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Database: UniProt
Entry: A0A2C5Y6M2_9HYPO
LinkDB: A0A2C5Y6M2_9HYPO
Original site: A0A2C5Y6M2_9HYPO 
ID   A0A2C5Y6M2_9HYPO        Unreviewed;       666 AA.
AC   A0A2C5Y6M2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE            EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN   ORFNames=CDD81_3266 {ECO:0000313|EMBL:PHH65135.1};
OS   Ophiocordyceps australis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=1399860 {ECO:0000313|EMBL:PHH65135.1, ECO:0000313|Proteomes:UP000226192};
RN   [1] {ECO:0000313|EMBL:PHH65135.1, ECO:0000313|Proteomes:UP000226192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Map64 {ECO:0000313|EMBL:PHH65135.1,
RC   ECO:0000313|Proteomes:UP000226192};
RA   De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT   "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT   behavioral manipulation genes and a possible major role for enterotoxins.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:PHH65135.1}.
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DR   EMBL; NJET01000021; PHH65135.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C5Y6M2; -.
DR   STRING; 1399860.A0A2C5Y6M2; -.
DR   OrthoDB; 144557at2759; -.
DR   Proteomes; UP000226192; 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:UP000226192}.
FT   DOMAIN          41..97
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          99..484
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          546..624
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   666 AA;  74040 MW;  F71805215DEBACF5 CRC64;
     MAGQPNGMRV YEAHEVDTFH PPEKMFAKHP SKPHLANLDE YRKLYKESIT DPAAFWGRNA
     RELLSWYRDF ETVYSGSLAN GDSKWFVEGQ LNASYNCVDR HAFKDPERVA IIYEADEPGN
     GRNVTYGELL RDVSKVAWTL KQMGVRKGDS VAIYLPMIPE ALVAILACVR IGAVHSVVFA
     GFSADSLRDR VVDADSKVVI TTDEGKRGGK LIGTKKIVDD ALKQCPHVNH VLVYKRTGAD
     VPMQRGRDLW WHEEVEKWPS YIAPEVMNSE DPLFLLYTSG STGKPKGVMH TTAGFLIGCA
     MTGKYVFDIH DGDRYFCGGD VGWITGHSYV VYAPLLLGVS TVVFEGTPAY PNFSRYWEII
     DQNKVTQFYV APTALRLLKR AGDEHVKSRM ADLRVLGSVG EPIAAEVWKW YFEVVGKEEA
     HIVDTYWQTE TGSNVITPLA GVTPTKPGSA SFPFFGIEPA IIDPVSGQEL HGNDVDGVLA
     FKQAWPSMAR TVYGAHKRYM DTYLNVYKGY YFTGDGAGRD HDGFYWIRGR VDDVVNVSGH
     RLSTAEIEAA LIEHHAIAEA AVVGVSDELT GQAVNAFVAI KEGNEHDEAL QKEFIMQVRK
     SIGPFAAPKA IYVVPDLPKT RSGKIMRRIL RKILAGEEDQ LGDTSTLSDP SVVDKILKTV
     HESKRK
//
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