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
//