ID A0A0S2JFG1_9GAMM Unreviewed; 394 AA.
AC A0A0S2JFG1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ALO34366.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:ALO34366.1};
GN ORFNames=CMT41_06180 {ECO:0000313|EMBL:ALO34366.1};
OS Colwellia sp. MT41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=58049 {ECO:0000313|EMBL:ALO34366.1, ECO:0000313|Proteomes:UP000065319};
RN [1] {ECO:0000313|EMBL:ALO34366.1, ECO:0000313|Proteomes:UP000065319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MT41 {ECO:0000313|EMBL:ALO34366.1,
RC ECO:0000313|Proteomes:UP000065319};
RA Kyaw T.S., Ugalde J., Peoples L., Narasingarao P., Chastain R.A.,
RA Yayanos A., Methe B.A., Bartlett D.H.;
RT "Distinctive Gene and Protein Characteristics of Extremely Piezophilic
RT Colwellia.";
RL Submitted (NOV-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}.
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DR EMBL; CP013145; ALO34366.1; -; Genomic_DNA.
DR RefSeq; WP_058026648.1; NZ_CP013145.1.
DR AlphaFoldDB; A0A0S2JFG1; -.
DR STRING; 58049.CMT41_06180; -.
DR KEGG; com:CMT41_06180; -.
DR OrthoDB; 8951704at2; -.
DR Proteomes; UP000065319; Chromosome.
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; -; 2.
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; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF144; ACYL-COA THIOLASE-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; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:ALO34366.1};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000065319};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ALO34366.1}.
FT DOMAIN 7..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..392
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 91
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 394 AA; 40730 MW; D1ADBEB4C41934B3 CRC64;
MSSSDPIVIV SAVRTPMGGF GGCFASVTAP DLGANAIKAA VAQANLAADQ IDEVIMGCVL
PAGLKQAPAR QAAIAADLSL STVCTTINKV CGSGMKAVMQ AHDALLAGSI DTAVAGGMES
MSNAPYILPK ARTGLRMGHG QVIDHMMQDG LENAYDGIAM GCFAQDTADE ANFTREAMDE
FAIRSLSRAN QAIESGAFKN EITAVTVKNR RSEVVIDTDE QPGNARPDKI PSLRAVFKKD
GTITAANSSS ISDGAAALVM MKLSEAKSRD LTPLCKIVAH ATHAQAPSEF TVAPVGAMSK
VLAKANWSTD DVDLFEINEA FAMVTMLAVK EMSLDINKVN IHGGACALGH PLGASGARIM
VTLIHALKNK GLSKGVASLC IGGGEATAIA LEML
//
