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Q473L9 (NADK_CUPPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 55. 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:Reut_A1035
OrganismCupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134)) [Complete proteome] [HAMAP]
Taxonomic identifier264198 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length305 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.

Sequence caution

The sequence AAZ60414.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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 – 305305NAD kinase HAMAP-Rule MF_00361
PRO_0000229683

Regions

Nucleotide binding82 – 832NAD By similarity
Nucleotide binding156 – 1572NAD By similarity
Nucleotide binding197 – 2026NAD By similarity

Sites

Active site821Proton acceptor By similarity
Binding site1841NAD By similarity
Binding site1861NAD By similarity
Binding site2211NAD; via carbonyl oxygen By similarity
Binding site2551NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q473L9 [UniParc].

Last modified April 4, 2006. Version 2.
Checksum: 62198642F670FCB8

FASTA30532,820
        10         20         30         40         50         60 
MSAPQKTSAL RTPFKTVALV GRYSTAGIEG PLEELASYIL RNGQDVVFER ETSLATGLTG 

        70         80         90        100        110        120 
YPALTAEEIG READVAVVLG GDGTLLGIAR QLAGHNVPLI GVNHGRLGFM TDIPLEDVQS 

       130        140        150        160        170        180 
VLPDMLGGRY EAETRLLLES SVVRDDSPIF SALALNDVVV NRSGISGMVE LAVSVDGYFM 

       190        200        210        220        230        240 
YNQRSDGLIV STATGSTAYA LSAGGPILHP TLSGLVLVPI APHSLSNRPI VLPQEAEVTI 

       250        260        270        280        290        300 
EVATARDASV NFDMQSLTSL LPGDRIVVRR SKKTIQLLHP VGYNYYATLR KKLHWHEYPT 


EDNRL 

« Hide

References

[1]"Complete sequence of chromosome 1 of Ralstonia eutropha JMP134."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JMP134 / LMG 1197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000090 Genomic DNA. Translation: AAZ60414.1. Different initiation.
RefSeqYP_295258.1. NC_007347.1.

3D structure databases

ProteinModelPortalQ473L9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264198.Reut_A1035.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ60414; AAZ60414; Reut_A1035.
GeneID3609774.
KEGGreu:Reut_A1035.
PATRIC20227559. VBIRalEut24049_1651.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227221.
KOK00858.
OMATHEMLYH.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycCPIN264198:GIW3-1043-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_CUPPJ
AccessionPrimary (citable) accession number: Q473L9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: April 4, 2006
Last modified: July 9, 2014
This is version 55 of the entry and version 2 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