ID   ACSA_METSO              Reviewed;         672 AA.
AC   P27095;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   16-JUN-2009, entry version 54.
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=acsA; Synonyms=acs;
OS   Methanothrix soehngenii.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosaetaceae; Methanosaeta.
OX   NCBI_TaxID=2223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Opfikon / DSM 2139;
RX   MEDLINE=92011409; PubMed=1680850;
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   MEDLINE=90008777; PubMed=2571608;
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   -!- CATALYTIC ACTIVITY: ATP + acetate + CoA = AMP + diphosphate +
CC       acetyl-CoA.
CC   -!- SUBUNIT: Homodimer.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
CC       activates the enzyme (By similarity).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family.
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DR   EMBL; M63968; AAA73007.1; -; Genomic_DNA.
DR   PIR; A41043; A41043.
DR   HSSP; Q8ZKF6; 1PG4.
DR   BRENDA; 6.2.1.1; 267.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:HAMAP.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   HAMAP; MF_01123; -; 1.
DR   InterPro; IPR011904; Ac_CoA_lig_AcsA.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF00501; AMP-binding; 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; Nucleotide-binding.
FT   CHAIN         1    672       Acetyl-coenzyme A synthetase.
FT                                /FTId=PRO_0000208401.
FT   ACT_SITE    546    546       By similarity.
FT   MOD_RES     638    638       N6-acetyllysine (By similarity).
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
//