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

Q66DA9 (NADK_YERPS) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 60. 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:YPTB1140
OrganismYersinia pseudotuberculosis serotype I (strain IP32953) [Complete proteome] [HAMAP]
Taxonomic identifier273123 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length293 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 – 293293NAD kinase HAMAP-Rule MF_00361
PRO_0000229715

Regions

Nucleotide binding74 – 752NAD By similarity
Nucleotide binding148 – 1492NAD By similarity
Nucleotide binding189 – 1946NAD By similarity

Sites

Active site741Proton acceptor By similarity
Binding site1591NAD By similarity
Binding site1761NAD By similarity
Binding site1781NAD By similarity
Binding site2481NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q66DA9 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: C0231B200E8B5E0E

FASTA29332,412
        10         20         30         40         50         60 
MNNRRFDCIG IVGHPRHPAA LATHEILYHW LKARGYAVMV EQQIAHDLNL TDAITGSLAD 

        70         80         90        100        110        120 
IGQKADLAVV VGGDGNMLGA ARVLARYDIK VIGVNRGNLG FLTDLDPDNA LQQLSDVLEG 

       130        140        150        160        170        180 
EYLSEQRFLL ETHVRRTNQQ SRISTAINEV VLHPGKVAHM IEFEVYIDDR FAFSQRSDGL 

       190        200        210        220        230        240 
IIATPTGSTA YSLSAGGPIL TPTLDAIVLV PMFPHTLTAR PLVISSTSTI RLKFSHITSD 

       250        260        270        280        290 
LEISCDSQIA LPIQEGEEVL IRRSDFHLNL IHPKDYSYFN TLSTKLGWSK KLF 

« Hide

References

[1]"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis."
Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B. expand/collapse author list , Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E.
Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IP32953.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX936398 Genomic DNA. Translation: CAH20380.1.
RefSeqYP_069675.1. NC_006155.1.

3D structure databases

ProteinModelPortalQ66DA9.
SMRQ66DA9. Positions 6-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273123.YPTB1140.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH20380; CAH20380; YPTB1140.
GeneID2953485.
KEGGyps:YPTB1140.
PATRIC18640740. VBIYerPse22266_1447.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227221.
KOK00858.
OMAIRRASCA.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycYPSE273123:GI1M-1200-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_YERPS
AccessionPrimary (citable) accession number: Q66DA9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 11, 2004
Last modified: July 9, 2014
This is version 60 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