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Database: UniProt
Entry: A0A317WPF9_9EURO
LinkDB: A0A317WPF9_9EURO
Original site: A0A317WPF9_9EURO 
ID   A0A317WPF9_9EURO        Unreviewed;       697 AA.
AC   A0A317WPF9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Acetoacetyl-CoA synthase {ECO:0000313|EMBL:PWY88319.1};
GN   ORFNames=BO70DRAFT_309955 {ECO:0000313|EMBL:PWY88319.1};
OS   Aspergillus heteromorphus CBS 117.55.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY88319.1, ECO:0000313|Proteomes:UP000247233};
RN   [1] {ECO:0000313|EMBL:PWY88319.1, ECO:0000313|Proteomes:UP000247233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY88319.1,
RC   ECO:0000313|Proteomes:UP000247233};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:PWY88319.1}.
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DR   EMBL; MSFL01000005; PWY88319.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317WPF9; -.
DR   STRING; 1448321.A0A317WPF9; -.
DR   VEuPathDB; FungiDB:BO70DRAFT_309955; -.
DR   OrthoDB; 45466at2759; -.
DR   Proteomes; UP000247233; Unassembled WGS sequence.
DR   GO; GO:0030729; F:acetoacetate-CoA ligase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR005914; Acac_CoA_synth.
DR   InterPro; IPR032387; ACAS_N.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   NCBIfam; TIGR01217; ac_ac_CoA_syn; 1.
DR   PANTHER; PTHR42921:SF4; ACETOACETYL-COA SYNTHASE (AFU_ORTHOLOGUE AFUA_8G04770); 1.
DR   PANTHER; PTHR42921; ACETOACETYL-COA SYNTHETASE; 1.
DR   Pfam; PF16177; ACAS_N; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000247233}.
FT   DOMAIN          41..97
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          120..501
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
SQ   SEQUENCE   697 AA;  77307 MW;  274F885DB798F0B7 CRC64;
     MATHPTPRKL WDHPNPNATA MARFKRRLEA TKDVTLPDFY SLYQWSTTHR AAFWDFCWKY
     FPIIHDGTYT HVVDESARID SNPDWFPGIR LNFAENVLFS RGDSDAAALT TVGKEDGKIA
     VTEVREGAIE PPVDLTWKEL RQRTGRLVQA LKAAGLQRGD RVAAVAGNGI DTLVVFLATT
     ALGGIFTSTS TDTGITGILD RLRQTKPVWV FMDDVTVYNG KTVDLTPKFV NVVEGLSQFQ
     EFKGVVALPR FRDRPADVTH LPRTQTLAKF LATATSDRLE FVRLGFRDPF LIVYSSGTTG
     EPKCIVHSVG GVVLNMYKEG RLHRDMDSEA VLLQYTTTGW IMYLSCISVL LIGAKSILYD
     GSPFLPDIAI LVRLLEKHGV THFGTSPRWM QEIRKSQISP RQIADLHRLK AVVSTGMVLS
     ESLYEWFYDE AFPPRTQLAN ISGGTDLAAC FALDNPLSSL YVGGCQGPSL GIPIAAFEQA
     DESVTQVKGI ETKDGEPGEL VATAAFPSMP VRFWGDEGGK KYFGSYFARF DNVWTHGDFI
     SKHPTTHQIF FLGRSDGVLN PSGVRFGSAE IYNVIDTQFS SEVVDSVCVG QRRPTDTDES
     VMLFLLIRDG ATFSPDLVQR VRTAIRKALS ARHVPRFVFE TPAIPVTVNG KKVELPVKQI
     VSGKRIKPSG TLLNPESLEF YYQFAEVENL GGVEAKL
//
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