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Database: UniProt
Entry: A0A2S0MCE4_9BURK
LinkDB: A0A2S0MCE4_9BURK
Original site: A0A2S0MCE4_9BURK 
ID   A0A2S0MCE4_9BURK        Unreviewed;       393 AA.
AC   A0A2S0MCE4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Acetyl-CoA C-acyltransferase {ECO:0000313|EMBL:AVO33562.1};
DE            EC=2.3.1.9 {ECO:0000313|EMBL:AVO33562.1};
GN   ORFNames=C6570_04310 {ECO:0000313|EMBL:AVO33562.1};
OS   Ottowia oryzae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ottowia.
OX   NCBI_TaxID=2109914 {ECO:0000313|EMBL:AVO33562.1, ECO:0000313|Proteomes:UP000239709};
RN   [1] {ECO:0000313|EMBL:AVO33562.1, ECO:0000313|Proteomes:UP000239709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KADR8-3 {ECO:0000313|EMBL:AVO33562.1,
RC   ECO:0000313|Proteomes:UP000239709};
RA   Kim S.-J., Heo J., Kwon S.-W.;
RT   "Genome sequencing of Ottowia sp.";
RL   Submitted (MAR-2018) 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; CP027666; AVO33562.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S0MCE4; -.
DR   KEGG; otk:C6570_04310; -.
DR   OrthoDB; 9764638at2; -.
DR   Proteomes; UP000239709; Chromosome.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020610; Thiolase_AS.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020616; Thiolase_N.
DR   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   PANTHER; PTHR18919:SF138; ACETYL-COA C-ACETYLTRANSFERASE; 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; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000313|EMBL:AVO33562.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239709};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AVO33562.1}.
FT   DOMAIN          5..263
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          271..391
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        89
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        349
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        379
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   393 AA;  40975 MW;  399B100B59CBED96 CRC64;
     MSDPIVIVSA ARTPMGAFQG DFANLAAHDL GGVAIKAAVE RAGIAPELVT EVLFGNCLLA
     GQGQAPARQA AFKGGLAKSA GAVTLSKMCG SGMRAAMFAH DMLVAGSHDV LVAGGMESMT
     GAPYLLQKAR GGYRLGHDRI FDHMMLDGLE DAYEPGRSMG TFGEDCAAKY HFTREQQDNF
     AVASVQRAQA ATNNGAFKDE IAPVTVKDRK GERVVSTDEG PGKINVDKIP TLKPAFKKDG
     TVTAASSSSI NDGAAAMVLM RESTAQKLGV QPLARIVSHA THAQEPEWFS TAPIGATEKA
     LAKAGWQVGD VDLWEINEAF AVVPMALMHD LKVPHDKVNV NGGACALGHP IGASGARILV
     TLLYALKNRG LKKGLATLCI GGGEATAMAV ELL
//
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