ID A0A150L9C9_9BACI Unreviewed; 391 AA.
AC A0A150L9C9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=B4102_1857 {ECO:0000313|EMBL:KYD08850.1};
OS Heyndrickxia sporothermodurans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX NCBI_TaxID=46224 {ECO:0000313|EMBL:KYD08850.1, ECO:0000313|Proteomes:UP000075666};
RN [1] {ECO:0000313|EMBL:KYD08850.1, ECO:0000313|Proteomes:UP000075666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4102 {ECO:0000313|EMBL:KYD08850.1,
RC ECO:0000313|Proteomes:UP000075666};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Genome Sequences of Twelve Sporeforming Bacillus Species Isolated from
RT Foods.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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:KYD08850.1}.
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DR EMBL; LQYN01000028; KYD08850.1; -; Genomic_DNA.
DR RefSeq; WP_066229242.1; NZ_NAZD01000150.1.
DR AlphaFoldDB; A0A150L9C9; -.
DR STRING; 46224.B4102_1857; -.
DR PATRIC; fig|46224.3.peg.2013; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000075666; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 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; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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:KYD08850.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075666};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KYD08850.1}.
FT DOMAIN 5..260
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..389
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 391 AA; 40827 MW; 07815203BAB35850 CRC64;
MREAVIVAGA RTPVGKASKG TLANVRPDDL GALVVKETLK RAGNYEGNID DLIIGCAMPE
AEQGLNMARN IGALAGLPNT VPAVTVNRYC SSGLQSIAYG AERIMLGSSD TVLAGGAESM
SLVPMMGHVV RPNATLAETA PEYYMGMGHT AEQVAQKFGV SREDQDAFAV RSHQKAAKAI
AEGKFADEIV PVDVTLRSVG ADNKLVEKHV VFSKDEGVRP ESSVEVLGKL RPAFNLKGSV
TAGNSSQTSD GAAAVLLMDR EKAVSHGLAP MAKFRSFAVA GVPPEIMGIG PVEAIPRALK
IAGLELADIG LFELNEAFAS QSIQVIRQLG LDEEIVNVNG GAIALGHPLG CTGTKLTLSL
IHEMKRRNVQ FGVVTMCIGG GMGAAGVFEL I
//
