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 08-NOV-2023, entry version 144.
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; 7227-FBpp0078067; -.
DR GeneID; 40348; -.
DR KEGG; dme:Dmel_CG9390; -.
DR AGR; FB:FBgn0012034; -.
DR CTD; 40348; -.
DR FlyBase; FBgn0012034; AcCoAS.
DR VEuPathDB; VectorBase:FBgn0012034; -.
DR eggNOG; KOG1175; Eukaryota.
DR InParanoid; Q9VP61; -.
DR OrthoDB; 144557at2759; -.
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 GO; GO:0045494; P:photoreceptor cell maintenance; IGI:FlyBase.
DR CDD; cd05966; ACS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR InterPro; IPR042099; ANL_N_sf.
DR NCBIfam; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR24095:SF244; ACETYL-COENZYME A SYNTHETASE; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 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
//
