ID A0A0A8X2Y9_9BACI Unreviewed; 391 AA.
AC A0A0A8X2Y9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=SAMD00020551_2489 {ECO:0000313|EMBL:GAM14340.1};
OS Mesobacillus selenatarsenatis SF-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=1321606 {ECO:0000313|EMBL:GAM14340.1, ECO:0000313|Proteomes:UP000031014};
RN [1] {ECO:0000313|EMBL:GAM14340.1, ECO:0000313|Proteomes:UP000031014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF-1 {ECO:0000313|EMBL:GAM14340.1,
RC ECO:0000313|Proteomes:UP000031014};
RA Kuroda M., Sei K., Yamashita M., Ike M.;
RT "Whole genome shotgun sequence of Bacillus selenatarsenatis SF-1.";
RL Submitted (JUN-2013) 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:GAM14340.1}.
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DR EMBL; BASE01000054; GAM14340.1; -; Genomic_DNA.
DR RefSeq; WP_041966098.1; NZ_BASE01000054.1.
DR AlphaFoldDB; A0A0A8X2Y9; -.
DR STRING; 1321606.SAMD00020551_2489; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000031014; 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:GAM14340.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031014};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:GAM14340.1}.
FT DOMAIN 5..260
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 268..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; 41411 MW; ADFD1D641478B9D7 CRC64;
MREAVIVAGA RTPVGKAKKG TLANVRPDDL GALVVRETLK RAGNYEGNID DLIIGCAMPE
AEQGLNMARN IGALAGLSHE VPAITINRYC SSGLQAIANA SERIMLGHTD TIIAGGAESM
SLVPMMGHVV RPNSKLAETA PQYYMGMGHT AEEVAKKYGI SREDQDAFAV RSHQRAAKAI
QEGKFEDEIV PVDVTLRTVG KDNKLVEKTI QFKQDEGVRP DTNMETLAKL RPAFNIKGTV
TAGNSSQTSD GAAAVMVMDR EKAESLGLKP LAKFRSFALG GVPPEIMGIG PVVAIPKALK
LAGLQVSDIG VFELNEAFAS QSIQVIRELG LDEDKVNVNG GAIALGHPLG TTGAKLTLTV
IHEMKRRNEQ FGVVTMCIGG GMGAAGVFEL L
//
