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Database: UniProt
Entry: A0A0D2BQ51_9EURO
LinkDB: A0A0D2BQ51_9EURO
Original site: A0A0D2BQ51_9EURO 
ID   A0A0D2BQ51_9EURO        Unreviewed;       664 AA.
AC   A0A0D2BQ51;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acetoacetate-CoA ligase {ECO:0000313|EMBL:KIW54666.1};
GN   ORFNames=PV05_07013 {ECO:0000313|EMBL:KIW54666.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW54666.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW54666.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW54666.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN847320; KIW54666.1; -; Genomic_DNA.
DR   RefSeq; XP_013315250.1; XM_013459796.1.
DR   AlphaFoldDB; A0A0D2BQ51; -.
DR   STRING; 348802.A0A0D2BQ51; -.
DR   GeneID; 25328921; -.
DR   HOGENOM; CLU_000022_3_3_1; -.
DR   OrthoDB; 45466at2759; -.
DR   Proteomes; UP000054342; 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, ECO:0000313|EMBL:KIW54666.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054342}.
FT   DOMAIN          37..94
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          101..477
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          549..619
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   664 AA;  73451 MW;  DCBF5AB18390F670 CRC64;
     MSATQKPLWV HPAPQFSQAD GFRRLINRKY GLKLETYDDL HRWSVDELET FSVEVWTFCG
     MVYSKPPTAT AVGLESMWPR PQWFPGARLN YAENMLATGL AVHPDAIAIS ACREGGTEWR
     HLSWMQLRAE VERYVSAFKQ AGISKGDRVA AVMTNSPEAL LVLLASAAVG AIFSSTAPDM
     GQKGITERYL QIRPKVLFVD TEVLYGGGEK DLRQKVSSVV RSLQASVSEL EKVVVTRGHL
     WSGTNSMSLE TFLQAPRQEL IFEQVEFDHP VYILYSSGTT GPPKCICHAG GAALLQQKKD
     LMLIKDMGPN SVYYQYTTTG WMMWNYLVAG LSTGARIVMY DGSPSHPSPA YQVQLLSEQG
     VTEWGTSPKF LAALKQHGLG AMPNLENLAL TLVTGSPLSV ELSEWFYQKF PRHVATFSSS
     GGTDLVSAIV NGSMLRPFYA GELATKCLGM AVEIWDASGK NIEDTGEKGD LVITKPFFSM
     PVTFWGENGM EKYRKAYFDQ FPGVWCHGDF ISKNPATKGF TILGRSDGVL NPGGIRFGTA
     ELYGVVDKFK EVEDCIAVGQ RREHDSDERV LLFLKLAQKP MSKELEQRIR TAIRTELSAR
     HVPSYILEVA DIPYTANGKK IENVVKDVVS GRVPKIGGTA VNPECLEEYK AFANLPPLPA
     KARL
//
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