ID   ACSA_BURTA              Reviewed;         660 AA.
AC   Q2T3N9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-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=BTH_II2017;
OS   Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 /
OS   CIP 106301).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R.,
RA   Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D.,
RA   Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P.,
RA   Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F.,
RA   Roberts K., Hatch B., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) 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.
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DR   EMBL; CP000085; ABC35414.1; -; Genomic_DNA.
DR   RefSeq; YP_440210.1; -.
DR   GeneID; 3846624; -.
DR   GenomeReviews; CP000085_GR; BTH_II2017.
DR   KEGG; bte:BTH_II2017; -.
DR   TIGR; BTH_II2017; -.
DR   HOGENOM; Q2T3N9; -.
DR   OMA; Q2T3N9; ETASEHC.
DR   BioCyc; BTHA271848:BTH_II2017-MON; -.
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    660       Acetyl-coenzyme A synthetase.
FT                                /FTId=PRO_1000065286.
FT   ACT_SITE    530    530       By similarity.
FT   MOD_RES     625    625       N6-acetyllysine (By similarity).
SQ   SEQUENCE   660 AA;  72217 MW;  79A3CEB29447DD7D CRC64;
     MSAIESVLHE RRQFAPPAAV EKAAAISGMA AYRALAEEAE RDYEGFWARL ARETLEWRKP
     FGKALDETNA PFYKWFDDGE LNASYNCLDR HVAAGLGERI AVIFEADDGT VARVTYADLL
     ARVSRFANAL KKRGIGRGDR VVIYIPMSVE GIVAMQACAR IGATHSVVFG GFSSKSLHER
     IVDVGATALV TADEQMRGGK TLPLKSIADE ALAMGGCDAV KTVVVYRRTG GNVDWHAGRD
     VWMHEIVANE SDACEPEWVG AEHPLFILYT SGSTGKPKGV QHSTAGYLLW VAQTMKWTFD
     WKPDDVFWCT ADIGWVTGHS YITYGPLAVG ATQVVFEGVP TYPNAGRFWK MIGDHKVSVF
     YTAPTAIRSL IKAAEADEHV HPKSYDLSSL RIIGTVGEPI NPEAWIWYHK NVGQERCPIV
     DTWWQTETGG HMITPLPGAT PTVPGSCTLP LPGIMAAVVD ETGQDVPNGQ GGILVVKRPW
     PAMARTIWGD PERFKKSYFP DELGGRLYLA GDGTVRDKET GYFTIMGRID DVLNVSGHRL
     GTMEIESALV SHELVAEAAV VGRPDDTTGE AVVAFVVLKR SRPEGEEAAA LAKTLRDWVG
     KEIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEAI TQDTSTLENP AILEQLAEVR
//