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C5CYY6 (NADK_VARPS) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 31. 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:Vapar_4336
OrganismVariovorax paradoxus (strain S110) [Complete proteome] [HAMAP]
Taxonomic identifier543728 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeVariovorax

Protein attributes

Sequence length303 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 – 303303NAD kinase HAMAP-Rule MF_00361
PRO_1000205435

Regions

Nucleotide binding85 – 862NAD By similarity
Nucleotide binding159 – 1602NAD By similarity
Nucleotide binding200 – 2056NAD By similarity

Sites

Active site851Proton acceptor By similarity
Binding site1871NAD By similarity
Binding site1891NAD By similarity
Binding site2241NAD; via carbonyl oxygen By similarity
Binding site2581NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
C5CYY6 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 795B2B97C5955CBC

FASTA30332,583
        10         20         30         40         50         60 
MTSRFRHVAL IGKYQASGAR AQADARDGVM EDIGAFLESQ GCEVFVEKSA AEEADADASV 

        70         80         90        100        110        120 
GGRYQPLTVE EIGQRCDLGL VVGGDGTMLG IGRQLACYGI PLIGINRGRL GFITDIPLDN 

       130        140        150        160        170        180 
YQATLIPMLA GEYEEDHRSL MHAQVMRDGA SVFDALAMND VVVNRGATSG MVELRVSVGR 

       190        200        210        220        230        240 
HFVANQRADG LIIASPTGST AYALSAGGPL LHPAVPGWVL VPIAPHTLSN RPVLLPDADE 

       250        260        270        280        290        300 
IVIELVAGRD ASANFDMQSL ASLAIGDRVV VRRSDFRVRF LHPRGWSYFD TLRKKLHWNE 


GGS 

« Hide

References

[1]"Complete genome sequence of the metabolically versatile plant growth-promoting endophyte, Variovorax paradoxus S110."
Han J.I., Choi H.K., Lee S.W., Orwin P.M., Kim J., Laroe S.L., Kim T.G., O'Neil J., Leadbetter J.R., Lee S.Y., Hur C.G., Spain J.C., Ovchinnikova G., Goodwin L., Han C.
J. Bacteriol. 193:1183-1190(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S110.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001635 Genomic DNA. Translation: ACS20947.1.
RefSeqYP_002946213.1. NC_012791.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING543728.Vapar_4336.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS20947; ACS20947; Vapar_4336.
GeneID7970526.
KEGGvap:Vapar_4336.
PATRIC24009177. VBIVarPar36677_4365.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227221.
KOK00858.
OMATHEMLYH.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycVPAR543728:GHLL-4378-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_VARPS
AccessionPrimary (citable) accession number: C5CYY6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: July 9, 2014
This is version 31 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