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Q8DKK1 (NADK1_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 63. 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 1

EC=2.7.1.23
Alternative name(s):
ATP-dependent NAD kinase 1
Gene names
Name:nadK1
Ordered Locus Names:tll0858
OrganismThermosynechococcus elongatus (strain BP-1) [Reference proteome] [HAMAP]
Taxonomic identifier197221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus

Protein attributes

Sequence length307 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
Reference 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 – 307307NAD kinase 1 HAMAP-Rule MF_00361
PRO_0000120676

Regions

Nucleotide binding77 – 782NAD By similarity
Nucleotide binding151 – 1522NAD By similarity
Nucleotide binding192 – 1976NAD By similarity

Sites

Active site771Proton acceptor By similarity
Binding site1811NAD By similarity
Binding site2511NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DKK1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E9002ECD7605593D

FASTA30733,282
        10         20         30         40         50         60 
MKAGIIYNEG KPLAVELAAH VRRILELQGW EVHMATGIGG ILGYSRPDSP VCHTPIDQLV 

        70         80         90        100        110        120 
PPGFDASMAF AVVLGGDGTV LSAFRQLAPC EIPLLTINTG HLGFLTEGYV ADLEPALDQV 

       130        140        150        160        170        180 
LRGDYTIEDR TMLTVQVLRD QTVIWEALSL NEMVIHKEPL TGMCHFEVDV GAHARVDIAA 

       190        200        210        220        230        240 
DGLILSTPTG STAYALSAGG PVITPGVAAL QLVPICPHSL ASRALVFSNS EPVWIYPANP 

       250        260        270        280        290        300 
FKHLILVVDG NAGCYIQPED QVFVQRAPYR ARFIRLRAPE FFHVLQQKLG WGLPHVAKPR 


AKKSTDS 

« Hide

References

[1]"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takeuchi C., Yamada M., Tabata S.
DNA Res. 9:123-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000039 Genomic DNA. Translation: BAC08410.1.
RefSeqNP_681648.1. NC_004113.1.

3D structure databases

ProteinModelPortalQ8DKK1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING197221.tll0858.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC08410; BAC08410; BAC08410.
GeneID1011490.
KEGGtel:tll0858.
PATRIC23927006. VBITheElo119873_0903.

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227222.
KOK00858.
OMAPRKTKFV.
OrthoDBEOG6PZXDR.

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 nameNADK1_THEEB
AccessionPrimary (citable) accession number: Q8DKK1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 63 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