Reviewed, UniProtKB/Swiss-Prot Q9XZT6 (DNK_DROME)

Names and origin

Protein names

Recommended name:
    Deoxynucleoside kinase
    EC=2.7.1.145
Alternative name(s):
    Deoxyribonucleoside kinase
      Short name=Dm-dNK
    Multispecific deoxynucleoside kinase

Gene names

Name:	dnk
ORF Names:	CG5452

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

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	250 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Deoxyribonucleoside kinase that has a broad specificity phosphorylating thymidine, deoxyadenosine, deoxycytidine and deoxyguanosine. Specificity is higher for pyrimidine nucleosides. Several anti-viral and anti-cancer nucleoside analogs are also efficiently phosphorylated.
Catalytic activity	ATP + 2'-deoxynucleoside = ADP + 2'-deoxynucleoside 5'-phosphate. Ref.5
Subunit structure	Monomer.
Sequence similarities	Belongs to the DCK/DGK family.
Biophysicochemical properties	Kinetic parameters: KM=0.9 µM for thymidine KM=1 µM for deoxycytidine KM=109 µM for deoxyadenosine KM=654 µM for deoxyguanosine Vmax=29.4 mmol/min/mg enzyme with thymidine as substrate Vmax=28.7 mmol/min/mg enzyme with deoxycytidine as substrate Vmax=35.5 mmol/min/mg enzyme with deoxyadenosine as substrate Vmax=37.7 mmol/min/mg enzyme with deoxyguanosine as substrate

Ontologies

Keywords
Biological process	DNA synthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW nucleoside diphosphate phosphorylation Ref.1 Ref.2 Ref.5 Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW deoxynucleoside kinase activity Ref.1 Ref.2 Ref.5 Inferred from direct assay. Source: UniProtKB phosphotransferase activity, alcohol group as acceptor Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
fal	Q9VVY4	1	EBI-99670,EBI-188912

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 250

250

Deoxynucleoside kinase

PRO_0000175097

Regions

Nucleotide binding

27 – 34

8

ATP Potential

Amino acid modifications

Modified residue

236

1

Phosphoserine Ref.7

Modified residue

241

1

Phosphoserine Ref.6

Modified residue

243

1

Phosphoserine Ref.7

Secondary structure

1

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250

Helix Strand Turn

Details...

Turn

15 – 17

3

Beta strand

21 – 26

6

Helix

33 – 37

5

Helix

41 – 43

3

Turn

44 – 46

3

Beta strand

47 – 50

4

Helix

54 – 57

4

Helix

65 – 71

7

Helix

73 – 92

20

Beta strand

98 – 105

8

Helix

107 – 112

6

Helix

114 – 120

7

Helix

126 – 142

17

Beta strand

148 – 154

7

Helix

157 – 167

11

Helix

170 – 172

3

Helix

177 – 191

15

Beta strand

200 – 206

7

Sequences

	Sequence		Length	Mass (Da)
	Q9XZT6-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 17C5DF197B8792DB	FASTA	250	29,088
	10 20 30 40 50 60 MAEAASCARK GTKYAEGTQP FTVLIEGNIG SGKTTYLNHF EKYKNDICLL TEPVEKWRNV 70 80 90 100 110 120 NGVNLLELMY KDPKKWAMPF QSYVTLTMLQ SHTAPTNKKL KIMERSIFSA RYCFVENMRR 130 140 150 160 170 180 NGSLEQGMYN TLEEWYKFIE ESIHVQADLI IYLRTSPEVA YERIRQRARS EESCVPLKYL 190 200 210 220 230 240 QELHELHEDW LIHQRRPQSC KVLVLDADLN LENIGTEYQR SESSIFDAIS SNQQPSPVLV 250 SPSKRQRVAR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of the multisubstrate deoxyribonucleoside kinase of Drosophila melanogaster." Johansson M., Van Rompay A.R., Degreve B., Balzarini J., Karlsson A. J. Biol. Chem. 274:23814-23819(1999) [PubMed: 10446143] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[2]	"Functional expression of a multisubstrate deoxyribonucleoside kinase from Drosophila melanogaster and its C-terminal deletion mutants." Munch-Petersen B., Knecht W., Lenz C., Sondergaard L., Piskur J. J. Biol. Chem. 275:6673-6679(2000) [PubMed: 10692477] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], CHARACTERIZATION. Strain: Oregon-R.
[3]	"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.
[4]	"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.
[5]	"Four deoxynucleoside kinase activities from Drosophila melanogaster are contained within a single monomeric enzyme, a new multifunctional deoxynucleoside kinase." Munch-Petersen B., Piskur J., Sondergaard L. J. Biol. Chem. 273:3926-3931(1998) [PubMed: 9461577] [Abstract] Cited for: ENZYME ACTIVITY.
[6]	"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells." Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A. Mol. Biosyst. 3:275-286(2007) [PubMed: 17372656] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, MASS SPECTROMETRY.
[7]	"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-236 AND SER-243, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF045610 mRNA. Translation: AAD47355.2.
AF185268 Genomic DNA. Translation: AAD56545.1.
Y18048 mRNA. Translation: CAB41881.1.
AE014297 Genomic DNA. Translation: AAF55615.1.

RefSeq

NP_524399.1.

UniGene

Dm.1248

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J90	X-ray	2.56	A/B	1-230	[»]
1OE0	X-ray	2.40	A/B/C/D	1-230	[»]
1OT3	X-ray	2.50	A/B/C/D/E/F/G/H	1-250	[»]
1ZM7	X-ray	2.20	A/B/C/D	1-230	[»]
1ZMX	X-ray	3.10	A/B/C/D/E/F/G/H	1-230	[»]
2JCS	X-ray	2.50	A/B	1-230	[»]
2JJ8	X-ray	2.80	A/B/C/D	1-230	[»]
2VP0	X-ray	2.20	A/B	1-250	[»]
2VP2	X-ray	2.50	A/B	1-230	[»]
2VP4	X-ray	2.20	A/B/C/D	1-230	[»]
2VP5	X-ray	2.30	A/B	1-230	[»]
2VP6	X-ray	3.00	A/B/C/D/E/F/G/H	1-230	[»]
2VP9	X-ray	2.90	A/B/C/D/E/F/G/H	1-230	[»]
2VPP	X-ray	2.20	A/B	1-230	[»]
2VQS	X-ray	2.90	A/B/C/D	1-230	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:23491N.

IntAct

Q9XZT6. 4 interactions.

STRING

Q9XZT6.

Proteomic databases

PRIDE

Q9XZT6.

Genome annotation databases

Ensembl

FBtr0083707; FBpp0083121; FBgn0022338; Drosophila melanogaster. [Genome view]

GeneID

42273.

KEGG

dme:Dmel_CG5452.

NMPDR

fig|7227.3.peg.13539.

Organism-specific databases

CTD

42273.

FlyBase

FBgn0022338. dnk.

Phylogenomic databases

HOGENOM

Q9XZT6.

OMA

TEPVEKW.

Enzyme and pathway databases

BioCyc

DMEL-XXX-02:DMEL-XXX-02-012305-MON.

BRENDA

2.7.1.145. 48.

Gene expression databases

ArrayExpress

Q9XZT6.

GermOnline

CG5452. Drosophila melanogaster.

Family and domain databases

InterPro

IPR002624. Deoxynucleoside_kinase.
[Graphical view]

PANTHER

PTHR10513. dNK. 1 hit.

Pfam

PF01712. dNK. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

828000.

Entry information

Entry name

DNK_DROME

Accession

Primary (citable) accession number: Q9XZT6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	November 1, 1999
Last modified:	November 3, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project