ID   ACSA_LEPBL              Reviewed;         654 AA.
AC   Q056J9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   16-JUN-2009, entry version 18.
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=LBL_0125;
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain L550).
OC   Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A.,
RA   Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P.,
RA   Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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; CP000348; ABJ77746.1; -; Genomic_DNA.
DR   RefSeq; YP_796679.1; -.
DR   GeneID; 4408535; -.
DR   GenomeReviews; CP000348_GR; LBL_0125.
DR   KEGG; lbl:LBL_0125; -.
DR   OMA; Q056J9; TGGYNLY.
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    654       Acetyl-coenzyme A synthetase.
FT                                /FTId=PRO_1000085002.
FT   ACT_SITE    521    521       By similarity.
FT   MOD_RES     613    613       N6-acetyllysine (By similarity).
SQ   SEQUENCE   654 AA;  73402 MW;  2A51CC717429B00A CRC64;
     MAKERIVLPS AEFKKNSNIT LKDYKSLYKE SIENPNKFWA KEANRLTWFK KWTKVLNHDF
     KNAKVEWFKG GKLNVSYNCL DRHISTPLKN KAALIWEGDN PSESKVLTYY DVYREVNRFA
     NVLKKYGVKK GDRVLVYLPM IPELAITILA CTRIGAIHSV VFGGFSPEAL QSRIDDCKPK
     LIVTADGGFR GGKPIELKRN VDIALEKSKE DVKTVIVVRR TGNESGLVWK DGRDYWYHFL
     ISDPDLSPYC KPESMDAEDP LFILYTSGST GKPKGVLHTT GGYLLGVNLT FHYVFDIKPE
     DTYWCTADIG WVTGHSYLVY GPLSNGASSV MFEGVPSYPD AGRFWDVIDK YGVNIFYTAP
     TAIRALMREG LTHVQKRNLS SLRLLGSVGE PINPEAWEWY FKIIGKEKCP IVDTWWQTET
     GSIMITALPG AIPQKPGSAT LPFFGVQPVL VDNDGKEIND KGEVSGNLCI KSPWPSMMRG
     VYGDSKRFFD TYFSQFKGYY FTGDGARRDK DGYYWITGRV DDVINVSGHR IGSAEVESAL
     VENRSVAEAA VVGFPHDIKG QGIYAYVTVK EGIATNDTLK KELVAIVEKV IGKIARPDVI
     HWAPSLPKTR SGKIMRRILR KIASGEFEGL GDTSTLADPS VVQKLIEDKR KFHS
//