ID   ACSA_METSH              Reviewed;         672 AA.
AC   P27095;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000255|HAMAP-Rule:MF_01123};
DE            Short=AcCoA synthetase {ECO:0000255|HAMAP-Rule:MF_01123};
DE            Short=Acs {ECO:0000255|HAMAP-Rule:MF_01123};
DE            EC=6.2.1.1 {ECO:0000255|HAMAP-Rule:MF_01123};
DE   AltName: Full=Acetate--CoA ligase {ECO:0000255|HAMAP-Rule:MF_01123};
DE   AltName: Full=Acyl-activating enzyme {ECO:0000255|HAMAP-Rule:MF_01123};
GN   Name=acsA {ECO:0000255|HAMAP-Rule:MF_01123}; Synonyms=acs;
OS   Methanothrix soehngenii (Methanosaeta concilii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=2223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Opfikon / DSM 2139;
RX   PubMed=1680850; DOI=10.1128/jb.173.20.6383-6389.1991;
RA   Eggen R.I.L., Geerling A.C.M., Boshoven A.B.P., de Vos W.M.;
RT   "Cloning, sequence analysis, and functional expression of the acetyl
RT   coenzyme A synthetase gene from Methanothrix soehngenii in Escherichia
RT   coli.";
RL   J. Bacteriol. 173:6383-6389(1991).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=2571608; DOI=10.1128/jb.171.10.5430-5435.1989;
RA   Jetten M.S., Stams A.J., Zehnder A.J.;
RT   "Isolation and characterization of acetyl-coenzyme A synthetase from
RT   Methanothrix soehngenii.";
RL   J. Bacteriol. 171:5430-5435(1989).
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. {ECO:0000255|HAMAP-Rule:MF_01123}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01123};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01123};
CC   -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
CC       activates the enzyme. {ECO:0000255|HAMAP-Rule:MF_01123}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000255|HAMAP-Rule:MF_01123}.
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DR   EMBL; M63968; AAA73007.1; -; Genomic_DNA.
DR   PIR; A41043; A41043.
DR   AlphaFoldDB; P27095; -.
DR   SMR; P27095; -.
DR   PRIDE; P27095; -.
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-KW.
DR   GO; GO:0046872; F:metal ion 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   HAMAP; MF_01123; Ac_CoA_synth; 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   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding.
FT   CHAIN           1..672
FT                   /note="Acetyl-coenzyme A synthetase"
FT                   /id="PRO_0000208401"
FT   BINDING         217..220
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         335
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         411..413
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         435..440
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         529
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         544
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         555
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         566
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         568
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         571
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         613
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   MOD_RES         638
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
SQ   SEQUENCE   672 AA;  75527 MW;  D3CB6AC88BAEAF65 CRC64;
     MLKLAGKEDK KLKTTVFQDE TRIFNPPKEL VEKSIVMQWM KKKGFKTEKE MRAWCSSDEH
     YLEFWDEMAK TYVDWHKPYT KVMDDSEMPY FHWFTGGEIN ITYNAVDRHA KGAKKDKVAY
     IWIPEPTDQP VQKITYGDLY KEVNKFANGL KSLGLKKGDR VSIYMPMIPQ LPIAMLACAK
     LGVSHIVVFS GFSSKGLMDR AAHCGSRAII TVDGFYRRGK PVPLKPNADE AAGGAPSVEK
     IIVYKRAGVD VSMKEGRDVW WHDLVKGQSE ECEPVWVDPE HRLYILYTSG TTGKPKGIEH
     ATGGNAVGPA QTLHWVFDLK DDDVWWCTAD IGWVTGHSYI VYAPLILGMT SLMYEGAADY
     PDFGRWWKNI QDHKVTVLYT APTAVRMFMK QGAEWPDKYD LSSLRLLGSV GEPINPEAWM
     WYREHIGRGE LQIMDTWWQT ETGTFLNSPL PITPLKPGSC TFPLPGYDIS ILDEEGNEVP
     LGSGGNIVAL KPYPSMLRAF WGDKERFMKE YWQFYWDVPG RRGVYLAGDK AQRDKDGYFF
     IQGRIDDVLS VAGHRIANAE VESALVAHPK IAEAAVVGKP DEVKGESIVA FVILRVGNEP
     SPELAKDAIA FVRKTLGPVA APTEVHFVND LPKTRSGKIM RRVVKARALG NPVGDISTLM
     NPEAVDGIPK IV