P08879 (NDKA_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nucleoside diphosphate kinase
Short name=NDK
Short name=NDP kinase
EC=2.7.4.6

Alternative name(s):
Abnormal wing disks protein
Killer of prune protein

Gene names

Name:	awd
Synonyms:	K-pn
ORF Names:	CG2210

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	153 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.7 Ref.9
Catalytic activity	ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. Ref.8
Cofactor	Magnesium. Ref.12
Subunit structure	Homohexamer. Ref.8
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Note: Microtubule-associated. Ref.7
Miscellaneous	Mutations cause abnormal tissue morphology and necrosis and widespread aberrant differentiation.
Sequence similarities	Belongs to the NDK family.
Mass spectrometry	Molecular mass is 17082.3±0.6 Da from positions 2 - 153. Determined by ESI. Acetylated. Ref.5
Sequence caution	The sequence AAF57188.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Cellular component	Cytoplasm Cytoskeleton Microtubule
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	CTP biosynthetic process Traceable author statement Ref.12. Source: UniProtKB GTP biosynthetic process Traceable author statement Ref.12. Source: UniProtKB UTP biosynthetic process Traceable author statement Ref.12. Source: UniProtKB adherens junction organization Inferred from mutant phenotype. Source: FlyBase epithelial cell migration, open tracheal system Inferred from mutant phenotype. Source: FlyBase establishment or maintenance of polarity of follicular epithelium Inferred from mutant phenotype. Source: FlyBase microtubule-based process Inferred from mutant phenotype Ref.7. Source: FlyBase mitosis Inferred from mutant phenotype Ref.7. Source: FlyBase peptidyl-serine phosphorylation Inferred from direct assay. Source: FlyBase protein autophosphorylation Inferred from direct assay. Source: FlyBase regulation of tube architecture, open tracheal system Inferred from mutant phenotype. Source: FlyBase
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule associated complex Inferred from direct assay. Source: FlyBase nuclear microtubule Inferred from mutant phenotype Ref.7. Source: UniProtKB
Molecular function	ATP binding Inferred from direct assay Ref.8. Source: UniProtKB GTP binding Inferred from direct assay. Source: FlyBase magnesium ion binding Inferred from direct assay Ref.12. Source: UniProtKB microtubule binding Inferred from direct assay Ref.7. Source: FlyBase nucleoside diphosphate kinase activity Inferred from direct assay Ref.8. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 153

152

Nucleoside diphosphate kinase

PRO_0000137108

Sites

Active site

119

1

Pros-phosphohistidine intermediate

Binding site

13

1

ATP

Binding site

61

1

ATP

Binding site

89

1

ATP

Binding site

95

1

ATP

Binding site

106

1

ATP

Binding site

116

1

ATP

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.5

Modified residue

126

1

Phosphoserine Ref.10

Experimental info

Mutagenesis

15

1

D → N in KRm5; lethal due to loss of phosphorylated active site intermediate; when associated with S-97. Ref.9

Mutagenesis

89

1

R → C in KRn3; lethal due to loss of phosphorylated active site intermediate; when associated with S-97. Ref.9

Mutagenesis

97

1

P → S: Killer of prune mutation. Conditionally dominant lethal mutation in individuals with a null mutation in the prune gene. Ref.8

Mutagenesis

106

1

R → C in KRm7; lethal due to loss of phosphorylated active site intermediate; when associated with S-97. Ref.9

Mutagenesis

122

1

D → N in KRm12; lethal due to lower enzyme activity; when associated with S-97. Ref.9

Mutagenesis

127

1

A → T in KRm9; lower enzyme activity; when associated with S-97.

Mutagenesis

130

1

E → K in KRm4; lethal due to loss of catalytic activity; when associated with S-97. Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

153

Helix Strand Turn

Details...

Helix

3 – 5

3

Beta strand

7 – 12

6

Helix

14 – 18

5

Helix

22 – 32

11

Beta strand

35 – 40

6

Helix

46 – 52

7

Helix

54 – 56

3

Helix

62 – 69

8

Beta strand

74 – 81

8

Helix

84 – 92

9

Helix

97 – 99

3

Helix

105 – 109

5

Helix

113 – 115

3

Beta strand

118 – 120

3

Helix

124 – 134

11

Helix

137 – 139

3

Helix

148 – 151

4

Sequences

	Sequence		Length	Mass (Da)
	P08879 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E98765853255445E	FASTA	153	17,170
	10 20 30 40 50 60 MAANKERTFI MVKPDGVQRG LVGKIIERFE QKGFKLVALK FTWASKELLE KHYADLSARP 70 80 90 100 110 120 FFPGLVNYMN SGPVVPMVWE GLNVVKTGRQ MLGATNPADS LPGTIRGDFC IQVGRNIIHG 130 140 150 SDAVESAEKE IALWFNEKEL VTWTPAAKDW IYE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2849580] [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: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] 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: 12537569] [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: 12099695] [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: 8500545] [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: 2175255] [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: 1320004] [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: 7559441] [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: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, 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: 8081741] [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: 7669763] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), COFACTOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X13107 mRNA. Translation: CAA31500.1.
AE014297 Genomic DNA. Translation: AAF57188.3. Different initiation.
AY113576 mRNA. Translation: AAM29581.1.

PIR

S01908.

RefSeq

NP_476761.2. NM_057413.4.

UniGene

Dm.6904.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NDL	X-ray	2.40	A/B/C	1-153	[»]
1NSQ	X-ray	2.18	A/B/C	1-153	[»]

ProteinModelPortal

P08879.

SMR

P08879. Positions 2-153.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-20572N.

MINT

MINT-936330.

STRING

P08879.

Proteomic databases

PRIDE

P08879.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

43739.

KEGG

dme:Dmel_CG2210.

NMPDR

fig|7227.3.peg.15639.

Organism-specific databases

CTD

43739.

FlyBase

FBgn0000150. awd.

Phylogenomic databases

eggNOG

inNOG05717.

GeneTree

EMGT00050000005753.

InParanoid

P08879.

OrthoDB

EOG4XGXG7.

PhylomeDB

P08879.

Gene expression databases

Bgee

P08879.

GermOnline

CG2210. Drosophila melanogaster.

Family and domain databases

InterPro

IPR001564. Nucleoside_diP_kinase.
IPR023005. Nucleoside_diP_kinase_AS.
[Graphical view]

Gene3D

G3DSA:3.30.70.141. NDK. 1 hit.

KO

K00940.

PANTHER

PTHR11349. Nuc_diP_kinase_core. 1 hit.

Pfam

PF00334. NDK. 1 hit.
[Graphical view]

PRINTS

PR01243. NUCDPKINASE.

SMART

SM00562. NDK. 1 hit.
[Graphical view]

SUPFAM

SSF54919. NDK. 1 hit.

PROSITE

PS00469. NDP_KINASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

835532.

Entry information

Entry name

NDKA_DROME

Accession

Primary (citable) accession number: P08879
Secondary accession number(s): Q9V9U5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 133 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project