ID   ACSA_ALHEH              Reviewed;         645 AA.
AC   Q0AAW0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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; OrderedLocusNames=Mlg_0673;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + acetate + CoA = AMP + diphosphate +
CC       acetyl-CoA.
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000453; ABI56027.1; -; Genomic_DNA.
DR   RefSeq; YP_741517.1; -.
DR   GeneID; 4268468; -.
DR   GenomeReviews; CP000453_GR; Mlg_0673.
DR   KEGG; aeh:Mlg_0673; -.
DR   NMPDR; fig|187272.6.peg.645; -.
DR   HOGENOM; Q0AAW0; -.
DR   OMA; Q0AAW0; HQRMVDT.
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   3: Inferred from homology;
KW   Acetylation; ATP-binding; Complete proteome; Ligase;
KW   Nucleotide-binding.
FT   CHAIN         1    645       Acetyl-coenzyme A synthetase.
FT                                /FTId=PRO_1000065268.
FT   ACT_SITE    514    514       By similarity.
FT   MOD_RES     606    606       N6-acetyllysine (By similarity).
SQ   SEQUENCE   645 AA;  71429 MW;  C56D61DCD4C81904 CRC64;
     MSDTKVYPVP DYIREKAHIT KDTYEEMYRR SLDDPEGFWG EQAEKFLDWF SKWDKVYHSD
     LKNGEIRFFE GGKLNVAHNC LDRHLEQRGD QTAIIWEGDD PNNSEHITYK DLHERVCRLA
     NAMKARGVKK GDRVCIYLPM IPEAAVAMLA CARIGAIHSI VFGGFSPDAL KDRIQNADCE
     TVITADEGVR GGRNVALKSN ADKALESCPD VKNVFVVKRT GGDIDWKEGR DIWYHEAVAD
     VSADCPAEEL DAEDPLFILY TSGSTGKPKG VQHCSAGYLL GAAMTHKYVF DYQEGEVYWC
     TADVGWVTGH SYIVYGPLAN GATTLMFEGV PTYPSAARCW EVVDKHNVSI FYTAPTAIRA
     LMGQGNEHVT KTSRKSLRIL GTVGEPINPE AWEWYYNVVG DGRCPIVDTW WQTETGSILI
     APLPGATDLK PGSATLPFFG VEPALVDPEG KELEGAASGN LVIKRAWPSM MRTVYGDHKR
     FMETYLAAYP GMYFTGDGAR RDEDGYYWIT GRVDDVINVS GHRMGTAEVE SALVLHDAVA
     EAAVVGYPHD IKGQGIYAYV TLMAGVEPSD ELKKELVKLV SNEIGPIAKP DVIQWAPGLP
     KTRSGKIMRR ILRKVAANEL DSLGDTSTLA DPTVVDNLIE DRPNK
//