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Q8ZH09 (NADK_YERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:YPO1106, y3074, YP_1050
OrganismYersinia pestis [Reference proteome] [HAMAP]
Taxonomic identifier632 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length293 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Subunit structure

Homodimer. Ref.4

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00361.

Sequence similarities

Belongs to the NAD kinase family.

Sequence caution

The sequence AAS61300.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
NAD
NADP
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Reference 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_0000120695

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 site1861NAD; via carbonyl oxygen By similarity
Binding site2481NAD By similarity
Site1761Responsible for conferring strict specificity to NAD By similarity

Secondary structure

.................................................. 293
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8ZH09 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: C0231F341E8F4A1E

FASTA29332,398
        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 PLVISSSSTI RLKFSHITSD 

       250        260        270        280        290 
LEISCDSQIA LPIQEGEEVL IRRSDFHLNL IHPKDYSYFN TLSTKLGWSK KLF 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of Yersinia pestis, the causative agent of plague."
Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. expand/collapse author list , Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:523-527(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CO-92 / Biovar Orientalis.
[2]"Genome sequence of Yersinia pestis KIM."
Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. expand/collapse author list , Matson J.S., Blattner F.R., Perry R.D.
J. Bacteriol. 184:4601-4611(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KIM10+ / Biovar Mediaevalis.
[3]"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."
Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. expand/collapse author list , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.
DNA Res. 11:179-197(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 91001 / Biovar Mediaevalis.
[4]"Crystal structure of inorganic polyphosphate/ATP-NAD kinase from Yersinia pestis CO92."
Center for structural genomics of infectious diseases (CSGID)
Submitted (SEP-2012) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL590842 Genomic DNA. Translation: CAL19772.1.
AE009952 Genomic DNA. Translation: AAM86624.1.
AE017042 Genomic DNA. Translation: AAS61300.1. Different initiation.
PIRAB0136.
RefSeqNP_670373.1. NC_004088.1.
YP_002346149.1. NC_003143.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4HAOX-ray2.55A/B1-293[»]
ProteinModelPortalQ8ZH09.
SMRQ8ZH09. Positions 6-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8ZH09. 1 interaction.
STRING214092.YPO1106.

Proteomic databases

PRIDEQ8ZH09.

Protocols and materials databases

DNASU1148021.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM86624; AAM86624; y3074.
AAS61300; AAS61300; YP_1050.
GeneID1148021.
1173954.
KEGGype:YPO1106.
ypk:y3074.
PATRIC18591493. VBIYerPes7843_1474.

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227221.
KOK00858.
OMAIRRASCA.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycYPES214092:GKDD-1101-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_YERPE
AccessionPrimary (citable) accession number: Q8ZH09
Secondary accession number(s): Q0WHT9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 92 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references