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Q7VKR8 (NADK_HAEDU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 62. 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:HD_1804
OrganismHaemophilus ducreyi (strain 35000HP / ATCC 700724) [Complete proteome] [HAMAP]
Taxonomic identifier233412 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length296 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 AAP96554.1 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 – 296296NAD kinase HAMAP-Rule MF_00361
PRO_0000120621

Regions

Nucleotide binding75 – 762NAD By similarity
Nucleotide binding150 – 1512NAD By similarity
Nucleotide binding191 – 1966NAD By similarity

Sites

Active site751Proton acceptor By similarity
Binding site1611NAD By similarity
Binding site1781NAD By similarity
Binding site1801NAD By similarity
Binding site2511NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VKR8 [UniParc].

Last modified July 19, 2005. Version 2.
Checksum: C6BE4C899FED7D62

FASTA29632,934
        10         20         30         40         50         60 
MKNVTKRSFQ TIAIVGKPRH DNALETHLAV YNWLKDRHYS VLVEEKIAEQ LQLPNGKRIE 

        70         80         90        100        110        120 
EIGQIADLVI VIGGDGNMLG MARSLAKYQV PLIGINRGNL GFLTDIAPQS AFEQLYSCLE 

       130        140        150        160        170        180 
KGEFIIEQRF LLEAQIEQNG KIISANNALN EVAIHPTQVA RIIEFEVYID SKFAFSQRSD 

       190        200        210        220        230        240 
GLIIATPTGS TAYSLSAGGP ILTPNMNAIA LVPMHPHALS SRPLVIDGDS HISLRFAQYN 

       250        260        270        280        290 
QPNLEISCDG QDDLPFTPED RIIVRKSPDI LHLLHLKDYN YFTVLGSKLG WSSKLF 

« Hide

References

[1]"The complete genome sequence of Haemophilus ducreyi."
Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., Nguyen D., Wang J., Forst C., Hood L.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 35000HP / ATCC 700724.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017143 Genomic DNA. Translation: AAP96554.1. Different initiation.
RefSeqNP_874165.1. NC_002940.2.

3D structure databases

ProteinModelPortalQ7VKR8.
SMRQ7VKR8. Positions 8-296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233412.HD1804.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP96554; AAP96554; HD_1804.
GeneID1491651.
KEGGhdu:HD1804.
PATRIC20179778. VBIHaeDuc133973_1516.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
KOK00858.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycHDUC233412:GH5F-1627-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_HAEDU
AccessionPrimary (citable) accession number: Q7VKR8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: July 9, 2014
This is version 62 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