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P65774

- NADK_SALTY

UniProt

P65774 - NADK_SALTY

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Protein

NAD kinase

Gene

nadK

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - 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.1 PublicationUniRule annotation

Catalytic activityi

ATP + NAD+ = ADP + NADP+.1 PublicationUniRule annotation

Cofactori

Divalent metal ions.1 PublicationUniRule annotation

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: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
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:
PDBe
RCSB PDB
PDBj
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.
OMAiTHEMLYH.
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 [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 11, 2004 - v1
Checksum:i93585C83A2EEF41C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE006468 Genomic DNA. Translation: AAL21572.1 .
RefSeqi NP_461613.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2AN1 X-ray 2.00 A/B/C/D 1-292 [» ]
ProteinModelPortali P65774.
SMRi P65774. Positions 4-292.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 99287.STM2683.

Proteomic databases

PRIDEi P65774.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL21572 ; AAL21572 ; STM2683 .
GeneIDi 1254206.
KEGGi stm:STM2683.
PATRICi 32384022. VBISalEnt20916_2828.

Phylogenomic databases

HOGENOMi HOG000227221.
KOi K00858.
OMAi THEMLYH.
OrthoDBi EOG6PZXDR.
PhylomeDBi P65774.

Enzyme and pathway databases

BioCyci SENT99287:GCTI-2698-MONOMER.

Miscellaneous databases

EvolutionaryTracei P65774.

Family and domain databases

Gene3Di 2.60.200.30. 1 hit.
3.40.50.10330. 1 hit.
HAMAPi MF_00361. NAD_kinase.
InterProi IPR017438. 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 ]
PANTHERi PTHR20275. PTHR20275. 1 hit.
Pfami PF01513. NAD_kinase. 1 hit.
[Graphical view ]
SUPFAMi SSF111331. SSF111331. 1 hit.
ProtoNeti Search...

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(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.

Entry informationi

Entry nameiNADK_SALTY
AccessioniPrimary (citable) accession number: P65774
Secondary accession number(s): Q8XFN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: October 29, 2014
This is version 68 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