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Database: UniProt
Entry: A6WM52
LinkDB: A6WM52
Original site: A6WM52 
ID   ACSA_SHEB8              Reviewed;         650 AA.
AC   A6WM52;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   19-FEB-2014, entry version 45.
DE   RecName: Full=Acetyl-coenzyme A synthetase;
DE            Short=AcCoA synthetase;
DE            Short=Acs;
DE            EC=6.2.1.1;
DE   AltName: Full=Acetate--CoA ligase;
DE   AltName: Full=Acyl-activating enzyme;
GN   Name=acsA; OrderedLocusNames=Shew185_1748;
OS   Shewanella baltica (strain OS185).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=402882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS185;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Brettar I., Rodrigues J.,
RA   Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS185.";
RL   Submitted (JUL-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 (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + acetate + CoA = AMP + diphosphate +
CC       acetyl-CoA.
CC   -!- COFACTOR: Magnesium (By similarity).
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; CP000753; ABS07891.1; -; Genomic_DNA.
DR   RefSeq; YP_001365954.1; NC_009665.1.
DR   ProteinModelPortal; A6WM52; -.
DR   SMR; A6WM52; 7-645.
DR   STRING; 402882.Shew185_1748; -.
DR   EnsemblBacteria; ABS07891; ABS07891; Shew185_1748.
DR   GeneID; 5371220; -.
DR   KEGG; sbm:Shew185_1748; -.
DR   PATRIC; 23460216; VBISheBal127872_1928.
DR   eggNOG; COG0365; -.
DR   HOGENOM; HOG000229981; -.
DR   KO; K01895; -.
DR   OMA; WVMGRVD; -.
DR   OrthoDB; EOG68WR2H; -.
DR   ProtClustDB; PRK00174; -.
DR   BioCyc; SBAL402882:GJ99-1795-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    650       Acetyl-coenzyme A synthetase.
FT                                /FTId=PRO_1000065317.
FT   REGION      411    416       Substrate binding (By similarity).
FT   ACT_SITE    517    517       By similarity.
FT   METAL       537    537       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       539    539       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       542    542       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     311    311       Coenzyme A (By similarity).
FT   BINDING     335    335       Coenzyme A (By similarity).
FT   BINDING     387    387       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     500    500       Substrate (By similarity).
FT   BINDING     515    515       Substrate (By similarity).
FT   BINDING     523    523       Coenzyme A (By similarity).
FT   BINDING     526    526       Substrate (By similarity).
FT   BINDING     584    584       Coenzyme A.
FT   MOD_RES     609    609       N6-acetyllysine (By similarity).
SQ   SEQUENCE   650 AA;  72396 MW;  0A9257FD9BB53BF8 CRC64;
     MSSQSLYKVS GNIAANALVN NDKYKTMYQE SIVNPEGFWR EHGKRIDWIK PYTKIKKTSF
     DDHNLSINWF YDGTLNASAN CLDRHLAEHS DRVAIIWEGD NASEQRKITY GELHADVCKF
     ANALRSQGVR RGDIVTIYMP MVPEAAVAML ACARIGAVHS VVFGGFSPDS IASRVIDGKS
     KVIITSDEGM RGGRAIPLKR NIDDALKNPD VTTVEKVIVL KRTGGKVDWV EGRDVWWHSL
     METASEYCQP EEMDAEAPLF LLYTSGSTGN PKGVLHTTGG YMVYASMTHE YVFDYKAGEV
     YWCTADVGWI TGHSYMVYGP LANGATVLIH EGVPNHPSPA RLGEMIDRHK VSILYTAPTL
     IRALMAEGKQ HFDKFDGSSL RIMGSVGEPI NPEAWRWYHE VIGHEHCPIV DTWWQTETGG
     ILITPLPGAT DTKPGSATRP FFGVQPALVD NMGNILEGEN EGNLVLLDSW PGQMRTVYGD
     HERFVLTYFK TFRGMYFTGD GARRDEDGYY WITGRVDDVI NVSGHRLGTA EVESALVSHE
     LVAEAAVVGY PHDIKGQGIY AYVTLTRGTE ETEELRQELR QWVRKEIGAL ATPDLIQWAT
     GLPKTRSGKI MRRFLRKIAA NEVTNLGDAS TLADPAVIET LIESRLNRTE
//
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