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Database: UniProt
Entry: Q82EL5
LinkDB: Q82EL5
Original site: Q82EL5 
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   26-NOV-2014, entry version 75.
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=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.
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:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={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; 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   PRIDE; Q82EL5; -.
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; SPWLNGA; -.
DR   OrthoDB; EOG68WR2H; -.
DR   BioCyc; SAVE227882:GJU1-4652-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; Reference proteome.
FT   CHAIN         1    652       Acetyl-coenzyme A synthetase.
FT                                /FTId=PRO_0000208388.
FT   NP_BIND     388    390       ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   NP_BIND     412    417       ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   REGION      193    196       Coenzyme A binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01123}.
FT   METAL       538    538       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   METAL       540    540       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   METAL       543    543       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   BINDING     312    312       Coenzyme A. {ECO:0000255|HAMAP-
FT                                Rule:MF_01123}.
FT   BINDING     501    501       ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   BINDING     516    516       ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   BINDING     524    524       Coenzyme A; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   MOD_RES     611    611       N6-acetyllysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01123}.
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
//
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