ID   ACSA_NOSLI              Reviewed;         337 AA.
AC   Q93LL2;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Acetyl-coenzyme A synthetase;
DE            Short=AcCoA synthetase;
DE            Short=Acs;
DE            EC=6.2.1.1;
DE   AltName: Full=Acetate--CoA ligase;
DE   AltName: Full=Acyl-activating enzyme;
DE   Flags: Fragment;
GN   Name=acsA;
OS   Nostoc linckia.
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=92942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Dvornyk V.Y., Vinogradova O.N., Krugman T., Nevo E.;
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA),
CC       an essential intermediate at the junction of anabolic and catabolic
CC       pathways. AcsA undergoes a two-step reaction. In the first half
CC       reaction, AcsA combines acetate with ATP to form acetyl-adenylate
CC       (AcAMP) intermediate. In the second half reaction, it can then transfer
CC       the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the
CC       product AcCoA (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
CC       activates the enzyme (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AY037787; AAK68857.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q93LL2; -.
DR   SMR; Q93LL2; -.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR020459; AMP-binding.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 1.
DR   PRINTS; PR00154; AMPBINDING.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Acetylation; ATP-binding; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding.
FT   CHAIN           <1..>337
FT                   /note="Acetyl-coenzyme A synthetase"
FT                   /id="PRO_0000208371"
FT   BINDING         131..134
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         273
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         325..327
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         337
SQ   SEQUENCE   337 AA;  37143 MW;  342E68DEA8362B28 CRC64;
     TSGKVSIKWF EDGVLNVTES CLDRHLATRG DQVAIIWEGD DPNADSKVTY RELHARVCQL
     ANAMRGMGVQ KGDRVCIYLP MIEEAAVAML ACARIGAVHS IVFGGFSPDS LSSRIQDSDC
     VLLITADEGR RGGRKVPLKV NADEALKTCP SIRHVIVAKN TGGNVAMQEG RDHWWADACD
     NQPKTSTPEP MGAEDPLFIL YTSGSTGKPK GVLHTTGGYL VWASFTHQNV FDYRDGEIYW
     CTADVGWVTG HTYIVYGPLA NGATTLMFEG VPNYPTVSRF WEVIDKHQVN IFYTAPTAIR
     ALMRDGEAPV KKTSRKSLRI LGSVGEPINP EAWLWYY