFGG ALSALQATDI GTTVLKALIE RTGIAPEQVS EVILGQVLTA
     GCGQNPARQT TLMAGLPHTV PAMTINKVCG SGLKAVHLAM QAVACGDAEI VIAGGQESMS
     QSSHVLPRSR EGQRMGDWPM KDTMIVDGLW DAFNQCHMGV TAENIAKKYA FTREAQDAFA
     AASQQKAEAA IQSGRFADEI IPVSIPQRKG DPLVFDTDEF PRPGTTAETL GRLRPAFDKQ
     GTVTAGNASG INDGAAMVVV MKESKAKELG LTPMARLVAF SSAGVDPAIM GTGPIPASTD
     CLKKAGWAPA DLDLVEANEA FAAQAMSVNQ EMGWDLSKVN VNGGAIAIGH PIGASGARVL
     VTLLYEMQKR DAKKGLATLC IGGGQGVALA VERL