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ACSA_DROME
ID   ACSA_DROME              Reviewed;         670 AA.
AC   Q9VP61; Q24226; Q8IH30; Q9VP60;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Acetyl-coenzyme A synthetase;
DE            EC=6.2.1.1;
DE   AltName: Full=Acetate--CoA ligase;
DE   AltName: Full=Acetyl-CoA synthetase;
DE            Short=ACS;
DE            Short=AceCS;
DE   AltName: Full=Acyl-activating enzyme;
GN   Name=AcCoAS; ORFNames=CG9390;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000312|EMBL:AAL90278.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE (ISOFORM B).
RA   Russell S.R., Heimbeck G.M., Carpenter A.T., Ashburner M.;
RT   "A Drosophila melanogaster acetyl-CoA-synthetase gene.";
RL   Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3] {ECO:0000305}
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC   STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC   TISSUE=Embryo {ECO:0000269|PubMed:12537569}, and
RC   Ovary {ECO:0000269|PubMed:12537569};
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: Activates acetate so that it can be used for lipid synthesis
CC       or for energy generation. {ECO:0000250|UniProtKB:Q9NR19}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:456215; EC=6.2.1.1;
CC         Evidence={ECO:0000250|UniProtKB:Q9NR19};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A {ECO:0000305};
CC         IsoId=Q9VP61-1; Sequence=Displayed;
CC       Name=B {ECO:0000305};
CC         IsoId=Q9VP61-2; Sequence=VSP_008310;
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; Z46786; CAA86738.1; ALT_SEQ; mRNA.
DR   EMBL; AE014296; AAF51695.2; -; Genomic_DNA.
DR   EMBL; AE014296; AAF51696.3; -; Genomic_DNA.
DR   EMBL; AY089540; AAL90278.1; -; mRNA.
DR   EMBL; BT001456; AAN71211.1; -; mRNA.
DR   PIR; S52154; S52154.
DR   RefSeq; NP_001014599.2; NM_001014599.2.
DR   RefSeq; NP_524196.2; NM_079472.3.
DR   RefSeq; NP_730611.1; NM_168894.3.
DR   AlphaFoldDB; Q9VP61; -.
DR   SMR; Q9VP61; -.
DR   BioGRID; 65596; 4.
DR   STRING; 7227.FBpp0078067; -.
DR   PaxDb; Q9VP61; -.
DR   PRIDE; Q9VP61; -.
DR   GeneID; 40348; -.
DR   KEGG; dme:Dmel_CG9390; -.
DR   CTD; 40348; -.
DR   FlyBase; FBgn0012034; AcCoAS.
DR   VEuPathDB; VectorBase:FBgn0012034; -.
DR   eggNOG; KOG1175; Eukaryota.
DR   InParanoid; Q9VP61; -.
DR   PhylomeDB; Q9VP61; -.
DR   Reactome; R-DME-71384; Ethanol oxidation.
DR   BioGRID-ORCS; 40348; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 40348; -.
DR   PRO; PR:Q9VP61; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   ExpressionAtlas; Q9VP61; baseline and differential.
DR   Genevisible; Q9VP61; DM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IBA:GO_Central.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031955; F:short-chain fatty acid-CoA ligase activity; TAS:FlyBase.
DR   GO; GO:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR   GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; TAS:FlyBase.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR011904; Ac_CoA_lig.
DR   InterPro; IPR032387; ACAS_N.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF16177; ACAS_N; 1.
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   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..670
FT                   /note="Acetyl-coenzyme A synthetase"
FT                   /id="PRO_0000208425"
FT   VAR_SEQ         1..146
FT                   /note="Missing (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:12537569"
FT                   /id="VSP_008310"
FT   CONFLICT        227
FT                   /note="C -> S (in Ref. 1; CAA86738)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        326
FT                   /note="A -> G (in Ref. 2; AAF51695/AAF51696)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   670 AA;  75960 MW;  CE24364755CDBFFC CRC64;
     MPAEKSIYDP NPAISQNAYI SSFEEYQKFY QESLDNPAEF WSRVAKQFHW ETPADQDKFL
     KYNFNISKGP ISIKWMEGAS TNLCYNLLDR NVRNGLGDQI AYYWEGNHPD DYSRGLTYRK
     LLEEVCRFAN VLKDHGIRKG DRVSIYMPMI LELPIAMLAC ARIGAVHSIV FAGFSPDSLA
     ERMFDCKAKL LITADGAWRG EKPLYLKALC DTALEKVEEM GHSVEKCIVV SHLKRVTPCQ
     PDHVEEEIPW TDDRDYWWHE EMEDKEPACY PEWMDAEDPL FMLYTSGSTG KPKGVLHTTA
     GYLLYAATTF KIVFDYKPGD IYWCTADVGW ITGHTYVVYG PLANGATSVI FEGTPFFPGN
     DRYWSVIDKY KVTQFYTAPT AIRALMKFGE GPVLKHNLSG LKVLGSVGEP INPEAWLWYY
     KYIGKEQCSI VDTFWQTETG GHVITPLPGA TPMKPGSASF PFFGVKPTLL DECGIEIKGE
     GEGYLVFSQP WPGMMRTLYN NHERFEDTYF SKFPGYYCTG DGARRDADGY LWITGRVDDM
     LNVSGHLMST AEVESVLTEH PRVAESAVVS RPHPVKGECL YCFITPNENE VFDQKLISDL
     KKMVRERIGP FAMPDVIQNA PGLPKTRSGK IMRRVLRKIA VNDRNVGDTS TLADEQIVEQ
     LFANRPVEAK
 
 
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