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Database: UniProt
Entry: A0A165SD11_9APHY
LinkDB: A0A165SD11_9APHY
Original site: A0A165SD11_9APHY 
ID   A0A165SD11_9APHY        Unreviewed;       677 AA.
AC   A0A165SD11;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Acetoacetate-CoA ligase {ECO:0000313|EMBL:KZT71816.1};
GN   ORFNames=DAEQUDRAFT_755635 {ECO:0000313|EMBL:KZT71816.1};
OS   Daedalea quercina L-15889.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Daedalea.
OX   NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT71816.1, ECO:0000313|Proteomes:UP000076727};
RN   [1] {ECO:0000313|EMBL:KZT71816.1, ECO:0000313|Proteomes:UP000076727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-15889 {ECO:0000313|EMBL:KZT71816.1,
RC   ECO:0000313|Proteomes:UP000076727};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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DR   EMBL; KV429044; KZT71816.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165SD11; -.
DR   STRING; 1314783.A0A165SD11; -.
DR   OrthoDB; 45466at2759; -.
DR   Proteomes; UP000076727; 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; 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   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, ECO:0000313|EMBL:KZT71816.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076727}.
FT   DOMAIN          40..95
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          102..484
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
SQ   SEQUENCE   677 AA;  74320 MW;  3FB95F056AE7B568 CRC64;
     MEGHFAHSKL IWSPSRPSYS SLDVFRRIVN RKHGLNLEDY HELHKYSIES YNFWMDVWEF
     VGIISSIPPE KILEEGRMKE LPTWFPGARL NYAENLLRRS DDGVACIAAR ESGAVRHYTF
     RQLREMVRSL TAAMRTNGIT KGDRVAAIVT NSVEAVVIAL ASAAIGAIFS STAPDMGTQG
     ILDRYQQIQP KIIFSESQVV YAGKVFDVVP KVSAVAKALV SHGLQSVVLL PSTSTGKELS
     AARMIDVPKS VAISAFLATG DNGPLVFEQL PFNHPLYILY SSGTTGPPKC IIHSAGGVLL
     QAKKDLRLSI GLNENDTYFQ YTTTGWMMWP YMLHGLACGS CIVVYDGSPF HPDVRNFLHF
     LSHEGVSVFG TSPRFLSEVQ GLGIEPAKLA SFAALRVISS TGSVLTPPMF EWTQQAFNPD
     IHLLSVSGGT DICGAFVGGM PVLPVYAGEI QGKLLGMKVE IFDADGKNID DTGIPGELVC
     TRPHPSQPLG FWGDESGEKV GKAYFSTYPG VWHQGDFIVK NPKTQGLMIL GRSDGVLNPS
     GVRFGSAEIY SILEDFSDII DDSLCVGQRR PKDSDERVLL FLKMRPDHPF NEELVSRIRS
     AIRAALSPRH VPAHIFEIEE IPYTVNGKKI EIAVKQIVSG STLKPSGTVA NPESLKLYYK
     FLDLEGLISN KVVKAKL
//
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