ID A0A0D2HGW1_9EURO Unreviewed; 775 AA.
AC A0A0D2HGW1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE SubName: Full=Acetoacetate-CoA ligase {ECO:0000313|EMBL:KIW83684.1};
GN ORFNames=Z517_02930 {ECO:0000313|EMBL:KIW83684.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW83684.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW83684.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW83684.1,
RC ECO:0000313|Proteomes:UP000053029};
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 Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN846970; KIW83684.1; -; Genomic_DNA.
DR RefSeq; XP_013287492.1; XM_013432038.1.
DR AlphaFoldDB; A0A0D2HGW1; -.
DR STRING; 1442368.A0A0D2HGW1; -.
DR GeneID; 25302420; -.
DR VEuPathDB; FungiDB:Z517_02930; -.
DR HOGENOM; CLU_000022_3_3_1; -.
DR OrthoDB; 45466at2759; -.
DR Proteomes; UP000053029; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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:SF4; ACETOACETYL-COA SYNTHASE (AFU_ORTHOLOGUE AFUA_8G04770); 1.
DR PANTHER; PTHR42921; ACETOACETYL-COA SYNTHETASE; 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 Ligase {ECO:0000313|EMBL:KIW83684.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053029};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 207..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 157..548
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT REGION 23..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 775 AA; 85973 MW; A192848B6D4A7165 CRC64;
MPSESPASCN AVGLPMKYCS KQYRDQAKRT LDSPGTSSSS STPSRNQNPS SSTDSNSTSL
PTPLWTPADP EAPPMSRYRQ HVNTKFSQSL RDSHELHSWT VQNPHQFWID LYEYCGIVPS
LPKHTKLAYN PKARLRDIPT FFPGLRLNYA ENVLVPNAAA NPNAVALVGL RENRLDDPEE
ITWAELTELV RVARSAMVRR GIKKGDVVAG LMANSVWIIV LFLATASIGA IFTSVSPDLG
VSGCVSRFAQ VEPKWLFADV DVAVRGTRPS MLGKVMQVLK ALPAAKAKPR LVFVPTCHRP
HRQQHMDYIK PVGGAISLHE FLTKARAGDK LTYTRVPTDH PLVIVYSSGT TGEPKCIVSP
HMSVLNYKKI SLLHNGLGPG STVFQFSSTS WILWNVMNGH LSVGAKVVCY DGGALHPDPS
TMLRICAQFR ATYWGTSPRY LLELEQSGIR PDAFDLSRLA LVTTTGATLT GEQFHWFYRA
FPRRIHLSSV AGGTDIASSW IATNPAGPVY ANEMQMWALG HDCDILDSET GRSCAAEGRP
GELVCRKPFP SMPCRFWGDT PDHRKYREAY FEKFPLSNNS TDKTAAADGE EYLDVWAQHD
FIVMNPLTKG LQILGRSDGV LNPSGIRFGS SEVYNIVEGP QFNTLISDTL CVGRRRAHDK
DETVFLFVVM APGHDADFTP GLVEQLRTAI REGLSPRHVP KFIEQVREIP YTVNGKKVEV
AVKRVISGQV VKTSSTVRNP ACLAEYERFR DLERAPQRQR QQQQQQTGRR GMAKL
//