ID   J5J6H7_BEAB2            Unreviewed;       663 AA.
AC   J5J6H7;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE            EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN   ORFNames=BBA_08910 {ECO:0000313|EMBL:EJP62113.1};
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP62113.1, ECO:0000313|Proteomes:UP000002762};
RN   [1] {ECO:0000313|EMBL:EJP62113.1, ECO:0000313|Proteomes:UP000002762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP62113.1,
RC   ECO:0000313|Proteomes:UP000002762};
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA   St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:456215; EC=6.2.1.1;
CC         Evidence={ECO:0000256|RuleBase:RU361147};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432, ECO:0000256|RuleBase:RU361147}.
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DR   EMBL; JH725191; EJP62113.1; -; Genomic_DNA.
DR   RefSeq; XP_008602229.1; XM_008604007.1.
DR   AlphaFoldDB; J5J6H7; -.
DR   STRING; 655819.J5J6H7; -.
DR   GeneID; 19891922; -.
DR   HOGENOM; CLU_000022_3_6_1; -.
DR   InParanoid; J5J6H7; -.
DR   OrthoDB; 144557at2759; -.
DR   PHI-base; PHI:123537; -.
DR   Proteomes; UP000002762; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR   CDD; cd05966; ACS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR011904; Ac_CoA_lig.
DR   InterPro; IPR032387; ACAS_N.
DR   InterPro; IPR025110; AMP-bd_C.
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; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR   PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR   PANTHER; PTHR24095:SF14; ACETYL-COENZYME A SYNTHETASE 1; 1.
DR   Pfam; PF16177; ACAS_N; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361147};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU361147};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361147};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002762}.
FT   DOMAIN          37..93
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          95..480
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          542..620
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   663 AA;  73350 MW;  C4E77E381D491597 CRC64;
     MAAEQPKVQE AVAALSPPEK MLAKHPSKPH LANTEEYQKL YKESITDPTN FWGTQARDLL
     SWTRDFDTVY SGSLQGGDSK WFVEGELNAS YNCVDRHALK DPNRVAIIYE ADEAGDGRNV
     TYSELLRDVC KVAWTLRKMG VKKGDTVAIY LPMIPEAIVA ILACIRLGAV HSVVFAGFSA
     DSLRDRVLDA DSRVVITSDE GKRGGKLIGT KKIVDDALKQ CPNVRNCLVF RRTGTEVPMQ
     EGRDVWWHDE VEKWPNYIAP EPMNSEDPLF LLYTSGSTGK PKGIMHTTAG YLLGCALTGR
     YVFDIHDGDR FFCGGDVGWI TGHSYVVYAP LLLGITTVVF EGTPAYPNFS RYWDIINKHQ
     ITQFYVAPTA LRLLKRAGDE YVTGEMKHLR VLGSVGEPIA AEVWKWYYDI VGRKESQIVD
     TYWQTETGSH VITPLAGVTA TKPGSASLPF FGIEPAIIDP LSGEEIHGND VEGVLAFKQA
     WPSMARTVYG AHKRYMDTYF NVYPGFYFTG DGAARDHEGF YWIRGRVDDV VNVSGHRLST
     AEIEAALIEH TAVAEAAVVG VNDELTGQAV NAFVAVKGGN EINDALRKEF IMQVRKSIGP
     FAAPKAVFVV TDLPKTRSGK IMRRILRKIL AGEEDQLGDT STLSDPSVVD QIIATVHEAR
     SKK
//