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Protein

Nucleoside diphosphate kinase

Gene

awd

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

Functioni

Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.3 Publications

Catalytic activityi

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.1 Publication

Cofactori

Mg2+1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei13 – 131ATP
Binding sitei61 – 611ATP
Binding sitei89 – 891ATP
Binding sitei95 – 951ATP
Binding sitei106 – 1061ATP
Binding sitei116 – 1161ATP
Active sitei119 – 1191Pros-phosphohistidine intermediate

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • GTP binding Source: FlyBase
  • kinase activity Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • microtubule binding Source: FlyBase
  • nucleoside diphosphate kinase activity Source: UniProtKB

GO - Biological processi

  • adherens junction organization Source: FlyBase
  • CTP biosynthetic process Source: UniProtKB
  • epithelial cell migration, open tracheal system Source: FlyBase
  • establishment or maintenance of polarity of follicular epithelium Source: FlyBase
  • GTP biosynthetic process Source: UniProtKB
  • microtubule-based process Source: FlyBase
  • mitotic nuclear division Source: FlyBase
  • nucleoside diphosphate phosphorylation Source: FlyBase
  • nucleotide metabolic process Source: UniProtKB
  • open tracheal system development Source: FlyBase
  • peptidyl-serine phosphorylation Source: FlyBase
  • protein autophosphorylation Source: FlyBase
  • protein phosphorylation Source: FlyBase
  • regulation of tube architecture, open tracheal system Source: FlyBase
  • UTP biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoside diphosphate kinase (EC:2.7.4.6)
Short name:
NDK
Short name:
NDP kinase
Alternative name(s):
Abnormal wing disks protein
Killer of prune protein
Gene namesi
Name:awd
Synonyms:K-pn
ORF Names:CG2210
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0000150. awd.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • microtubule Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • nuclear microtubule Source: UniProtKB
  • plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi15 – 151D → N in KRm5; lethal due to loss of phosphorylated active site intermediate; when associated with S-97. 1 Publication
Mutagenesisi89 – 891R → C in KRn3; lethal due to loss of phosphorylated active site intermediate; when associated with S-97. 1 Publication
Mutagenesisi97 – 971P → S: Killer of prune mutation. Conditionally dominant lethal mutation in individuals with a null mutation in the prune gene. 1 Publication
Mutagenesisi106 – 1061R → C in KRm7; lethal due to loss of phosphorylated active site intermediate; when associated with S-97. 1 Publication
Mutagenesisi122 – 1221D → N in KRm12; lethal due to lower enzyme activity; when associated with S-97. 1 Publication
Mutagenesisi127 – 1271A → T in KRm9; lower enzyme activity; when associated with S-97.
Mutagenesisi130 – 1301E → K in KRm4; lethal due to loss of catalytic activity; when associated with S-97. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 153152Nucleoside diphosphate kinasePRO_0000137108Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei126 – 1261Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP08879.
PRIDEiP08879.

PTM databases

iPTMnetiP08879.

Expressioni

Gene expression databases

BgeeiP08879.
ExpressionAtlasiP08879. differential.
GenevisibleiP08879. DM.

Interactioni

Subunit structurei

Homohexamer.1 Publication

GO - Molecular functioni

  • microtubule binding Source: FlyBase

Protein-protein interaction databases

BioGridi68580. 102 interactions.
DIPiDIP-20572N.
IntActiP08879. 3 interactions.
MINTiMINT-936330.
STRINGi7227.FBpp0085223.

Structurei

Secondary structure

1
153
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Beta strandi7 – 126Combined sources
Helixi14 – 185Combined sources
Helixi22 – 3211Combined sources
Beta strandi35 – 395Combined sources
Helixi46 – 527Combined sources
Helixi54 – 563Combined sources
Helixi62 – 698Combined sources
Beta strandi74 – 818Combined sources
Helixi84 – 929Combined sources
Helixi97 – 993Combined sources
Helixi105 – 1095Combined sources
Helixi113 – 1153Combined sources
Beta strandi118 – 1203Combined sources
Helixi124 – 13411Combined sources
Helixi137 – 1393Combined sources
Helixi148 – 1514Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NDLX-ray2.40A/B/C1-153[»]
1NSQX-ray2.18A/B/C1-153[»]
3WX8X-ray1.95A/B/C1-153[»]
ProteinModelPortaliP08879.
SMRiP08879. Positions 2-153.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08879.

Family & Domainsi

Sequence similaritiesi

Belongs to the NDK family.Curated

Phylogenomic databases

eggNOGiKOG0888. Eukaryota.
COG0105. LUCA.
GeneTreeiENSGT00760000119146.
InParanoidiP08879.
KOiK00940.
OrthoDBiEOG7GJ6FG.
PhylomeDBiP08879.

Family and domain databases

HAMAPiMF_00451. NDP_kinase.
InterProiIPR001564. Nucleoside_diP_kinase.
IPR023005. Nucleoside_diP_kinase_AS.
[Graphical view]
PfamiPF00334. NDK. 1 hit.
[Graphical view]
PRINTSiPR01243. NUCDPKINASE.
SMARTiSM00562. NDK. 1 hit.
[Graphical view]
PROSITEiPS00469. NDP_KINASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08879-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAANKERTFI MVKPDGVQRG LVGKIIERFE QKGFKLVALK FTWASKELLE
60 70 80 90 100
KHYADLSARP FFPGLVNYMN SGPVVPMVWE GLNVVKTGRQ MLGATNPADS
110 120 130 140 150
LPGTIRGDFC IQVGRNIIHG SDAVESAEKE IALWFNEKEL VTWTPAAKDW

IYE
Length:153
Mass (Da):17,170
Last modified:January 23, 2007 - v3
Checksum:iE98765853255445E
GO

Sequence cautioni

The sequence AAF57188.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Mass spectrometryi

Molecular mass is 17082.3±0.6 Da from positions 2 - 153. Determined by ESI. Acetylated.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13107 mRNA. Translation: CAA31500.1.
AE014297 Genomic DNA. Translation: AAF57188.3. Different initiation.
AY113576 mRNA. Translation: AAM29581.1.
PIRiS01908.
RefSeqiNP_001287624.1. NM_001300695.1.
NP_001287625.1. NM_001300696.1.
NP_476761.3. NM_057413.4.
UniGeneiDm.6904.

