ID A0A2C9SYZ7_9MYCO Unreviewed; 450 AA.
AC A0A2C9SYZ7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:GAY16420.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:GAY16420.1};
GN ORFNames=MSZK_31460 {ECO:0000313|EMBL:GAY16420.1};
OS Mycobacterium sp. shizuoka-1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=2039281 {ECO:0000313|EMBL:GAY16420.1, ECO:0000313|Proteomes:UP000223528};
RN [1] {ECO:0000313|EMBL:GAY16420.1, ECO:0000313|Proteomes:UP000223528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=shizuoka-1 {ECO:0000313|Proteomes:UP000223528};
RA Yoshida M., Izumiyama S., Fukano H., Sugiyama K., Suzuki M., Shibayama K.,
RA Hoshino Y.;
RT "Draft genome sequence of Mycobacterium sp. shizuoka-1.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {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:GAY16420.1}.
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DR EMBL; BEWG01000054; GAY16420.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9SYZ7; -.
DR Proteomes; UP000223528; 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; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:GAY16420.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000223528};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:GAY16420.1}.
FT DOMAIN 27..295
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 303..449
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 111
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 402
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 437
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 450 AA; 47165 MW; D6E3586950C94F7A CRC64;
MGWVYPHQTE LTAEIDVAST SANSRRVAVI GGNRIPFARS DGAYAEASNQ DMFTAALAGL
VDRFGLAGER LGAVIGGAVL KHSRDFNLMR ESVLGSQLSP YTPAIDLQQA CGTGLQAAIA
AADGIAAGRY EVAAAGGVDT TSDAPIGLGD ELRRTLLGLR RAKSNVGRLK LVGKLPASLG
IEIPTNGEPR TGLSMGEHAA ITAKKMGIKR VDQDELAAAS HRNMAAAYDR GFFDDLVTPF
LGLYRDNNLR ADSSAEKLAT LKPVFGVRNG DATMTAGNST PLTDGASVAL LASEEWARSH
SLEPLAYFVD SETAAVDYVN GADGLLMAPT YAVPRLLARN GLTLQDFDFY EIHEAFASVV
LAHLQAWESE EYCKERLGLD AALGAIDRSK LNVNGSSLAA GHPFAATGGR IVAQLAKQLA
EQKKATGQPV RGLISICAAG GQGVTAILEA
//
