ID A0A0M9GTY8_9BACI Unreviewed; 392 AA.
AC A0A0M9GTY8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00044137};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
DE AltName: Full=Acetoacetyl-CoA thiolase {ECO:0000256|ARBA:ARBA00030755};
GN ORFNames=AAV98_05960 {ECO:0000313|EMBL:KPB05823.1};
OS Bacillus sp. CHD6a.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1643452 {ECO:0000313|EMBL:KPB05823.1, ECO:0000313|Proteomes:UP000037908};
RN [1] {ECO:0000313|EMBL:KPB05823.1, ECO:0000313|Proteomes:UP000037908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHD6a {ECO:0000313|EMBL:KPB05823.1,
RC ECO:0000313|Proteomes:UP000037908};
RA Lin W., Liu Y., Zheng Q., Jiao N.;
RT "Genome sequence of Bacillus sp. CHD6a isolated from the shallow-sea
RT hydrothermal environment.";
RL Submitted (APR-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:KPB05823.1}.
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DR EMBL; LBMD01000003; KPB05823.1; -; Genomic_DNA.
DR RefSeq; WP_060664647.1; NZ_LBMD01000003.1.
DR AlphaFoldDB; A0A0M9GTY8; -.
DR STRING; 1643452.AAV98_05960; -.
DR PATRIC; fig|1643452.3.peg.3131; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000037908; 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; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_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; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 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.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:KPB05823.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KPB05823.1}.
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 88
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 392 AA; 41056 MW; CBA322BA2B7949DC CRC64;
MGKTVIVSGV RTPIGRFAGG LSTLSASDLG AVAIKEALNR ANLSGDQVGE VIMGTVLQGG
QGQLPSRQAS QKAGLPWEVR TETINKVCAS GMRSVTLGDI LIRSGEEEVI VAGGMESMSN
APYMLPKARW GLRMGDSTVQ DMMVHDGLTC TFTGVHMGTY GNSVAKEMEI SREDQDAWAF
RSHQRAIEAT EKGYFTDEIV PVSVPQRKGD PIVVSKDESP RKDTSIEKLA SLRPAFDHDG
TITAGNAPGV NDGASALVLM SEDRAVKEGK EVLATILGHA SIAVEAKDFP KTPGLVITEL
LKKTGTKLEE IDLFEINEAF AAVSLASANL AGLDLEKVNV NGGAVALGHP IGASGARIIV
SLIHELKRRG GGLGIASICS GGGQGDAMLI QV
//
