ID A0A0Q3WWM8_9BACI Unreviewed; 391 AA.
AC A0A0Q3WWM8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-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=AN964_06380 {ECO:0000313|EMBL:KQL53170.1};
OS Heyndrickxia shackletonii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX NCBI_TaxID=157838 {ECO:0000313|EMBL:KQL53170.1, ECO:0000313|Proteomes:UP000051888};
RN [1] {ECO:0000313|EMBL:KQL53170.1, ECO:0000313|Proteomes:UP000051888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 18435 {ECO:0000313|EMBL:KQL53170.1,
RC ECO:0000313|Proteomes:UP000051888};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (SEP-2015) 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:KQL53170.1}.
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DR EMBL; LJJC01000004; KQL53170.1; -; Genomic_DNA.
DR RefSeq; WP_055738898.1; NZ_LJJC01000004.1.
DR AlphaFoldDB; A0A0Q3WWM8; -.
DR STRING; 157838.AN964_06380; -.
DR PATRIC; fig|157838.3.peg.1429; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000051888; 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:KQL53170.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051888};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KQL53170.1}.
FT DOMAIN 5..259
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; 41010 MW; 55B2B24DF9CEF633 CRC64;
MREAVIVAGA RTPVGKANKG TLANVRPDDL GALVVKETLK RAGNYEGNID DLIIGCAMPE
AEQGLNMARN IGALAGLPDT VPAVTINRYC SSGLQAIAYG AERIMLGSSD TILAGGAESM
SLVPMMGHVV RPNATLAETA PQYYMGMGHT AEQVATKFGV SREDQDAFAV RSHQKAAKAI
EEGKFKDEIV PVDVTLRSVD SKNKLVENKI LFTNDEGVRP ESTVEVLGKL RPAFSVTGSV
TAGNSSQTSD GAAAVLLMDG EKAKSLGYQP MAKFRSFAVA GVPPEIMGIG PVEAIPKALK
IAGLELSDIG LFELNEAFAS QSIQVIRKLG LNEEIVNVNG GAIALGHPLG CTGTKLTLSL
IHEMKRRNVQ FGVVTMCIGG GMGAAGVFEL M
//
