ID ACSA_STRAW Reviewed; 652 AA.
AC Q82EL5;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 01-MAY-2013, entry version 65.
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=SAV_4599;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 /
OS NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Streptomycineae; Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 /
RC MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C.,
RA Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T.,
RA Kikuchi H., Shiba T., Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces
RT avermitilis: deducing the ability of producing secondary
RT metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 /
RC MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
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; BA000030; BAC72311.1; -; Genomic_DNA.
DR RefSeq; NP_825776.1; NC_003155.4.
DR ProteinModelPortal; Q82EL5; -.
DR SMR; Q82EL5; 15-644.
DR STRING; 227882.SAV_4599; -.
DR EnsemblBacteria; BAC72311; BAC72311; SAV_4599.
DR GeneID; 1211019; -.
DR KEGG; sma:SAV_4599; -.
DR PATRIC; 23723073; VBIStrAve112782_4916.
DR eggNOG; COG0365; -.
DR HOGENOM; HOG000229981; -.
DR KO; K01895; -.
DR OMA; ENAPFFK; -.
DR ProtClustDB; PRK00174; -.
DR BioCyc; SAVE227882:GJU1-4652-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 1 652 Acetyl-coenzyme A synthetase.
FT /FTId=PRO_0000208388.
FT REGION 412 417 Substrate binding (By similarity).
FT ACT_SITE 518 518 By similarity.
FT METAL 538 538 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 540 540 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 543 543 Magnesium; via carbonyl oxygen (By
FT similarity).
FT BINDING 312 312 Coenzyme A (By similarity).
FT BINDING 388 388 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 501 501 Substrate (By similarity).
FT BINDING 516 516 Substrate (By similarity).
FT BINDING 524 524 Coenzyme A (By similarity).
FT BINDING 527 527 Substrate (By similarity).
FT BINDING 586 586 Coenzyme A.
FT MOD_RES 611 611 N6-acetyllysine (By similarity).
SQ SEQUENCE 652 AA; 71091 MW; F9834F4332A3279A CRC64;
MSNESLANLL KEERRFAPPA DLAANANVTA EAYEQAKADR LGFWAEQARR LTWATEPTET
LDWSNPPFAK WFKDGKLNVA YNCVDRHVEA GHGDRVAIHF EGEPGDSRAI TYAELKDEVS
KAANALTELG VQKGDRVAVY LPMIPEAVVA MLACARIGAA HSVVFGGFSA DAIAARIKDA
DAKLVITADG GYRRGKPSAL KPAVDDAVSR GDGVEKVLVV RRTGQEVAWT EGRDVWWHEI
TAKQSAEHTP EAFDAEHPLF ILYTSGTTGK PKGILHTSGG YLTQTSYTHH AVFDLKPETD
VYWCTADIGW VTGHSYITYG PLSNGATQVM YEGTPDTPHQ GRFWEIVQKY GVTILYTAPT
AIRTFMKWGD DIPAKFDLSS LRVLGSVGEP INPEAWIWYR KHIGGDRTPI VDTWWQTETG
AMMISPLPGV TETKPGSAQR PLPGISATVV DDEAREVPNG GGGYLVLTEP WPSMLRTIWG
DDQRFLDTYW SRFEGKYFAG DGAKKDEDGD IWLLGRVDDV MLVSGHNIST TEVESALVSH
PSVAEAAVVG AADETTGQAI VAFVILRGTA NAEDDNLVAD LRNHVGTTLG PIAKPKRILP
VAELPKTRSG KIMRRLLRDV AENRALGDVT TLTDSSVMDL IQSKLPAAPS ED
//
