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Database: UniProt
Entry: A9M849
LinkDB: A9M849
Original site: A9M849 
ID   ACSA_BRUC2              Reviewed;         651 AA.
AC   A9M849;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   01-OCT-2014, entry version 46.
DE   RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000255|HAMAP-Rule:MF_01123};
DE            Short=AcCoA synthetase {ECO:0000255|HAMAP-Rule:MF_01123};
DE            Short=Acs {ECO:0000255|HAMAP-Rule:MF_01123};
DE            EC=6.2.1.1 {ECO:0000255|HAMAP-Rule:MF_01123};
DE   AltName: Full=Acetate--CoA ligase {ECO:0000255|HAMAP-Rule:MF_01123};
DE   AltName: Full=Acyl-activating enzyme {ECO:0000255|HAMAP-Rule:MF_01123};
GN   Name=acsA {ECO:0000255|HAMAP-Rule:MF_01123};
GN   OrderedLocusNames=BCAN_A1849;
OS   Brucella canis (strain ATCC 23365 / NCTC 10854).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=483179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23365 / NCTC 10854;
RA   Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J.,
RA   Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S.,
RA   Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K.,
RA   Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W.,
RA   Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C.,
RA   Munk C., Brettin T.S.;
RT   "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA
CC       (AcCoA), an essential intermediate at the junction of anabolic and
CC       catabolic pathways. AcsA undergoes a two-step reaction. In the
CC       first half reaction, AcsA combines acetate with ATP to form
CC       acetyl-adenylate (AcAMP) intermediate. In the second half
CC       reaction, it can then transfer the acetyl group from AcAMP to the
CC       sulfhydryl group of CoA, forming the product AcCoA.
CC       {ECO:0000255|HAMAP-Rule:MF_01123}.
CC   -!- CATALYTIC ACTIVITY: ATP + acetate + CoA = AMP + diphosphate +
CC       acetyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01123}.
CC   -!- COFACTOR: Magnesium. {ECO:0000255|HAMAP-Rule:MF_01123}.
CC   -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
CC       activates the enzyme. {ECO:0000255|HAMAP-Rule:MF_01123}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. {ECO:0000255|HAMAP-Rule:MF_01123}.
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DR   EMBL; CP000872; ABX62847.1; -; Genomic_DNA.
DR   RefSeq; YP_001593618.1; NC_010103.1.
DR   ProteinModelPortal; A9M849; -.
DR   SMR; A9M849; 17-648.
DR   STRING; 483179.BCAN_A1849; -.
DR   PRIDE; A9M849; -.
DR   EnsemblBacteria; ABX62847; ABX62847; BCAN_A1849.
DR   GeneID; 5785190; -.
DR   KEGG; bcs:BCAN_A1849; -.
DR   PATRIC; 17832405; VBIBruCan25663_1840.
DR   eggNOG; COG0365; -.
DR   HOGENOM; HOG000229981; -.
DR   KO; K01895; -.
DR   OMA; RRIFEPT; -.
DR   OrthoDB; EOG68WR2H; -.
DR   BioCyc; BCAN483179:GJ7I-1828-MONOMER; -.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR   HAMAP; MF_01123; Ac_CoA_synth; 1.
DR   InterPro; IPR011904; Ac_CoA_lig.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 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; Magnesium;
KW   Metal-binding; Nucleotide-binding.
FT   CHAIN         1    651       Acetyl-coenzyme A synthetase.
FT                                /FTId=PRO_1000084999.
FT   NP_BIND     387    389       ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   NP_BIND     411    416       ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   REGION      189    192       Coenzyme A binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01123}.
FT   METAL       537    537       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   METAL       539    539       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   METAL       542    542       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   BINDING     311    311       Coenzyme A. {ECO:0000255|HAMAP-
FT                                Rule:MF_01123}.
FT   BINDING     335    335       Coenzyme A. {ECO:0000255|HAMAP-
FT                                Rule:MF_01123}.
FT   BINDING     500    500       ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   BINDING     515    515       ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   BINDING     523    523       Coenzyme A; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   BINDING     526    526       ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   BINDING     586    586       Coenzyme A.
FT   MOD_RES     611    611       N6-acetyllysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01123}.
SQ   SEQUENCE   651 AA;  72731 MW;  7FB222A3EE6476CE CRC64;
     MSEKLYPVLP EAKKNTLIDN ETYLEWYEES VSDPDGFWAK HGRRIDWFKP FTKVKNTDFN
     GDVTIKWYED GVTNVSYNCI DRHLKSRGDK VAIIWEGDNP YIDKKITYRE LYENVCRMAN
     VLKKHGVKKG DRVTIYLPMI PEAAYAMLAC ARIGAVHSVV FAGFSPEALA GRIVDCESTF
     VITADEGVRG GKPVALKENT DTAIDIAAKQ YVMVNKVLVV RRTGGKVSWG RGRDLWYHQE
     VASVEPHCEP EPMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYASMTHQ YVFDYHDGEI
     YWCTADVGWV TGHSYIVYGP LANGATTLMF EGVPNFPDQG RFWEVVDKHH VNIFYTAPTA
     LRALMGAGDE FVTRSSRSTL RLLGSVGEPI NPEAWEWYYN VVGDQKCPIV DTWWQTENGG
     ILITPLPGAT DLKPGSATRP FFGVKPVLVD NEGNVQEGVA DGNLCISDSW PGQMRTVYGD
     HKRFIETYFS TYKGMYFSGD GCRRDEDGYY WITGRVDDVL NISGHRLGTA EIESALVSHH
     SVSEAAVVGY PHPIKGQGIY CYVTLMTGAD AQDPDELRKE LVQHVRKEIG PIATPDKIQF
     APGLPKTRSG KIMRRILRKI AEDEFGALGD TSTLADPGVV DDLIENRQNK K
//
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