ID A4C682_9GAMM Unreviewed; 435 AA.
AC A4C682;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EAR29486.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:EAR29486.1};
GN ORFNames=PTD2_11739 {ECO:0000313|EMBL:EAR29486.1};
OS Pseudoalteromonas tunicata D2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=87626 {ECO:0000313|EMBL:EAR29486.1, ECO:0000313|Proteomes:UP000006201};
RN [1] {ECO:0000313|EMBL:EAR29486.1, ECO:0000313|Proteomes:UP000006201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D2 {ECO:0000313|EMBL:EAR29486.1,
RC ECO:0000313|Proteomes:UP000006201};
RA Moran M.A., Kjelleberg S., Egan S., Saunders N., Thomas T., Ferriera S.,
RA Johnson J., Kravitz S., Halpern A., Remington K., Beeson K., Tran B.,
RA Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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:EAR29486.1}.
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DR EMBL; AAOH01000002; EAR29486.1; -; Genomic_DNA.
DR RefSeq; WP_009837360.1; NZ_AAOH01000002.1.
DR AlphaFoldDB; A4C682; -.
DR STRING; 87626.PTD2_11739; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_0_6; -.
DR OrthoDB; 8951704at2; -.
DR Proteomes; UP000006201; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR012806; Ac-CoA_C-AcTrfase_FadI.
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 NCBIfam; TIGR02446; FadI; 1.
DR PANTHER; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003557}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EAR29486.1}.
FT DOMAIN 15..288
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 297..433
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 99
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 391
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 421
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 435 AA; 46478 MW; A14ED323BD1DF4DF CRC64;
MSEQIKLRTA QGDRIAIVSG LRTPFAKQAT YFHHVSALDL GKLVVNEMLE RLNFDRNEID
QLVFGQVVQM PEAPNIAREI VLGTGMPVSV DAYSVSRACA TSFQAIANVT ESIMAGSVNV
AVAGGADSSS VLPIGVSKKL AGSLVDLTKA RTFGDKLKIF SKLRLKDLLP VPPAVAEYST
GLSMGQTAEQ MAKTHSISRA DQDALAHRSH TLASKAWQDG YFKEEVMTAH VAPYKTFLEQ
DNNIRHNSTL EGYAKLRPVF DRQHGSVTAA NATPLTDGAA AVLMMSESKA KALGYPILGY
IRSFAFSAIG VHDDMLMGPA HSTPIALRRA GIELADLDLI EMHEAFAAQT LANMKMFESE
KFAKEIGLSK AIGSIDMAKF NVNGGSLAYG HPFAATGARL ITQSLHELKR RGGGLALTTA
CAAGGLGAAF VLEVE
//
