ID A0A1B8W3F1_9BACI Unreviewed; 404 AA.
AC A0A1B8W3F1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=A7975_19515 {ECO:0000313|EMBL:OBZ11157.1};
OS Bacillus sp. FJAT-26390.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1743142 {ECO:0000313|EMBL:OBZ11157.1, ECO:0000313|Proteomes:UP000092623};
RN [1] {ECO:0000313|EMBL:OBZ11157.1, ECO:0000313|Proteomes:UP000092623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-26390 {ECO:0000313|EMBL:OBZ11157.1,
RC ECO:0000313|Proteomes:UP000092623};
RA Liu X., Pan Z., Shi H., Ge C., Che J., Lan J., Chen Z., Chen Q., Liu B.,
RA Zhu Y., Wang J., Liu G.;
RT "Bacillus sp. FJAT-26390.";
RL Submitted (MAY-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:OBZ11157.1}.
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DR EMBL; MAQX01000032; OBZ11157.1; -; Genomic_DNA.
DR RefSeq; WP_065386643.1; NZ_MAQX01000032.1.
DR AlphaFoldDB; A0A1B8W3F1; -.
DR Proteomes; UP000092623; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; -; 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 Reference proteome {ECO:0000313|Proteomes:UP000092623};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:OBZ11157.1}.
FT DOMAIN 15..271
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 280..400
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 101
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 358
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 404 AA; 41875 MW; B4A8099AD7B98253 CRC64;
MSASSPFEDH DRDAVIVAAV RTAVGKASKG SLAETRAEDL GRAVLQGALA RVPALSPELV
EDVIIGCAMP EGEQGLNMAR TISLYAGLPV TTPAVTINRF CASGLQAIAY AAERIRLGDA
DIIAAGGVES MSHVPMTGFK LSPHPAIVDT RPEVYMGMGH TAEEVARRYG VTREAQDAFA
SSSHRKAAAA IEAGRFQAEI VPITTSRSGV NDAGRPWSKV IQFDTDEGVR PETTVQTLAP
LKPSFAREGT VTAGNTSQMS DGAAAVIVMS RARAAELGLR PLAVFRSYSV AGVAPEVMGI
GPIEAVPKAL RKAGITLEQV DLFELNEAFA AQCVPIIREL GINPEIVNVN GGAIALGHPL
GCTGTKLTVS LIHELGRRGG GIGVVTMCVG GGMGAAGIIE VYGS
//
