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 01-MAY-2013, entry version 41.
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; PPIKRSC; -.
DR ProtClustDB; PRK00174; -.
DR BioCyc; SBAL402882:GJ99-1795-MONOMER; -.
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: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; IPR024597; Acyl-CoA_synth_DUF3448.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR025110; DUF4009.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF11930; DUF3448; 1.
DR Pfam; PF13193; DUF4009; 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
//
