ACSA_COPCI
ID ACSA_COPCI Reviewed; 661 AA.
AC O13440; O13441;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 68.
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;
OS Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=5346;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=JV6;
RA Chaure P.T., Casselton L.A., Connerton I.F.;
RL Submitted (NOV-1997) 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 -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; Y15417; CAA75612.1; -; mRNA.
DR EMBL; Y15418; CAA75613.1; -; Genomic_DNA.
DR AlphaFoldDB; O13440; -.
DR SMR; O13440; -.
DR VEuPathDB; FungiDB:CC1G_09467; -.
DR VEuPathDB; FungiDB:CC2G_014513; -.
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 2: Evidence at transcript level;
KW ATP-binding; Ligase; Nucleotide-binding.
FT CHAIN 1..661
FT /note="Acetyl-coenzyme A synthetase"
FT /id="PRO_0000208409"
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"
FT CONFLICT 14
FT /note="A -> G (in Ref. 1; CAA75613)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="F -> L (in Ref. 1; CAA75613)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 661 AA; 73094 MW; D647C974095795D9 CRC64;
MSEGPIRVAP HPIAKRVKHG CKTPHVSHID DYRSQHRETI GHESDKWWAK KAHELLYWDR
PFHTVRSGSF ENGDIAWFPE GGLNASYNCV DRWAFKHPEK TAIIYEADEP GEGREISYAE
LLREVCSIAN VLKSFGVKKG DTVSVYLPMT WQAVAAFLAC ARIGAIHSVV FAGFSAEALR
DRMQDCKSRV LITSDEGRRG GKAIATKAIA DAALKECPAV EKVLVLKRTG NPVPWTEGRD
VWWHEAVARV PRYCPPEVMA SEDPLFILYT SGSTGKPKGV VHTTGGYLLC AALTVKYVFD
VHPDDRFACM ADVGWITGHT YIVYGPLAIG ATTTVFESTP VYPTPSRYWE TVEKYKLTQF
YSAPTAIRLL RRLGHEHVNK HDLSSLRVLG SVGEPINPEA WHWYNEHVGK TECAIVDTFW
QTETGSIVVT PFPGAIETKP GAATVPFFGI EPAILEPTTG KVLEGNDVEG VLTIAHPWPS
IARTIYGDHQ RYLETYMKPY PGYFYTGDGA ARDEDGYIWI KGRVDDVINV SGHRLSTAEI
ESALITHTGV AETAVIGTAD ELTGQAVYAF VTLKPEFKFD AENEAGLSKE LILQVRKIIG
PFAAPKRIYI VSDLPKTRSG KIMRRILRKI VAGEADQLGD LSTFADPGIV EVIKEKVASA
A