ID A0A0J1JIS8_9GAMM Unreviewed; 415 AA.
AC A0A0J1JIS8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KLV01927.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KLV01927.1};
GN ORFNames=ABT58_05865 {ECO:0000313|EMBL:KLV01927.1};
OS Photobacterium aphoticum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=754436 {ECO:0000313|EMBL:KLV01927.1, ECO:0000313|Proteomes:UP000036426};
RN [1] {ECO:0000313|EMBL:KLV01927.1, ECO:0000313|Proteomes:UP000036426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25995 {ECO:0000313|EMBL:KLV01927.1,
RC ECO:0000313|Proteomes:UP000036426};
RA Machado H., Gram L.;
RT "Photobacterium galathea sp. nov.";
RL Submitted (MAY-2015) 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:KLV01927.1}.
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DR EMBL; LDOV01000010; KLV01927.1; -; Genomic_DNA.
DR RefSeq; WP_047873380.1; NZ_PYMF01000001.1.
DR AlphaFoldDB; A0A0J1JIS8; -.
DR PATRIC; fig|754436.4.peg.1245; -.
DR OrthoDB; 8951704at2; -.
DR Proteomes; UP000036426; Unassembled WGS sequence.
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; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919:SF138; ACETYL-COA C-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:KLV01927.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036426};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KLV01927.1}.
FT DOMAIN 5..270
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 279..407
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 98
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 357
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 395
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 415 AA; 43419 MW; 8617E6E1D498D67C CRC64;
MRKEVWVIAA NRTPIGSFLG ELSSLTAPQL GSQAIAGCFN VFNVPSAGDT ATFSPDDIGE
VFMGNVLSAG CGQAPARQAA LGAKLPESVP CTTINKVCGS GMKAVMMGVD SIIAGTQTAV
VSGGMESMTN APHLQTQARS GQRLGNAVLH DHMFIDGLLD AYEGNLMGVY AQQIADEKGY
SREAMDDWAI QSVKRAQQAQ AQDWFHDEIS SVCVSHRHDT LNIAQDEHPQ EVDTQKISRL
KPAFSADGTV TAANSSAISD GAAALVLVDA DMAKAKGLQP LAIIRSHASH ARAPSEFTIA
PVFAIQTLLS QLDWSADSVD LWEINEAFAV VTQIAVDALA LDAEKVNVCG GACALGHPIG
ASGARIIVTL IHQLRRLQQQ SSQSSLPLRG IAACCIGGGE ATAIAIEVPV GTVPQ
//