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Database: UniProt
Entry: A0A0M9ES02_FUSLA
LinkDB: A0A0M9ES02_FUSLA
Original site: A0A0M9ES02_FUSLA 
ID   A0A0M9ES02_FUSLA        Unreviewed;       421 AA.
AC   A0A0M9ES02;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE            EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN   ORFNames=FLAG1_08461 {ECO:0000313|EMBL:KPA38699.1};
OS   Fusarium langsethiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=179993 {ECO:0000313|EMBL:KPA38699.1, ECO:0000313|Proteomes:UP000037904};
RN   [1] {ECO:0000313|EMBL:KPA38699.1, ECO:0000313|Proteomes:UP000037904}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fl201059 {ECO:0000313|EMBL:KPA38699.1,
RC   ECO:0000313|Proteomes:UP000037904};
RA   Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA   Frandsen R.J., Nielsen K., Thrane U.;
RT   "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT   producer.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|ARBA:ARBA00001958};
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:KPA38699.1}.
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DR   EMBL; JXCE01000253; KPA38699.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M9ES02; -.
DR   OrthoDB; 5481312at2759; -.
DR   Proteomes; UP000037904; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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; 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:SF9; ACETYL-COA C-ACETYLTRANSFERASE; 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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000313|EMBL:KPA38699.1}; Potassium {ECO:0000256|ARBA:ARBA00022958};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037904};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KPA38699.1}.
FT   DOMAIN          19..276
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          284..392
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
SQ   SEQUENCE   421 AA;  44769 MW;  04F4F316FCE64D27 CRC64;
     MTTVSSVLRG LRTKSPNDVV VLSAVRSPIT RSFKGKFKDA WPEDILAPVM AEAPRRAGIR
     PQDVQDVLIG NVLAELGFAK TGRMALLHAG FPVSTTFHTV NRQCSSSLQA ITHMANSISA
     GIVDVAMAGG VESMSKNYTT RGVPIDVGPT LRATPVKSAA DCLMPMGITS ENVATRYGID
     RKAQDEFALL SHTRANDAQA EGRFTSEIVP IEYRIVADGD GQNATVRVEA DDTIRPGVTL
     EKLAKLKPAF IENGGSTAGN SSQISDGASA VILARRSWAE QRGLKPIARF LGTQVAGCEP
     DEMGIGPIHA IAQLYKYTGL SRQDIDIFEL NEAFASQTLA CIEQLGLDVA KVNPNGGAIA
     LGHPTGATGS RQLATLLAEL ARRDQELGVI SILYMSFADL VISFRLMFST GIGVAAAFAR
     E
//
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