ID G4UGB1_NEUT9 Unreviewed; 707 AA. AC G4UGB1; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 03-MAY-2023, entry version 35. DE SubName: Full=Acetoacetate-CoA ligase {ECO:0000313|EMBL:EGZ75310.1}; GN ORFNames=NEUTE2DRAFT_83536 {ECO:0000313|EMBL:EGZ75310.1}; OS Neurospora tetrasperma (strain FGSC 2509 / P0656). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora. OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ75310.1, ECO:0000313|Proteomes:UP000008513}; RN [1] {ECO:0000313|EMBL:EGZ75310.1, ECO:0000313|Proteomes:UP000008513} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513}; RX PubMed=21750257; DOI=10.1534/genetics.111.130690; RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A., RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.; RT "Massive changes in genome architecture accompany the transition to self- RT fertility in the filamentous fungus Neurospora tetrasperma."; RL Genetics 189:55-69(2011). CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family. CC {ECO:0000256|ARBA:ARBA00006432}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GL891107; EGZ75310.1; -; Genomic_DNA. DR AlphaFoldDB; G4UGB1; -. DR STRING; 510952.G4UGB1; -. DR eggNOG; KOG1175; Eukaryota. DR HOGENOM; CLU_000022_3_3_1; -. DR OMA; ISPRWMF; -. DR Proteomes; UP000008513; 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 PANTHER; PTHR42921:SF4; ACETOACETYL-COA SYNTHASE (AFU_ORTHOLOGUE AFUA_8G04770); 1. DR PANTHER; PTHR42921; 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 TIGRFAMs; TIGR01217; ac_ac_CoA_syn; 1. DR PROSITE; PS00455; AMP_BINDING; 1. PE 3: Inferred from homology; KW Ligase {ECO:0000313|EMBL:EGZ75310.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008513}. FT DOMAIN 40..97 FT /note="Acetyl-coenzyme A synthetase N-terminal" FT /evidence="ECO:0000259|Pfam:PF16177" FT DOMAIN 114..566 FT /note="AMP-dependent synthetase/ligase" FT /evidence="ECO:0000259|Pfam:PF00501" SQ SEQUENCE 707 AA; 78081 MW; BF12BB8DC2462E5B CRC64; MRPDVIPTKL WEHPDPESTP MWRFLQNVNK RHGLDMKTFS ELHEYSLQNR SQFWADVWEE ANYIHEGTYS RVVDESAPID AVPIWFEGVK LSYAENVLYS RPKGSSSSQT RSTVGKEDDK VAVTEVREGA SETRDATYGE LRERAGRLAA AMKARGVKKG DIVVIVGSNS IDTLLVWLAT SWLGAIFSSS STDMGTKGIL QRTVQVNPKL LFMDDAALYN GKIVDLREKM AEVVEGLKDC SNFDNIVSIR RFSEARDISA VPKAITWDDF LASAGATPAI PDFVRIPFHE PYLICYSSGT TGTPKAIVHS LGGVMISYFK EGGLHEGLTG SDVTLQYTTT GWIMYLSNVA ILLYGGKTII YDGSPFKPDS SILISLAAQH RVTKLGISPR WMFEFAKNGQ SPREMADLSA LRIVTCTGMV LSDQLFEWFY DSGFPPSVQL ANISGGTDIA GCFGICNPLT PVYVGGTQGP SLGVAVEIYD SMVGDGEPGR PVPEGTAGEL VATTAFPNLP CFFWADPIPE DQKGVASPGT RYHSAYFARF PHVWAHGDFC VIHPTTRSLH LLGRADGVLN PSGVRFGSAE IYSVIERRFA DRVQDSLCVG QRRPKDHDES VMLFLLMKPG QKLDEALVKE VKEAIGKDLS KRHVPKWIFE TPEIPTTINL KKVELPVKHI VCGRKVKPSG TLANPQSLDF YYQFAKVEEL VNPHPNL //