ID   ACSA_BARQU              Reviewed;         652 AA.
AC   Q6FYL4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 30.
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=BQ12330;
OS   Bartonella quintana (Rochalimaea quintana).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=803;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Toulouse;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897700; CAF26692.1; -; Genomic_DNA.
DR   RefSeq; YP_032761.1; -.
DR   GeneID; 2866783; -.
DR   GenomeReviews; BX897700_GR; BQ12330.
DR   KEGG; bqu:BQ12330; -.
DR   NMPDR; fig|283165.1.peg.1031; -.
DR   HOGENOM; Q6FYL4; -.
DR   OMA; Q6FYL4; DSSVINE.
DR   BioCyc; BQUI283165:BQ12330-MON; -.
DR   BRENDA; 6.2.1.1; 292235.
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    652       Acetyl-coenzyme A synthetase.
FT                                /FTId=PRO_1000065271.
FT   ACT_SITE    517    517       By similarity.
FT   MOD_RES     609    609       N6-acetyllysine (By similarity).
SQ   SEQUENCE   652 AA;  73513 MW;  B1D59C8E4037ED67 CRC64;
     MSEKIYPVPT DIKKNALINE ETYQKWYRES INDPEAFWAK HGQRIEWFKP YTKVKNTSFN
     GDVSIQWYED GITNVAYNCI DRHLKNSGNH IALIWEGNNP YHDKKITYNE LYEHVCRFAN
     ILKNHGVKKG DRVTIYLPMI PEAAYAMLAC ARIGAIHSVI FAGFSSEAIA DRIVDCKSTF
     IITADQGLRG GKLIKLKNNI DHAIDIAARR GVHVNQVLVI RRTSGTIDWV KGRDFWYHEE
     ISHAKTDCPA EMMNAEDPLF ILYTSGSTGK PKGVLHTTAG YLVYVSMTHQ YVFDYHPGEI
     YWCTADIGWI SGHSYLIYGP LCNGATTLMF EGIPTFPDQG RFWEIVDKHK VNTLYTAPTA
     IRALMGAGNS FVEHSKRTSL RLLGTVGEPI NPEAWKWFYH TVGDNRCPIL DTWWQTETGG
     HMITPLPGAT QLKAGSATHP FFGVQLQIID GEGNVLEGEA EGNLCIIDSW PGQMRTLYND
     HERFIETYFS TYKGKYFTGD GCKRDNDGYY WITGRIDDIL NVSGHRLGTA EIESALVSHP
     AISEAAVVGY PHPIKGQGIY SFVTLMEGIT PSEELYKDLI QHVKKEIGSI ALLDKIQFTP
     QLPKTRSGKI MRRILRKIAE NDFDNLGDIS TLAEPQVVDD LIANRQNTEA TA
//