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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)DescriptionActionsGraphical viewLength
Binding sitei13ATP1
Binding sitei61ATP1
Binding sitei89ATP1
Binding sitei95ATP1
Binding sitei106ATP1
Binding sitei116ATP1
Active sitei119Pros-phosphohistidine intermediate1

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
  • nucleoside triphosphate biosynthetic process Source: GO_Central
  • nucleotide metabolic process Source: UniProtKB
  • open tracheal system development Source: FlyBase
  • peptidyl-serine phosphorylation Source: FlyBase
  • protein autophosphorylation Source: FlyBase
  • protein phosphorylation Source: FlyBase
  • purine nucleotide metabolic process Source: GO_Central
  • pyrimidine nucleotide metabolic process Source: GO_Central
  • 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

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)DescriptionActionsGraphical viewLength
Mutagenesisi15D → N in KRm5; lethal due to loss of phosphorylated active site intermediate; when associated with S-97. 1 Publication1
Mutagenesisi89R → C in KRn3; lethal due to loss of phosphorylated active site intermediate; when associated with S-97. 1 Publication1
Mutagenesisi97P → S: Killer of prune mutation. Conditionally dominant lethal mutation in individuals with a null mutation in the prune gene. 1 Publication1
Mutagenesisi106R → C in KRm7; lethal due to loss of phosphorylated active site intermediate; when associated with S-97. 1 Publication1
Mutagenesisi122D → N in KRm12; lethal due to lower enzyme activity; when associated with S-97. 1 Publication1
Mutagenesisi127A → T in KRm9; lower enzyme activity; when associated with S-97. 1
Mutagenesisi130E → K in KRm4; lethal due to loss of catalytic activity; when associated with S-97. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001371082 – 153Nucleoside diphosphate kinaseAdd BLAST152

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei126Phosphoserine1 Publication1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP08879.
PRIDEiP08879.

PTM databases

iPTMnetiP08879.

Expressioni

Gene expression databases

BgeeiFBgn0000150.
ExpressionAtlasiP08879. baseline.
GenevisibleiP08879. DM.

Interactioni

Subunit structurei

Homohexamer.1 Publication

GO - Molecular functioni

  • microtubule binding Source: FlyBase

Protein-protein interaction databases

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

Structurei

Secondary structure

1153
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 5Combined sources3
Beta strandi7 – 12Combined sources6
Helixi14 – 18Combined sources5
Helixi22 – 32Combined sources11
Beta strandi35 – 39Combined sources5
Helixi46 – 52Combined sources7
Helixi54 – 56Combined sources3
Helixi62 – 69Combined sources8
Beta strandi74 – 81Combined sources8
Helixi84 – 92Combined sources9
Helixi97 – 99Combined sources3
Helixi105 – 109Combined sources5
Helixi113 – 115Combined sources3
Beta strandi118 – 120Combined sources3
Helixi124 – 134Combined sources11
Helixi137 – 139Combined sources3
Helixi148 – 151Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP08879.

Family & Domainsi

Sequence similaritiesi

Belongs to the NDK family.Curated

Phylogenomic databases

eggNOGiKOG0888. Eukaryota.
COG0105. LUCA.
GeneTreeiENSGT00760000119146.
InParanoidiP08879.
KOiK00940.
OrthoDBiEOG091G0PLD.
PhylomeDBiP08879.

Family and domain databases

HAMAPiMF_00451. NDP_kinase. 1 hit.
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 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NDLX-ray2.40A/B/C1-153[»]
1NSQX-ray2.18A/B/C1-153[»]
3WX8X-ray1.95A/B/C1-153[»]
ProteinModelPortaliP08879.
SMRiP08879.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68580. 102 interactors.
DIPiDIP-20572N.
IntActiP08879. 3 interactors.
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.
OrthoDBiEOG091G0PLD.
PhylomeDBiP08879.

Miscellaneous databases

ChiTaRSiawd. fly.
EvolutionaryTraceiP08879.
GenomeRNAii43739.
PROiP08879.

Gene expression databases

BgeeiFBgn0000150.
ExpressionAtlasiP08879. baseline.
GenevisibleiP08879. DM.

Family and domain databases

HAMAPiMF_00451. NDP_kinase. 1 hit.
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...

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: November 30, 2016
This is version 173 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.