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Database: UniProt
Entry: H0ETH5_GLAL7
LinkDB: H0ETH5_GLAL7
Original site: H0ETH5_GLAL7 
ID   H0ETH5_GLAL7            Unreviewed;       669 AA.
AC   H0ETH5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE            EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN   ORFNames=M7I_6038 {ECO:0000313|EMBL:EHK98166.1};
OS   Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHK98166.1, ECO:0000313|Proteomes:UP000005446};
RN   [1] {ECO:0000313|EMBL:EHK98166.1, ECO:0000313|Proteomes:UP000005446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX   PubMed=22302591; DOI=10.1128/EC.05302-11;
RA   Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT   "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT   of a species from the Helotiaceae family.";
RL   Eukaryot. Cell 11:250-250(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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHK98166.1}.
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DR   EMBL; AGUE01000163; EHK98166.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0ETH5; -.
DR   HOGENOM; CLU_000022_3_6_1; -.
DR   InParanoid; H0ETH5; -.
DR   Proteomes; UP000005446; Unassembled WGS sequence.
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:UP000005446}.
FT   DOMAIN          45..101
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          103..492
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          550..628
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   669 AA;  74111 MW;  D8811C2EBB896223 CRC64;
     MSEGDVKPSS GPVVAEAHQV DTFHPPEKMF AKHPSKPHIK DLEEYQKMYK ESITEPEKFW
     GNMAHDLLSW QTDFKTVHAG SFENGDNSWF LEGQLNASYN CVDRHAIKNP DKTAIIYEAD
     ETSDGRTLSY SELLRQVCKT AYVLKQMGVK KGDTVAIYLP MIPEAVIAFL ACARIGAVHS
     VVFAGFSADS LRDRVIDAQS KVVITTDEGK RGGKLIGTKK IVDDALKQCP DVTHCLVYKR
     TGAEVPWTEG RDWWWHDEVD KWPAYIAPEP MNSEDPLFLL YTSGSTGKPK GVMHSTAGYL
     LGAAATGKYV FDIHDTDKFF CGGDVGWITG HTYVVYAPLL LGVATVVFEG TPAYPNFSRY
     WDVIEKHGVT QFYVAPTALR LLKRAGNEHI KHQMKHLRVL GSVGEPIAAE VWKWYFEIVG
     KEEAHVVDTY WQTETGSHVI TPLAGVTPTK PGSASLPFFG IEPAIIDPVS GEEIHGNDVE
     GVLAFKQPWP SMARTVWGAH KRYMDTYLNV YKGYYFTGDG AGRDHEGYYW IRGRVDDVVN
     VSGHRLSTAE IEAALIEHPA VAEAAVVGIT DELTGQAVNA FVAIKDGNEV NDALKKDLVL
     QVRKSIGPFA APKAIFVVPD LPKTRSGKIM RRILRKILAK EEDQLGDTST LSDPSVVDKI
     IETVQASRK
//
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