Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A4IWQ8 (NADK_FRATW) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 52. 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:
NAD kinase

EC=2.7.1.23
Alternative name(s):
ATP-dependent NAD kinase
Gene names
Name:nadK
Ordered Locus Names:FTW_0434
OrganismFrancisella tularensis subsp. tularensis (strain WY96-3418) [Complete proteome] [HAMAP]
Taxonomic identifier418136 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length296 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP By similarity. HAMAP-Rule MF_00361

Catalytic activity

ATP + NAD+ = ADP + NADP+. HAMAP-Rule MF_00361

Cofactor

Divalent metal ions By similarity. HAMAP-Rule MF_00361

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00361.

Sequence similarities

Belongs to the NAD kinase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
NAD
NADP
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processNAD metabolic process

Inferred from electronic annotation. Source: InterPro

NADP 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-KW

NAD+ kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 296296NAD kinase HAMAP-Rule MF_00361
PRO_1000005411

Regions

Nucleotide binding73 – 742NAD By similarity
Nucleotide binding151 – 1522NAD By similarity
Nucleotide binding191 – 1966NAD By similarity

Sites

Active site731Proton acceptor By similarity
Binding site781NAD By similarity
Binding site1781NAD By similarity
Binding site1801NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A4IWQ8 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: DE8D074049F87351

FASTA29632,475
        10         20         30         40         50         60 
MAFKYHKVAI VGKHYKKEVS QMVETLYAYL QQQGLEIIIE NDTAADTSLV NVAIASLKEI 

        70         80         90        100        110        120 
ALRCDVAIVV GGDGNFLKAS RLLALYSNIP VIGINKGKLG FLTTLAADDN ALKNDLYAIL 

       130        140        150        160        170        180 
KGDSSVTKMS MLKYRVDNNL RAPLEASIAL NEIAITASRG LMFGLKVFID GRYAFDQRGD 

       190        200        210        220        230        240 
GLIVSTPTGS TAHAMSAGGP ILNPNQNSVV LVPICSHSLN SRPLVISDES VIDIYITDYN 

       250        260        270        280        290 
DPESVLSIDG RHDTILKAHQ KVTIQKARKK VTVLHTKDYN YYDTLREKLG WSKVLF 

« Hide

References

[1]"Complete genomic characterization of a pathogenic A.II strain of Francisella tularensis subspecies tularensis."
Beckstrom-Sternberg S.M., Auerbach R.K., Godbole S., Pearson J.V., Beckstrom-Sternberg J.S., Deng Z., Munk C., Kubota K., Zhou Y., Bruce D., Noronha J., Scheuermann R.H., Wang A., Wei X., Wang J., Hao J., Wagner D.M., Brettin T.S. expand/collapse author list , Brown N., Gilna P., Keim P.S.
PLoS ONE 2:E947-E947(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WY96-3418.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000608 Genomic DNA. Translation: ABO46360.1.
RefSeqYP_001121480.1. NC_009257.1.

3D structure databases

ProteinModelPortalA4IWQ8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING418136.FTW_0434.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO46360; ABO46360; FTW_0434.
GeneID4960037.
KEGGftw:FTW_0434.
PATRIC17968196. VBIFraTul58433_0440.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227221.
KOK00858.
OMAGAEFCLN.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycFTUL418136:GHXJ-401-MONOMER.

Family and domain databases

Gene3D2.60.200.30. 1 hit.
3.40.50.10330. 1 hit.
HAMAPMF_00361. NAD_kinase.
InterProIPR017438. ATP-NAD_kinase_dom_1.
IPR016064. ATP-NAD_kinase_PpnK-typ.
IPR017437. ATP-NAD_kinase_PpnK-typ_all-b.
IPR002504. PolyP/ATP_NADK.
[Graphical view]
PANTHERPTHR20275. PTHR20275. 1 hit.
PfamPF01513. NAD_kinase. 1 hit.
[Graphical view]
SUPFAMSSF111331. SSF111331. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNADK_FRATW
AccessionPrimary (citable) accession number: A4IWQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 2007
Last modified: July 9, 2014
This is version 52 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