ID A0A0B0CVX8_9BACI Unreviewed; 274 AA.
AC A0A0B0CVX8;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KHE66858.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KHE66858.1};
DE Flags: Fragment;
GN ORFNames=LD39_20560 {ECO:0000313|EMBL:KHE66858.1};
OS Halobacillus sp. BBL2006.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=1543706 {ECO:0000313|EMBL:KHE66858.1, ECO:0000313|Proteomes:UP000030879};
RN [1] {ECO:0000313|EMBL:KHE66858.1, ECO:0000313|Proteomes:UP000030879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBL2006 {ECO:0000313|EMBL:KHE66858.1,
RC ECO:0000313|Proteomes:UP000030879};
RA Kirchner G., Treves D., Francis J.III.;
RT "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT BBL2006.";
RL Submitted (SEP-2014) 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:KHE66858.1}.
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DR EMBL; JRNX01000863; KHE66858.1; -; Genomic_DNA.
DR RefSeq; WP_035553100.1; NZ_JRNX01000863.1.
DR AlphaFoldDB; A0A0B0CVX8; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000030879; 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; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
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:SF2; 3-OXOADIPYL-COA_3-OXO-5,6-DEHYDROSUBERYL-COA THIOLASE; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
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:KHE66858.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030879};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KHE66858.1}.
FT DOMAIN 1..143
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 152..273
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KHE66858.1"
SQ SEQUENCE 274 AA; 29418 MW; 884D0E0E16728221 CRC64;
SMSRAPYLME RPERPYSPAP PKFKKSQLSP KEIGDPPMGI TAENLAEKYE IAREDQDRFA
QQSQERMAAA MEEGRFEEQI VPLTIPVRKG EPVVFKTDEH PRPQSTLEGM AKLRPAFLED
GSVTAGNSSG LNDAASALTL MSRAKAEEIG VTPMATVKAC TVAGVDPNIM GIGPVPATQK
VLEKTGLSLE DMDIIEINEA FAAQVLACNK EMQMNMEKVN VNGGAIAHGH PLGATGAILT
TKAIYELQRI GGRYALVTAC IGGGQGIAIV IERE
//
