ID A0A1G7FWW7_9FLAO Unreviewed; 393 AA.
AC A0A1G7FWW7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=acetyl-CoA C-acetyltransferase {ECO:0000256|ARBA:ARBA00012705};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=SAMN05421636_107310 {ECO:0000313|EMBL:SDE80272.1};
OS Pricia antarctica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Pricia.
OX NCBI_TaxID=641691 {ECO:0000313|EMBL:SDE80272.1, ECO:0000313|Proteomes:UP000199109};
RN [1] {ECO:0000313|EMBL:SDE80272.1, ECO:0000313|Proteomes:UP000199109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23421 {ECO:0000313|EMBL:SDE80272.1,
RC ECO:0000313|Proteomes:UP000199109};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNAO01000007; SDE80272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7FWW7; -.
DR STRING; 641691.SAMN05421636_107310; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000199109; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; PTHR18919:SF171; ACETYL-COA ACETYLTRANSFERASE, CYTOSOLIC; 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.
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:UP000199109};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SDE80272.1}.
FT DOMAIN 4..260
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..390
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
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 393 AA; 41194 MW; 3B5D7B80229A97B8 CRC64;
MNEVVIVSVA RTPIGSFMGS LSTIPAPKLG AIAIKGALEK INLNPDLVDE VLMGNVVQAG
TGQAPARQAA LFAGLPNSVP CTTINKVCAS GMKAVTQAAQ AIALGDISIA VAGGMENMSL
IPHYIYLRNG QKFGPATLID GMQKDGLVDV YDQNAMGVCA DACASEHQFS RKDQDNYAIQ
SYKRSAEAWK NGKFDNEVVP VEVPQRRGEP VVVSEDEEFK NVKIDKIPDL RPAFSKDGTV
TAANASTIND GAAALVLMSA EKAKELNLEP LATIRGYADA AQEPKWFTTA PAKALPKAIA
KAGLQIKDID FFEFNEAFAV VGLANMKLLG LTDKNVNVNG GAVSLGHPLG CSGARILITL
LGVLQQNNAK IGAAAICNGG GGASAIIIER HNK
//
