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ACSA_COPC7
ID   ACSA_COPC7              Reviewed;         661 AA.
AC   A8PDE3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Acetyl-coenzyme A synthetase;
DE            EC=6.2.1.1;
DE   AltName: Full=Acetate--CoA ligase;
DE   AltName: Full=Acyl-activating enzyme;
GN   Name=ACS-1; ORFNames=CC1G_09467;
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS   (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=240176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA   Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA   Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA   Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA   Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA   Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA   Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AACS02000006; EAU81223.1; -; Genomic_DNA.
DR   RefSeq; XP_001840583.1; XM_001840531.2.
DR   AlphaFoldDB; A8PDE3; -.
DR   SMR; A8PDE3; -.
DR   STRING; 5346.XP_001840583.1; -.
DR   EnsemblFungi; EAU81223; EAU81223; CC1G_09467.
DR   GeneID; 6017231; -.
DR   KEGG; cci:CC1G_09467; -.
DR   VEuPathDB; FungiDB:CC1G_09467; -.
DR   eggNOG; KOG1175; Eukaryota.
DR   HOGENOM; CLU_000022_3_6_1; -.
DR   InParanoid; A8PDE3; -.
DR   OMA; SPDIWEW; -.
DR   OrthoDB; 288915at2759; -.
DR   Proteomes; UP000001861; Unassembled WGS sequence.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 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.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF16177; ACAS_N; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..661
FT                   /note="Acetyl-coenzyme A synthetase"
FT                   /id="PRO_0000333258"
FT   BINDING         199..202
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         317
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         393..395
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         417..422
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         508
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         523
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         531
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         534
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         596
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   661 AA;  73128 MW;  C5137472DE171172 CRC64;
     MSEGPIRVAP HPIAKRVKHG CKTPHVSHID DYRSQHRETI GHESDKWWAK KAHELLYWDR
     PFHTVRSGSF ENGDIAWFPE GGLNASYNCV DRWAFKHPEK TAIIYEADEP GEGREISYAE
     LLREVCSIAN VLKSFGVKKG DTVSVYLPMT WQAIAAFLAC ARIGAIHSVV FAGFSAEALR
     DRMQDCKSRV LITSDEGRRG GKAIATKAIA DAALKECPAV EKVLVLKRTG NPVPWTEGRD
     VWWHEAVARV PRYCPPEVMA SEDPLFILYT SGSTGKPKGV VHTTGGYLLC AALTVKYVFD
     VHPDDRFACM ADVGWITGHT YIVYGPLAIG VTTTVFESTP VYPTPSRYWE TVEKYKLTQF
     YSAPTAIRLL RRLGHEHVNK HDLSSLRVLG SVGEPINPEA WHWYNEHVGK TECAIVDTFW
     QTETGSIVVT PFPGAIETKP GAATVPFFGI EPAILEPTTG KVLEGNDVEG VLTIAHPWPS
     IARTIYGDHQ RYLETYMKPY PGYFYTGDGA ARDEDGYIWI KGRVDDVINV SGHRLSTAEI
     ESALITHTGV AETAVIGTAD ELTGQAVYAF VTLKPEFKFD PENEAGLSKE LILQVRKIIG
     PFAAPKRIYI VSDLPKTRSG KIMRRILRKI VAGEADQLGD LSTLADPGIV EVIKEKVASA
     A
 
 
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