ID   A0A1A9BGS3_9ACTN        Unreviewed;       420 AA.
AC   A0A1A9BGS3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Acetyl-CoA C-acetyltransferase {ECO:0000313|EMBL:SBT68715.1};
GN   ORFNames=GA0070622_5825 {ECO:0000313|EMBL:SBT68715.1};
OS   Micromonospora sediminicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=946078 {ECO:0000313|EMBL:SBT68715.1, ECO:0000313|Proteomes:UP000199558};
RN   [1] {ECO:0000313|EMBL:SBT68715.1, ECO:0000313|Proteomes:UP000199558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45794 {ECO:0000313|EMBL:SBT68715.1,
RC   ECO:0000313|Proteomes:UP000199558};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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; FLRH01000004; SBT68715.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A9BGS3; -.
DR   STRING; 946078.GA0070622_5825; -.
DR   OrthoDB; 9764638at2; -.
DR   Proteomes; UP000199558; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 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:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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; PS00737; THIOLASE_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SBT68715.1}.
FT   DOMAIN          10..288
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          296..418
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        95
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        375
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        405
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   420 AA;  44154 MW;  DA98ACAB37683A6C CRC64;
     MPIESPRDAV IVATARSPIG RAFKGSLREV RPDDLAATIV QAALDKVPGL DPTTIDDLYL
     GCGLPGGEQG FNMARVVSTL LGLDGLPGAT LTRYCASSLQ TTRMAMHAIR AGEGDVFVSA
     GVEMVSRYAR GNSDTLPPEA QALVGGGWEN PRFAEARERS QARTQAGAEV WTDPREAGQL
     PDIYLTMGQT AENLAQVYDV TREDMDAFGV RSQNLAEKAI ADGFWAREIT PVTTPDGTVV
     GTDDGPRPGV TLEAVSGLKP VFRPDGRITA GNCCPLNDGA AAVVIMSAER ASELGLTPLA
     RIVSTGVTAL SPEIMGLGPV EASKQALRRA GMTIDDVDLV EINEAFAAQV IPSYRQLGIP
     EEKLNVMGGA IAVGHPFGMT GARITGTLLN ALEWHDKTIG LETMCVGGGQ GMAMVLERLG
//