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B1XXL7 (NDK_LEPCP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleoside diphosphate kinase

Short name=NDK
Short name=NDP kinase
EC=2.7.4.6
Alternative name(s):
Nucleoside-2-P kinase
Gene names
Name:ndk
Ordered Locus Names:Lcho_2872
OrganismLeptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix discophora (strain SP-6)) [Complete proteome] [HAMAP]
Taxonomic identifier395495 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesLeptothrix

Protein attributes

Sequence length141 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_00451

Catalytic activity

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. HAMAP-Rule MF_00451

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00451

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00451

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00451.

Sequence similarities

Belongs to the NDK family.

Ontologies

Keywords
   Biological processNucleotide metabolism
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processCTP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

GTP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

UTP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoside diphosphate kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 141141Nucleoside diphosphate kinase HAMAP-Rule MF_00451
PRO_1000192268

Sites

Active site1171Pros-phosphohistidine intermediate By similarity
Binding site111ATP By similarity
Binding site591ATP By similarity
Binding site871ATP By similarity
Binding site931ATP By similarity
Binding site1041ATP By similarity
Binding site1141ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B1XXL7 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: E353CB75AC00869B

FASTA14115,166
        10         20         30         40         50         60 
MAIERTLSII KPDAVAKNVI GQILARFEGA GLKIAAARLA QLSRAEAEQF YAVHKARPFF 

        70         80         90        100        110        120 
NDLVNFMISG PVMIQVLEGE GAILKNRDLM GATDPKKAEK GTIRADFADS IDANAVHGSD 

       130        140 
APETAAVEIA FFFPGMAVYS R 

« Hide

References

[1]"Complete sequence of Leptothrix cholodnii SP-6."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Emerson D., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51168 / LMG 8142 / SP-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001013 Genomic DNA. Translation: ACB35137.1.
RefSeqYP_001791902.1. NC_010524.1.

3D structure databases

ProteinModelPortalB1XXL7.
SMRB1XXL7. Positions 2-140.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395495.Lcho_2872.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB35137; ACB35137; Lcho_2872.
GeneID6159747.
KEGGlch:Lcho_2872.
PATRIC22396155. VBILepCho83238_2903.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0105.
HOGENOMHOG000224565.
KOK00940.
OMATRTQERT.
OrthoDBEOG67DPRV.

Enzyme and pathway databases

BioCycLCHO395495:GHYL-2919-MONOMER.

Family and domain databases

Gene3D3.30.70.141. 1 hit.
HAMAPMF_00451. NDP_kinase.
InterProIPR001564. Nucleoside_diP_kinase.
IPR023005. Nucleoside_diP_kinase_AS.
[Graphical view]
PfamPF00334. NDK. 1 hit.
[Graphical view]
PRINTSPR01243. NUCDPKINASE.
SMARTSM00562. NDK. 1 hit.
[Graphical view]
SUPFAMSSF54919. SSF54919. 1 hit.
PROSITEPS00469. NDP_KINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNDK_LEPCP
AccessionPrimary (citable) accession number: B1XXL7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 20, 2008
Last modified: February 19, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families