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Q8EPB4 (NADK2_OCEIH) 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 2

EC=2.7.1.23
Alternative name(s):
ATP-dependent NAD kinase 2
Gene names
Name:nadK2
Ordered Locus Names:OB2196
OrganismOceanobacillus iheyensis (strain DSM 14371 / JCM 11309 / KCTC 3954 / HTE831) [Complete proteome] [HAMAP]
Taxonomic identifier221109 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeOceanobacillus

Protein attributes

Sequence length266 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 – 266266NAD kinase 2 HAMAP-Rule MF_00361
PRO_0000120643

Regions

Nucleotide binding51 – 522NAD By similarity
Nucleotide binding123 – 1242NAD By similarity
Nucleotide binding163 – 1686NAD By similarity

Sites

Active site511Proton acceptor By similarity
Binding site1501NAD By similarity
Binding site1521NAD By similarity
Binding site1871NAD; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8EPB4 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: FCF1BD5DF6AB442C

FASTA26630,030
        10         20         30         40         50         60 
MAERQNIFFY YHPDEEMDGK VKALKKISSE NGLNVVENSS DASIIVSIGG DGTFLQAVRK 

        70         80         90        100        110        120 
TGFRQDCIYT GIMREGQSGL YCDFNIDNFD NMIHSVLHED LEVRRFPTIK VQINGETPFY 

       130        140        150        160        170        180 
CLNEVSIRST IVKTIVINVC VDGFHFETFR GDGMIVSTPT GSTGYSKSAR GAVIDPLIHG 

       190        200        210        220        230        240 
FQVSEVASLN NNQYRTLGSS FLLNKDRKLE LEILQDGNDH PIISLDNEAS PIKRIQNIDV 

       250        260 
TMDETIIKTV KLKNNSYWER VKRTFL 

« Hide

References

[1]"Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments."
Takami H., Takaki Y., Uchiyama I.
Nucleic Acids Res. 30:3927-3935(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14371 / JCM 11309 / KCTC 3954 / HTE831.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000028 Genomic DNA. Translation: BAC14152.1.
RefSeqNP_693117.1. NC_004193.1.

3D structure databases

ProteinModelPortalQ8EPB4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING221109.OB2196.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC14152; BAC14152; BAC14152.
GeneID1015552.
KEGGoih:OB2196.
PATRIC22795434. VBIOceIhe82024_2225.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000275803.
KOK00858.
OMADDLHFET.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycOIHE221109:GI2A-2277-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 nameNADK2_OCEIH
AccessionPrimary (citable) accession number: Q8EPB4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: March 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