ID   A0A158JBU7_9BURK        Unreviewed;       392 AA.
AC   A0A158JBU7;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:SAL65780.1};
GN   ORFNames=AWB68_03648 {ECO:0000313|EMBL:SAL65780.1};
OS   Caballeronia choica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=326476 {ECO:0000313|EMBL:SAL65780.1, ECO:0000313|Proteomes:UP000054770};
RN   [1] {ECO:0000313|Proteomes:UP000054770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Peeters C.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR   EMBL; FCON02000038; SAL65780.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158JBU7; -.
DR   OrthoDB; 8951704at2; -.
DR   Proteomes; UP000054770; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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; IPR020617; Thiolase_C.
DR   InterPro; IPR020613; Thiolase_CS.
DR   InterPro; IPR020616; Thiolase_N.
DR   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR   PANTHER; PTHR43853:SF22; ACETYL-COA ACETYLTRANSFERASE; 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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SAL65780.1}.
FT   DOMAIN          5..261
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          270..390
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        90
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        348
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        378
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   392 AA;  40932 MW;  DEA56061BA41C1D2 CRC64;
     MTDAVIVSTA RTGLAKSWRG ALNMTHGATL GGHVTKAAVE RAGIDPARVE DVIMGCANPE
     GATGANIARQ IALRGGLPVT VPGMTVNRFC SSGLQTIALA AQRVIAGEGD VYVAGGVESI
     SCVQNEMNRH MIADGWLTEH KPEIYWSMLQ TAENVAKRYE ISKERQDEYG VQSQQRAAAG
     QAAGRFDAEI VPITVLAGVA EKASGRLFTK EVALSSDEGI RADTTLEGVS KIRTAMPGGV
     VTAGNASQFS DGASACVVMN ASVAEKEGLQ PLGIFRGFAV AGCEPDEMGI GPVFAVPKLL
     KQAGLKVEDI DLWELNEAFA VQVLYCRDKL GIPNERLNVN GGAIAVGHPY GVSGARLTGH
     ALIEGKRRGA KFVVVTMCIG GGQGAAGLFE VV
//