ID A0A074XLA8_AURPU Unreviewed; 689 AA.
AC A0A074XLA8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acetoacetate-CoA ligase {ECO:0000313|EMBL:KEQ84494.1};
GN ORFNames=M438DRAFT_296964 {ECO:0000313|EMBL:KEQ84494.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ84494.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ84494.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ84494.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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DR EMBL; KL584982; KEQ84494.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074XLA8; -.
DR STRING; 1043002.A0A074XLA8; -.
DR HOGENOM; CLU_000022_3_3_1; -.
DR OrthoDB; 45466at2759; -.
DR Proteomes; UP000030706; 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 CDD; cd05943; AACS; 1.
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:KEQ84494.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706}.
FT DOMAIN 51..108
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 117..452
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 689 AA; 75295 MW; F161B4009794E974 CRC64;
MPHANGTHDS YDTNGQGLGA ELWRHSSPES TQMWTFLQTV NKAKNIQLKN YDDLYNWSID
QTADFWEAVW QFTGIKASAS YDEVLPKDAP MFPRPSFFRG AKLNFAENLL FPPQAPSPDS
PAIIAATETG RETVTWAELR EKVRVCQSGM LALNVKAGDR VAGYVANHTN ALVAMLAATS
LGAIWTAISP DTGVTAVLDR LTQIEPVILF ADNASLYNGK THPTMPKVQE IGSSLPSLKA
LVIFPTVPSV SAEIDVPSLA GIVVSYDSFV KKEAAPKETI FTQLHPDHPV YILYSSGTTG
APKCIVHGAI GTLLQHKKEH ILHCDIQPGD KLFYFTTCTW MMWHWLVSGL ASGATLVLYD
GSPFRYVSDG KSVPDDLAMA RLIDELSITH FGTSAKYLSV LEQKSVMPKE QGVSLKTLKA
IYSTGSPLAP STFQYVYQAF GSVNLGSITG GTDIISLFGA PCPLTPVYTG EIQVLGLGMA
VRAWDYLGAD VTTTGSAGDL VCTKPFPCQP VQFWGPTGES KYQSSYFETF PGVWHHGDFI
RFNPKTGGLY MLGRSDGILK PSGVRFGSAE IYNILLKHFP DTVEDALCIG RRRETDDDET
VVLFLKMKEG EKFNTDLVKS IQKVIRGELS ARHVPGIVDE TPEIPVTTNG KKIEAAVKQI
LCGMNVKTSA SVANAGCLDW YREWANSHN
//
