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Database: UniProt
Entry: A0A316YD54_9BASI
LinkDB: A0A316YD54_9BASI
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ID   A0A316YD54_9BASI        Unreviewed;       719 AA.
AC   A0A316YD54;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Acetoacetate-CoA ligase {ECO:0000313|EMBL:PWN87142.1};
GN   ORFNames=FA10DRAFT_269749 {ECO:0000313|EMBL:PWN87142.1};
OS   Acaromyces ingoldii.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX   NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN87142.1, ECO:0000313|Proteomes:UP000245768};
RN   [1] {ECO:0000313|EMBL:PWN87142.1, ECO:0000313|Proteomes:UP000245768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN87142.1,
RC   ECO:0000313|Proteomes:UP000245768};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
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DR   EMBL; KZ819641; PWN87142.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316YD54; -.
DR   STRING; 215250.A0A316YD54; -.
DR   InParanoid; A0A316YD54; -.
DR   OrthoDB; 45466at2759; -.
DR   Proteomes; UP000245768; 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; 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:PWN87142.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245768}.
FT   DOMAIN          45..104
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          136..513
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
SQ   SEQUENCE   719 AA;  78776 MW;  1F5A40C94543E5D0 CRC64;
     MEQEAGDQLL SKVMYDPGNV SGTRLAKFQQ KIAEKYRRPD VGKDYESFWA WSCEDPASFW
     RECWDEVDII ASVRAKDDDV LPEGDRIYPP PKWFVGARLN VAENLLRHSL PGSELVNKPA
     LIQATEPSAE EPENFLVQTT TQSELRRQVA QAVRALRQRG VVAGDRVASY ASNCSANVVA
     FLATAAIGAI WISAAADFAP QGVLERLTTV RPKVLFAVNA VRYNGKVHDH TEKVRAVVDG
     LDASAGAEEQ KLEGVILIPY MASSPTTLDK TKGWTSWESF LKEEGRAREG EDESSIDFAQ
     LDFNHPLWIL FSSGTTGKPK AITHRAGGML LQLAKEHLIH GGMTPQDVFF QYTTPGWMMW
     NFLVAGLVSG APLVLFDGSP LRPSASSLWS LADKLGITVF GTSAAYLAAL EKSGCEPRRE
     FPSLKVRQVL STGSPLRADL YPFIMKAVGP DTLIGSITGG TDICSLFAGH NVALPVRAGE
     IQARNLGMAV QIYSDAGKPL GAGSPGDLVC TKPFPAQPLG FWGQASEDRH RETYYSTFDN
     VWYHGDYVVL TEHHGLVMLG RSDGVLNPGG IRFGSSEIYE VVAKLQQQQQ QQQQQGEAKT
     TAAARIQNSL VCGLKMPKGD DEVVVLFLVV EQIDDAQWQA LVDEIKSAIR RERSPRHVPR
     FVRRVKGVPL TMNGKLAEVP AKKLLNGASI EGINKATLSN SDVLTEYVEE GRVLRSQLS
//
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