ID A0A1E5LGN9_9BACI Unreviewed; 392 AA.
AC A0A1E5LGN9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, 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=BFG57_12585 {ECO:0000313|EMBL:OEH93234.1};
OS Bacillus solimangrovi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1305675 {ECO:0000313|EMBL:OEH93234.1, ECO:0000313|Proteomes:UP000095209};
RN [1] {ECO:0000313|EMBL:OEH93234.1, ECO:0000313|Proteomes:UP000095209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GH2-4 {ECO:0000313|EMBL:OEH93234.1,
RC ECO:0000313|Proteomes:UP000095209};
RA Lim S., Kim B.-C.;
RT "Genome of Bacillus solimangrovi GH2-4.";
RL Submitted (AUG-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}.
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:OEH93234.1}.
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DR EMBL; MJEH01000014; OEH93234.1; -; Genomic_DNA.
DR RefSeq; WP_069716699.1; NZ_MJEH01000014.1.
DR AlphaFoldDB; A0A1E5LGN9; -.
DR STRING; 1305675.BFG57_12585; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000095209; Unassembled WGS sequence.
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; -; 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 Reference proteome {ECO:0000313|Proteomes:UP000095209};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:OEH93234.1}.
FT DOMAIN 5..263
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 272..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; 41009 MW; 689F52836F460847 CRC64;
MTRTVIVGGA RTPFGKFGGS LSSLTASQLG GIAIKEALKR AGVDAANVGE VLMGNVLQAG
QGQIPSRQAS RYADIPWEVQ TETINKVCAS GMRSVTLADQ IIRVGDEDVI VAGGMESMSN
APYMLPKARW GMRMGDQKVI DAMVHDGLTC SFKGVHMGTY GNSTAKEFEL TREQQDEWAN
RSHQRALAAI EEGKFADEIV PVDVPQRKGD AVTIDTDEAP RVGTTTEKLS KLSPVFGEDG
TITAGNAPGV NDGAGALVLM SEERASKEGK EVMATIIGHT ALAVEAHRFP ETPGLVINKL
LNKTGKSVED IELFEVNEAF AAVALASGKI AGLNPDKVNV NGGAVALGHP IGASGTRIIL
TLIHELKRRG GGIGIAAICS GGGQGDAIMI QV
//
