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Protein

NAD kinase

Gene

nadK

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation1 Publication

Catalytic activityi

ATP + NAD+ = ADP + NADP+.UniRule annotation1 Publication

Cofactori

a divalent metal cationUniRule annotation1 Publication

Enzyme regulationi

Allosterically inhibited by NADPH and NADH. NADPH is the primary inhibitor during aerobic growth and NADH during anaerobic growth.1 Publication

Kineticsi

  1. KM=2.1 mM for NAD1 Publication
  2. KM=2.7 mM for ATP1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei73 – 731Proton acceptorUniRule annotation
Binding sitei158 – 1581NADUniRule annotation
Binding sitei175 – 1751NADUniRule annotation
Sitei175 – 1751Responsible for conferring strict specificity to NADBy similarity
Binding sitei177 – 1771NADUniRule annotation
Binding sitei185 – 1851NAD; via carbonyl oxygenUniRule annotation
Binding sitei247 – 2471NADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi73 – 742NADUniRule annotation
Nucleotide bindingi147 – 1482NADUniRule annotation
Nucleotide bindingi188 – 1936NADUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. metal ion binding Source: UniProtKB-HAMAP
  3. NAD+ kinase activity Source: UniProtKB
  4. NAD binding Source: UniProtKB

GO - Biological processi

  1. NAD metabolic process Source: InterPro
  2. NADP biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, NAD, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciSENT99287:GCTI-2698-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD kinaseUniRule annotation (EC:2.7.1.23UniRule annotation)
Alternative name(s):
ATP-dependent NAD kinaseUniRule annotation
Gene namesi
Name:nadKUniRule annotation
Ordered Locus Names:STM2683
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 292292NAD kinasePRO_0000120655Add
BLAST

Proteomic databases

PRIDEiP65774.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi99287.STM2683.

Structurei

Secondary structure

1
292
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115Combined sources
Helixi22 – 3211Combined sources
Beta strandi36 – 405Combined sources
Helixi41 – 466Combined sources
Helixi57 – 637Combined sources
Beta strandi65 – 695Combined sources
Helixi73 – 8311Combined sources
Beta strandi89 – 935Combined sources
Beta strandi95 – 973Combined sources
Helixi109 – 1179Combined sources
Beta strandi121 – 13414Combined sources
Beta strandi142 – 15514Combined sources
Beta strandi160 – 1667Combined sources
Beta strandi169 – 18214Combined sources
Helixi185 – 1884Combined sources
Helixi190 – 1934Combined sources
Beta strandi204 – 2129Combined sources
Beta strandi221 – 2244Combined sources
Beta strandi229 – 2335Combined sources
Beta strandi240 – 2445Combined sources
Beta strandi250 – 2523Combined sources
Beta strandi257 – 27216Combined sources
Helixi277 – 2859Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AN1X-ray2.00A/B/C/D1-292[»]
ProteinModelPortaliP65774.
SMRiP65774. Positions 4-292.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP65774.

Family & Domainsi

Sequence similaritiesi

Belongs to the NAD kinase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000227221.
KOiK00858.
OMAiGMVELRV.
OrthoDBiEOG6PZXDR.
PhylomeDBiP65774.

Family and domain databases

Gene3Di2.60.200.30. 1 hit.
3.40.50.10330. 1 hit.
HAMAPiMF_00361. NAD_kinase.
InterProiIPR017438. 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]
PANTHERiPTHR20275. PTHR20275. 1 hit.
PfamiPF01513. NAD_kinase. 1 hit.
[Graphical view]
SUPFAMiSSF111331. SSF111331. 1 hit.

Sequencei

Sequence statusi: Complete.

P65774-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNHFKCIGI VGHPRHPTAL TTHEMLYRWL CDQGYEVIVE QQIAHELQLK
60 70 80 90 100
NVPTGTLAEI GQQADLAVVV GGDGNMLGAA RTLARYDINV IGINRGNLGF
110 120 130 140 150
LTDLDPDNAL QQLSDVLEGR YISEKRFLLE AQVCQQDRQK RISTAINEVV
160 170 180 190 200
LHPGKVAHMI EFEVYIDETF AFSQRSDGLI ISTPTGSTAY SLSAGGPILT
210 220 230 240 250
PSLDAITLVP MFPHTLSARP LVINSSSTIR LRFSHRRSDL EISCDSQIAL
260 270 280 290
PIQEGEDVLI RRCDYHLNLI HPKDYSYFNT LSTKLGWSKK LF
Length:292
Mass (Da):32,584
Last modified:October 10, 2004 - v1
Checksum:i93585C83A2EEF41C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL21572.1.
RefSeqiNP_461613.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL21572; AAL21572; STM2683.
GeneIDi1254206.
KEGGistm:STM2683.
PATRICi32384022. VBISalEnt20916_2828.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL21572.1.
RefSeqiNP_461613.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AN1X-ray2.00A/B/C/D1-292[»]
ProteinModelPortaliP65774.
SMRiP65774. Positions 4-292.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM2683.

Proteomic databases

PRIDEiP65774.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL21572; AAL21572; STM2683.
GeneIDi1254206.
KEGGistm:STM2683.
PATRICi32384022. VBISalEnt20916_2828.

Phylogenomic databases

HOGENOMiHOG000227221.
KOiK00858.
OMAiGMVELRV.
OrthoDBiEOG6PZXDR.
PhylomeDBiP65774.

Enzyme and pathway databases

BioCyciSENT99287:GCTI-2698-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP65774.

Family and domain databases

Gene3Di2.60.200.30. 1 hit.
3.40.50.10330. 1 hit.
HAMAPiMF_00361. NAD_kinase.
InterProiIPR017438. 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]
PANTHERiPTHR20275. PTHR20275. 1 hit.
PfamiPF01513. NAD_kinase. 1 hit.
[Graphical view]
SUPFAMiSSF111331. SSF111331. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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(2005) [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 (JUL-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiNADK_SALTY
AccessioniPrimary (citable) accession number: P65774
Secondary accession number(s): Q8XFN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2004
Last sequence update: October 10, 2004
Last modified: January 6, 2015
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.