ID A0A2A8S875_9BACI Unreviewed; 393 AA.
AC A0A2A8S875;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=CN326_16370 {ECO:0000313|EMBL:PEZ04267.1};
OS Bacillus sp. AFS018417.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033491 {ECO:0000313|EMBL:PEZ04267.1, ECO:0000313|Proteomes:UP000220085};
RN [1] {ECO:0000313|EMBL:PEZ04267.1, ECO:0000313|Proteomes:UP000220085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS018417 {ECO:0000313|EMBL:PEZ04267.1,
RC ECO:0000313|Proteomes:UP000220085};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-2017) 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:PEZ04267.1}.
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DR EMBL; NTTM01000041; PEZ04267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A8S875; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000220085; 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:PEZ04267.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000220085};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:PEZ04267.1}.
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 393 AA; 41160 MW; D7A7383DCE084F0B CRC64;
MTRTVILSAA RTPVGKFGGA LKDVKATELG GIAIGAALER ANVAASDIEE VIFGAVIQGG
QGQIPSRQAA REAGIPWETR TETVNKVCAS GLRAVTLADQ IIRTGDQSLL VAGGMESMSN
SPYILRGARW GYRMGHNEVV DLNVADGLTC SFSGVHMGVY GGDVAKEDGI SREMQDEWAC
RSHMRAVASR KEGRFEEEIV PVSVPQRKGE PVVVAHDEAP REDTTVEKLA KLKPVFDKDA
AVTAGNAPGL NDGAAALVLM SEERAKQEGR KPLATILGHT AIAVEAKDFP RTPGYAINEL
LKKTGKKVEE IDLFEINEAF AAVAIASANI AGIDPEKINV NGGAVAMGHP IGASGARIIV
TLIHALKQRG GGIGIASICS GGGQGDAIMI EVQ
//
