ID A0A0M9YWH4_9ACTN Unreviewed; 385 AA.
AC A0A0M9YWH4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KOU69689.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KOU69689.1};
GN ORFNames=ADK57_13105 {ECO:0000313|EMBL:KOU69689.1};
OS Streptomyces sp. MMG1533.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415546 {ECO:0000313|EMBL:KOU69689.1, ECO:0000313|Proteomes:UP000037741};
RN [1] {ECO:0000313|Proteomes:UP000037741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1533 {ECO:0000313|Proteomes:UP000037741};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOU69689.1}.
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DR EMBL; LGDG01000111; KOU69689.1; -; Genomic_DNA.
DR RefSeq; WP_053749597.1; NZ_LGDG01000111.1.
DR AlphaFoldDB; A0A0M9YWH4; -.
DR STRING; 1415546.ADK57_13105; -.
DR PATRIC; fig|1415546.3.peg.2856; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000037741; Unassembled WGS sequence.
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; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43365; BLR7806 PROTEIN; 1.
DR PANTHER; PTHR43365:SF1; STEROID 3-KETOACYL-COA THIOLASE FADA6; 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 ECO:0000313|EMBL:KOU69689.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037741};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KOU69689.1}.
FT DOMAIN 5..254
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 263..384
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 341
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 371
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 385 AA; 40542 MW; 29C047AABCD74450 CRC64;
MAEAYIVEAV RTPVGRRGGG LGGVHPADLG AHVLKELVAR CGVDPAAVED VVFGCLDTVG
PQAGDIARTC WLAAGLPEEV PGVTVDRQCG SSQQAVHFAA QGVLSGTQDL VVAGGVQNMS
QIPIAFATRQ AAEPLGFTEG PFAGSEGWRA RYGDRAVNQF VGAEMIAAKW GISRQDQEEF
ALRSHRRALR AIDEGRFERE IVPYGQAAVD EGPRRDTSLE KMAALKPVID GGTVTAACSS
QVSDGAAAML LASERAVHEH GLRPRARVHH LSVRGEDPIR MLTAPIPATA HALKKTGLSL
DDIDLVEINE AFAPVVLAWL KETGADPDKV NVNGGAIALG HPLGATGVKL MTTLLHELER
TGGRFGLQTM CEGGGQANVT IIERL
//