Genome annotation databases

EnsemblMetazoaiFBtr0346611; FBpp0312191; FBgn0000150.
GeneIDi43739.
KEGGidme:Dmel_CG2210.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13107 mRNA. Translation: CAA31500.1.
AE014297 Genomic DNA. Translation: AAF57188.3. Different initiation.
AY113576 mRNA. Translation: AAM29581.1.
PIRiS01908.
RefSeqiNP_001287624.1. NM_001300695.1.
NP_001287625.1. NM_001300696.1.
NP_476761.3. NM_057413.4.
UniGeneiDm.6904.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NDLX-ray2.40A/B/C1-153[»]
1NSQX-ray2.18A/B/C1-153[»]
3WX8X-ray1.95A/B/C1-153[»]
ProteinModelPortaliP08879.
SMRiP08879. Positions 2-153.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68580. 102 interactions.
DIPiDIP-20572N.
IntActiP08879. 3 interactions.
MINTiMINT-936330.
STRINGi7227.FBpp0085223.

PTM databases

iPTMnetiP08879.

Proteomic databases

PaxDbiP08879.
PRIDEiP08879.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0346611; FBpp0312191; FBgn0000150.
GeneIDi43739.
KEGGidme:Dmel_CG2210.

Organism-specific databases

CTDi43739.
FlyBaseiFBgn0000150. awd.

Phylogenomic databases

eggNOGiKOG0888. Eukaryota.
COG0105. LUCA.
GeneTreeiENSGT00760000119146.
InParanoidiP08879.
KOiK00940.
OrthoDBiEOG7GJ6FG.
PhylomeDBiP08879.

Enzyme and pathway databases

ReactomeiR-DME-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

ChiTaRSiawd. fly.
EvolutionaryTraceiP08879.
GenomeRNAii43739.
PROiP08879.

Gene expression databases

BgeeiP08879.
ExpressionAtlasiP08879. differential.
GenevisibleiP08879. DM.

Family and domain databases

HAMAPiMF_00451. NDP_kinase.
InterProiIPR001564. Nucleoside_diP_kinase.
IPR023005. Nucleoside_diP_kinase_AS.
[Graphical view]
PfamiPF00334. NDK. 1 hit.
[Graphical view]
PRINTSiPR01243. NUCDPKINASE.
SMARTiSM00562. NDK. 1 hit.
[Graphical view]
PROSITEiPS00469. NDP_KINASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the lethal interaction between the prune and Killer of prune mutations of Drosophila."
    Biggs J., Tripoulas N., Hersperger E., Dearolf C., Shearn A.
    Genes Dev. 2:1333-1343(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  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: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    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].
    Strain: Berkeley.
    Tissue: Head.
  5. "Post-translational processing of Drosophila nucleoside diphosphate kinase."
    Stenberg L.M., Stenflo J., Holmgren P., Brown M.A.
    Biochem. Biophys. Res. Commun. 295:689-694(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 3-15; 33-35; 47-96 AND 147-153, MASS SPECTROMETRY, BLOCKAGE OF N-TERMINUS, ACETYLATION AT ALA-2.
  6. "Identification of Drosophila wing imaginal disc proteins by two-dimensional gel analysis and microsequencing."
    Santaren J.F., van Damme J., Puype M., Vandekerckhove J., Garcia-Bellido A.
    Exp. Cell Res. 206:220-226(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 90-106.
    Strain: Vallecas.
    Tissue: Wing imaginal disk.
  7. "A Drosophila gene that is homologous to a mammalian gene associated with tumor metastasis codes for a nucleoside diphosphate kinase."
    Biggs J., Hersperger E., Steeg P.S., Liotta L.A., Shearn A.
    Cell 63:933-940(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "A Pro/Ser substitution in nucleoside diphosphate kinase of Drosophila melanogaster (mutation killer of prune) affects stability but not catalytic efficiency of the enzyme."
    Lascu I., Chaffotte A., Limbourg-Bouchon B., Veron M.
    J. Biol. Chem. 267:12775-12781(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF PRO-97.
    Strain: Canton-S.
  9. "Point mutations in awdKpn which revert the prune/Killer of prune lethal interaction affect conserved residues that are involved in nucleoside diphosphate kinase substrate binding and catalysis."
    Timmons L., Xu J., Hersperger G., Deng X.F., Shearn A.
    J. Biol. Chem. 270:23021-23030(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-15; ARG-89; ARG-106; ASP-122 AND GLU-130.
  10. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  11. "Crystal structure of the Awd nucleotide diphosphate kinase from Drosophila."
    Chiadmi M., Morera S., Lascu I., Dumas C., le Bras G., Veron M., Janin J.
    Structure 1:283-293(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  12. "Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium."
    Morera S., Chiadmi M., Lebras G., Lascu I., Janin J.
    Biochemistry 34:11062-11070(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), COFACTOR.

Entry informationi

Entry nameiNDKA_DROME
AccessioniPrimary (citable) accession number: P08879
Secondary accession number(s): Q9V9U5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 168 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

Mutations cause abnormal tissue morphology and necrosis and widespread aberrant differentiation.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.