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