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P65774 (NADK_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 66. 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:STM2683
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length292 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. It can use ATP and other nucleoside triphosphates as a source of phosphorus. NADH can not replace NAD as a substrate. Ref.2

Catalytic activity

ATP + NAD+ = ADP + NADP+. Ref.2

Cofactor

Divalent metal ions. Ref.2

Enzyme regulation

Allosterically inhibited by NADPH and NADH. NADPH is the primary inhibitor during aerobic growth and NADH during anaerobic growth. Ref.2

Subunit structure

Equilibrium mixture of dimer and tetramer. It is converted entirely to tetramer in the presence of the inhibitor NADPH. Ref.2 Ref.3

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00361.

Sequence similarities

Belongs to the NAD kinase family.

Biophysicochemical properties

Kinetic parameters:

KM=2.1 mM for NAD Ref.2

KM=2.7 mM for ATP

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 direct assay Ref.2. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from direct assay Ref.2. Source: UniProtKB

NAD binding

Inferred from direct assay Ref.2. Source: UniProtKB

NAD+ kinase activity

Inferred from direct assay Ref.2. Source: UniProtKB

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 – 292292NAD kinase HAMAP-Rule MF_00361
PRO_0000120655

Regions

Nucleotide binding73 – 742NAD By similarity
Nucleotide binding147 – 1482NAD By similarity
Nucleotide binding188 – 1936NAD By similarity

Sites

Active site731Proton acceptor By similarity
Binding site1581NAD By similarity
Binding site1751NAD By similarity
Binding site1771NAD By similarity
Binding site1851NAD; via carbonyl oxygen By similarity
Binding site2471NAD By similarity
Site1751Responsible for conferring strict specificity to NAD By similarity

Secondary structure

.............................................. 292
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P65774 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 93585C83A2EEF41C

FASTA29232,584
        10         20         30         40         50         60 
MNNHFKCIGI VGHPRHPTAL TTHEMLYRWL CDQGYEVIVE QQIAHELQLK NVPTGTLAEI 

        70         80         90        100        110        120 
GQQADLAVVV GGDGNMLGAA RTLARYDINV IGINRGNLGF LTDLDPDNAL QQLSDVLEGR 

       130        140        150        160        170        180 
YISEKRFLLE AQVCQQDRQK RISTAINEVV LHPGKVAHMI EFEVYIDETF AFSQRSDGLI 

       190        200        210        220        230        240 
ISTPTGSTAY SLSAGGPILT PSLDAITLVP MFPHTLSARP LVINSSSTIR LRFSHRRSDL 

       250        260        270        280        290 
EISCDSQIAL PIQEGEDVLI RRCDYHLNLI HPKDYSYFNT LSTKLGWSKK LF 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[2]"Evidence that feedback inhibition of NAD kinase controls responses to oxidative stress."
Grose J.H., Joss L., Velick S.F., Roth J.R.
Proc. Natl. Acad. Sci. U.S.A. 103:7601-7606(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, NOMENCLATURE.
[3]"The crystal structure of a putative kinase from Salmonella typhimurim LT2."
Midwest center for structural genomics (MCSG)
Submitted (AUG-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006468 Genomic DNA. Translation: AAL21572.1.
RefSeqNP_461613.1. NC_003197.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AN1X-ray2.00A/B/C/D1-292[»]
ProteinModelPortalP65774.
SMRP65774. Positions 4-292.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM2683.

Proteomic databases

PRIDEP65774.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL21572; AAL21572; STM2683.
GeneID1254206.
KEGGstm:STM2683.
PATRIC32384022. VBISalEnt20916_2828.

Phylogenomic databases

HOGENOMHOG000227221.
KOK00858.
OMATHEMLYH.
OrthoDBEOG6PZXDR.
PhylomeDBP65774.

Enzyme and pathway databases

BioCycSENT99287:GCTI-2698-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...

Other

EvolutionaryTraceP65774.

Entry information

Entry nameNADK_SALTY
AccessionPrimary (citable) accession number: P65774
Secondary accession number(s): Q8XFN1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 9, 2014
This is version 66 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