ID   ACSA_CHLTE              Reviewed;         659 AA.
AC   Q8KBY0;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2003, sequence version 2.
DT   16-JUN-2009, entry version 39.
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; OrderedLocusNames=CT1652;
OS   Chlorobium tepidum.
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=1097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / TLS;
RX   MEDLINE=22103685; PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M.,
RA   Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F.,
RA   Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P.,
RA   Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B.,
RA   Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M.,
RA   Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a
RT   photosynthetic, anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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; AE006470; AAM72877.1; -; Genomic_DNA.
DR   RefSeq; NP_662535.1; -.
DR   HSSP; Q8ZKF6; 1PG4.
DR   GeneID; 1006138; -.
DR   GenomeReviews; AE006470_GR; CT1652.
DR   KEGG; cte:CT1652; -.
DR   NMPDR; fig|194439.1.peg.1629; -.
DR   TIGR; CT1652; -.
DR   HOGENOM; Q8KBY0; -.
DR   BioCyc; CTEP194439:CT_1652-MON; -.
DR   BRENDA; 6.2.1.1; 189605.
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    659       Acetyl-coenzyme A synthetase.
FT                                /FTId=PRO_0000208360.
FT   ACT_SITE    529    529       By similarity.
FT   MOD_RES     621    621       N6-acetyllysine (By similarity).
SQ   SEQUENCE   659 AA;  73576 MW;  2BB84C9AB13EA034 CRC64;
     MATEQTKGQS SESISSVLSE RRKFPPPEAF SSQSHISSME QYEKLYADAA ADPDKYWGDL
     AEQFHWFKKW DSVLEWNAPY AKWFNGGTTN IAYNCLDVHV GSWRKNKAAI IWEGEEGNER
     ILTYGELHRQ VSKFANVLKI AGIKPGDKVA IYMGMVPELV IAVLACARVG AVHNVIFAGF
     AAHAITERVN DSRAKIVICA DGTRRRGSTI NLKNIVDEAI INTPSVKNVI VLKVTGEEIH
     MHDGMDHWWH DLMGLAVDEC EPAQVDSEHP LFLLYTSGST GKPKGILHTT AGYMVHAASS
     FKYVFDIKDE DIYFCTADIG WITGHTYIIY GPLLNGATVF MYEGAPNYPQ WDRFWDIINR
     HKITILYTAP TAIRAFIRAG NEWVTKHDLS SLRLLGTVGE PINPEAWMWY HKYVGQEKCP
     IVDTWWQTET GGIMISPMPG ATPTKPGTAT RPLPGIMVDV VRKDGTPCNA NEGGYLVVKR
     PWPSMLRTIY GDNERYEKTY WSEFPGMYFT GDGARKDDDG YIWIMGRVDD VVNVSGHRLG
     TSEVESALVS HEAVAEAAVV SRPDEIKGNA LVAFVTLKDG YEGDAKLRDS LGKHVAKEIG
     AIAKPDEIRW AKGLPKTRSG KIMRRLLREL ATSNEIKGDV TTLEDLGVIE NLREQEDEG
//