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Protein

Acetyl-coenzyme A synthetase

Gene

AcCoAS

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Activates acetate so that it can be used for lipid synthesis or for energy generation.By similarity

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.By similarity

GO - Molecular functioni

GO - Biological processi

  • acetyl-CoA biosynthetic process from acetate Source: InterPro
  • acetyl-CoA metabolic process Source: FlyBase
  • behavioral response to ethanol Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-71384. Ethanol oxidation.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetase (EC:6.2.1.1)
Alternative name(s):
Acetate--CoA ligase
Acetyl-CoA synthetase
Short name:
ACS
Short name:
AceCS
Acyl-activating enzyme
Gene namesi
Name:AcCoAS
ORF Names:CG9390
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0012034. AcCoAS.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 670670Acetyl-coenzyme A synthetasePRO_0000208425Add
BLAST

Proteomic databases

PaxDbiQ9VP61.
PRIDEiQ9VP61.

Expressioni

Gene expression databases

BgeeiQ9VP61.
ExpressionAtlasiQ9VP61. differential.
GenevisibleiQ9VP61. DM.

Interactioni

Protein-protein interaction databases

BioGridi65596. 2 interactions.
MINTiMINT-1328607.
STRINGi7227.FBpp0078067.

Structurei

3D structure databases

ProteinModelPortaliQ9VP61.
SMRiQ9VP61. Positions 24-665.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1175. Eukaryota.
COG0365. LUCA.
InParanoidiQ9VP61.
KOiK01895.
OrthoDBiEOG77T140.
PhylomeDBiQ9VP61.

Family and domain databases

InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform ACurated (identifier: Q9VP61-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPAEKSIYDP NPAISQNAYI SSFEEYQKFY QESLDNPAEF WSRVAKQFHW
60 70 80 90 100
ETPADQDKFL KYNFNISKGP ISIKWMEGAS TNLCYNLLDR NVRNGLGDQI
110 120 130 140 150
AYYWEGNHPD DYSRGLTYRK LLEEVCRFAN VLKDHGIRKG DRVSIYMPMI
160 170 180 190 200
LELPIAMLAC ARIGAVHSIV FAGFSPDSLA ERMFDCKAKL LITADGAWRG
210 220 230 240 250
EKPLYLKALC DTALEKVEEM GHSVEKCIVV SHLKRVTPCQ PDHVEEEIPW
260 270 280 290 300
TDDRDYWWHE EMEDKEPACY PEWMDAEDPL FMLYTSGSTG KPKGVLHTTA
310 320 330 340 350
GYLLYAATTF KIVFDYKPGD IYWCTADVGW ITGHTYVVYG PLANGATSVI
360 370 380 390 400
FEGTPFFPGN DRYWSVIDKY KVTQFYTAPT AIRALMKFGE GPVLKHNLSG
410 420 430 440 450
LKVLGSVGEP INPEAWLWYY KYIGKEQCSI VDTFWQTETG GHVITPLPGA
460 470 480 490 500
TPMKPGSASF PFFGVKPTLL DECGIEIKGE GEGYLVFSQP WPGMMRTLYN
510 520 530 540 550
NHERFEDTYF SKFPGYYCTG DGARRDADGY LWITGRVDDM LNVSGHLMST
560 570 580 590 600
AEVESVLTEH PRVAESAVVS RPHPVKGECL YCFITPNENE VFDQKLISDL
610 620 630 640 650
KKMVRERIGP FAMPDVIQNA PGLPKTRSGK IMRRVLRKIA VNDRNVGDTS
660 670
TLADEQIVEQ LFANRPVEAK
Length:670
Mass (Da):75,960
Last modified:May 1, 2000 - v1
Checksum:iCE24364755CDBFFC
GO
Isoform BCurated (identifier: Q9VP61-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-146: Missing.

Show »
Length:524
Mass (Da):58,829
Checksum:i63D8E2976CC09CAA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti227 – 2271C → S in CAA86738 (Ref. 1) Curated
Sequence conflicti326 – 3261A → G in AAF51695 (PubMed:10731132).Curated
Sequence conflicti326 – 3261A → G in AAF51696 (PubMed:10731132).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 146146Missing in isoform B. 1 PublicationVSP_008310Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46786 mRNA. Translation: CAA86738.1. Sequence problems.
AE014296 Genomic DNA. Translation: AAF51695.2.
AE014296 Genomic DNA. Translation: AAF51696.3.
AY089540 mRNA. Translation: AAL90278.1.
BT001456 mRNA. Translation: AAN71211.1.
PIRiS52154.
RefSeqiNP_001014599.2. NM_001014599.2.
NP_524196.2. NM_079472.3.
NP_730611.1. NM_168894.3.
UniGeneiDm.7388.

Genome annotation databases

GeneIDi40348.
KEGGidme:Dmel_CG9390.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46786 mRNA. Translation: CAA86738.1. Sequence problems.
AE014296 Genomic DNA. Translation: AAF51695.2.
AE014296 Genomic DNA. Translation: AAF51696.3.
AY089540 mRNA. Translation: AAL90278.1.
BT001456 mRNA. Translation: AAN71211.1.
PIRiS52154.
RefSeqiNP_001014599.2. NM_001014599.2.
NP_524196.2. NM_079472.3.
NP_730611.1. NM_168894.3.
UniGeneiDm.7388.

3D structure databases

ProteinModelPortaliQ9VP61.
SMRiQ9VP61. Positions 24-665.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65596. 2 interactions.
MINTiMINT-1328607.
STRINGi7227.FBpp0078067.

Proteomic databases

PaxDbiQ9VP61.
PRIDEiQ9VP61.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi40348.
KEGGidme:Dmel_CG9390.

Organism-specific databases

CTDi40348.
FlyBaseiFBgn0012034. AcCoAS.

Phylogenomic databases

eggNOGiKOG1175. Eukaryota.
COG0365. LUCA.
InParanoidiQ9VP61.
KOiK01895.
OrthoDBiEOG77T140.
PhylomeDBiQ9VP61.

Enzyme and pathway databases

ReactomeiR-DME-71384. Ethanol oxidation.

Miscellaneous databases

GenomeRNAii40348.
PROiQ9VP61.

Gene expression databases

BgeeiQ9VP61.
ExpressionAtlasiQ9VP61. differential.
GenevisibleiQ9VP61. DM.

Family and domain databases

InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A Drosophila melanogaster acetyl-CoA-synthetase gene."
    Russell S.R., Heimbeck G.M., Carpenter A.T., Ashburner M.
    Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM B).
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication and Ovary1 Publication.

Entry informationi

Entry nameiACSA_DROME
AccessioniPrimary (citable) accession number: Q9VP61
Secondary accession number(s): Q24226, Q8IH30, Q9VP60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.