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Protein

Nucleoside diphosphate kinase

Gene

ndpk

Organism
Pisum sativum (Garden pea)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

KinaseUniRule annotationImported, Transferase

Keywords - Ligandi

ATP-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.4.6. 4872.
SABIO-RKQ9SP13.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoside diphosphate kinaseUniRule annotation (EC:2.7.4.6UniRule annotation)
Gene namesi
Name:ndpkImported
OrganismiPisum sativum (Garden pea)Imported
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Interactioni

Protein-protein interaction databases

IntActiQ9SP13. 1 interaction.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W7WX-ray2.80A/B/C/D/E/F81-233[»]
ProteinModelPortaliQ9SP13.
SMRiQ9SP13. Positions 81-231.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9SP13.

Family & Domainsi

Sequence similaritiesi

Belongs to the NDK family.UniRule annotation

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.

Q9SP13-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASHLCKSAS RAARSLLSAS FHSQGRAVAA AAAVASIRKV PVFAPNYRRT
60 70 80 90 100
GSGNGPSSWI AGALALPAAA YMLQDQEVHA AELERTFIAI KPDGVQRGLI
110 120 130 140 150
SEIISRFERK GFKLVGIKVL IPTKQFAQQH YHDLKERPFF NGLCDFLSSG
160 170 180 190 200
PVIAMVWEGE GVITYGRKLI GATDPQKSAP GTIRGDLAVV VGRNIIHGSD
210 220 230
GPETAKDEIK LWFKPEELVS FTSNSEKWIY GDN
Length:233
Mass (Da):25,264
Last modified:May 1, 2000 - v1
Checksum:i3BBEB0FED8E6159E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191098 mRNA. Translation: AAF08537.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191098 mRNA. Translation: AAF08537.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W7WX-ray2.80A/B/C/D/E/F81-233[»]
ProteinModelPortaliQ9SP13.
SMRiQ9SP13. Positions 81-231.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9SP13. 1 interaction.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.7.4.6. 4872.
SABIO-RKQ9SP13.

Miscellaneous databases

EvolutionaryTraceiQ9SP13.

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

  1. "Cloning and characterisation of a pea mitochondrial NDPK."
    Escobar Galvis M.L., Hakansson G., Alexciev K., Knorpp C.
    Biochimie 81:1089-1096(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Structure and mutational analysis of a plant mitochondrial nucleoside diphosphate kinase. Identification of residues involved in serine phosphorylation and oligomerization."
    Johansson M., Mackenzie-Hose A., Andersson I., Knorpp C.
    Plant Physiol. 136:3034-3042(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 81-233.

Entry informationi

Entry nameiQ9SP13_PEA
AccessioniPrimary (citable) accession number: Q9SP13
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: November 11, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.