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Q7VGM5 (NADK_HELHP) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 66. 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:HH_1296
OrganismHelicobacter hepaticus (strain ATCC 51449 / 3B1) [Complete proteome] [HAMAP]
Taxonomic identifier235279 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length301 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 – 301301NAD kinase HAMAP-Rule MF_00361
PRO_0000229644

Regions

Nucleotide binding73 – 742NAD By similarity
Nucleotide binding160 – 1612NAD By similarity
Nucleotide binding201 – 2066NAD By similarity

Sites

Active site731Proton acceptor By similarity
Binding site1881NAD By similarity
Binding site1901NAD By similarity
Binding site1981NAD; via carbonyl oxygen By similarity
Binding site2251NAD; via carbonyl oxygen By similarity
Binding site2571NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VGM5 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: A52412F0CD5A6A31

FASTA30133,777
        10         20         30         40         50         60 
MKSHNAPITK VGVILRPSSP ELKTTFLQIK EELNNAGIEV ILESISGGMI ELLGRDFHQL 

        70         80         90        100        110        120 
ATQCDALFSL GGDGTLISML RRAFEYELPC MGINTGRLGF LTALMPQNLH TFTSHLKSGD 

       130        140        150        160        170        180 
YTLQKHLVLQ ARIYSTLNTA YENNLDNKNQ TPTQTLIAIN EFLISKHELS GMVHIDASID 

       190        200        210        220        230        240 
RKYFNTYRCD GLIIGTPAGS TAYNISAGGS VIYPYCRNIL LTPIAPHSLT QRPLVLSDEF 

       250        260        270        280        290        300 
MLEFYAKERA KLIIDGQEMI DIMPSDRVQI QALPQSAMLM YPPTRDYFSV LKEKFKWGEE 


H 

« Hide

References

[1]"The complete genome sequence of the carcinogenic bacterium Helicobacter hepaticus."
Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M., Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R., Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B. expand/collapse author list , Shen Z., Weber J., Frosch M., Fox J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51449 / 3B1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017125 Genomic DNA. Translation: AAP77893.1.
RefSeqNP_860827.1. NC_004917.1.

3D structure databases

ProteinModelPortalQ7VGM5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING235279.HH1296.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP77893; AAP77893; HH_1296.
GeneID1492984.
KEGGhhe:HH1296.
PATRIC20590044. VBIHelHep90276_1282.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
KOK00858.
OMAHPSIPGW.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycHHEP235279:GHUA-1333-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_HELHP
AccessionPrimary (citable) accession number: Q7VGM5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 1, 2003
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