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
//