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Q8DU98 (NADK_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 68. 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:SMU_1045c
OrganismStreptococcus mutans serotype c (strain ATCC 700610 / UA159) [Complete proteome] [HAMAP]
Taxonomic identifier210007 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length277 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 – 277277NAD kinase HAMAP-Rule MF_00361
PRO_0000229694

Regions

Nucleotide binding55 – 562NAD By similarity
Nucleotide binding131 – 1322NAD By similarity
Nucleotide binding170 – 1756NAD By similarity

Sites

Active site551Proton acceptor By similarity
Binding site1571NAD By similarity
Binding site1591NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DU98 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 1DC19AE1A27112CE

FASTA27731,323
        10         20         30         40         50         60 
MTQMNFTDKI KVAIIANGKY QSKRLTAKLF AILRNDDRFY LTKKNPDIVI TIGGDGMLLS 

        70         80         90        100        110        120 
AFHMYEKCLD HVRFVGIHTG HLGFYTDYRD FEVDKLLENL HSDKGEKASY PILKVTATLA 

       130        140        150        160        170        180 
DGRQLTSRAL NEATIRRIEK TMVADVVINK VHFERFRGDG ISVSTPTGST AYNKSLGGAV 

       190        200        210        220        230        240 
LHPTIEALQL TEISSLNNRV FRTLGSSIIV PKKDKIEIVP KRLGSYVLSI DNKTYTHRNV 

       250        260        270 
AKIEYEIDRK KISFVSTPSH TSFWERVKDA FIGDFDS 

« Hide

References

[1]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014133 Genomic DNA. Translation: AAN58744.1.
RefSeqNP_721438.1. NC_004350.2.

3D structure databases

ProteinModelPortalQ8DU98.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING210007.SMU.1045c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN58744; AAN58744; SMU_1045c.
GeneID1028373.
KEGGsmu:SMU_1045c.
PATRIC19664205. VBIStrMut61772_0935.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
KOK00858.
OMAIQMSEIA.
OrthoDBEOG6PZXDR.
PhylomeDBQ8DU98.

Enzyme and pathway databases

BioCycSMUT210007:GC7Z-994-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_STRMU
AccessionPrimary (citable) accession number: Q8DU98
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 68 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