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Database: UniProt
Entry: A0A162KRL9_CORDF
LinkDB: A0A162KRL9_CORDF
Original site: A0A162KRL9_CORDF 
ID   A0A162KRL9_CORDF        Unreviewed;       691 AA.
AC   A0A162KRL9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Acetoacetyl-CoA synthase {ECO:0000313|EMBL:OAA78818.1};
GN   ORFNames=LEL_02304 {ECO:0000313|EMBL:OAA78818.1};
OS   Akanthomyces lecanii RCEF 1005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC   Cordyceps confragosa.
OX   NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA78818.1, ECO:0000313|Proteomes:UP000076881};
RN   [1] {ECO:0000313|EMBL:OAA78818.1, ECO:0000313|Proteomes:UP000076881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA78818.1,
RC   ECO:0000313|Proteomes:UP000076881};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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:OAA78818.1}.
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DR   EMBL; AZHF01000002; OAA78818.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162KRL9; -.
DR   STRING; 1081108.A0A162KRL9; -.
DR   OrthoDB; 45466at2759; -.
DR   Proteomes; UP000076881; Unassembled WGS sequence.
DR   GO; GO:0030729; F:acetoacetate-CoA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR025110; AMP-bd_C.
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; ACETOACETYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR42921:SF1; ACETOACETYL-COA SYNTHETASE; 1.
DR   Pfam; PF16177; ACAS_N; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076881}.
FT   DOMAIN          45..102
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          115..496
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          584..654
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   691 AA;  74536 MW;  26C94FA6322B48B3 CRC64;
     MGQSVPQDPP ALAEKLWTHP DPSSTPMWRF IQRINNKYNL AIAGYPELYQ WSIDNVAEFW
     SEAWHFVGIV ASKEAEQVLP KDAHMYPRPD FFGSARLNFA ENLLFPPTST PLDANATAVI
     TTTELPGDLR STSWAELREA VRRCSNSLRA AGLRPNDVVA GYVSNHVEAL VAMLAAASIG
     AVWTGISPDN GVSAVLDRLS QIGPKVLFAD NGTVYNGKEW SSTSKTDEIV AALKSTGLET
     VVVINNIKGG LGLTELTAHG VKAVDYTSFL EIASTDALKF EQMPSSHPLY ILYSSGTTGL
     PKAIVHTALG TLLQHKKEHV LHCSLTPASR MLYYTTTSWM MWHWSVGALA AGATLVLYSG
     SPFRPNSYLS IPRVLSDLQV THFGTSAAYL TALEANNVRP VEDKSIDLSR LEAIYSTASP
     LPPSTFKFVY EAFPKTVNLA SITGGTDIIS LFGAPCPLLP VRVGEIQCAG LGMAIKVVDS
     ATGEDVPAGE PGDLVCVKPF PCQPLTFFGA NGEAKYQAAY FERFADVCGV QGAVWHHGDF
     VKIPDASTGA LLMLGRSDGV LKPAGVRFGS AEIYNILTRF FAADVEDAVC VGRRRETDMD
     ETVCLFVVPV EGKSFTEELQ GQIKAKIRSE LSPRHVPGVI AAAGGGIPKT GNGKKIEVAV
     KQILSGMNIK TNASVANPES LEWFREWAKA N
//
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