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B5E4L2 (NADK_STRP4) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 43. 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:SPG_1018
OrganismStreptococcus pneumoniae serotype 19F (strain G54) [Complete proteome] [HAMAP]
Taxonomic identifier512566 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length272 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 – 272272NAD kinase HAMAP-Rule MF_00361
PRO_1000120890

Regions

Nucleotide binding50 – 512NAD By similarity
Nucleotide binding126 – 1272NAD By similarity
Nucleotide binding165 – 1706NAD By similarity

Sites

Active site501Proton acceptor By similarity
Binding site1521NAD By similarity
Binding site1541NAD By similarity
Binding site1891NAD; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
B5E4L2 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: 39C8FC194A1E794B

FASTA27231,056
        10         20         30         40         50         60 
MKNTGKRIDL IANRKPQXQR VLYELRDRLK RNQFILNXTN PDIVISIGGD GMLLSAFHKY 

        70         80         90        100        110        120 
ENQLDKVRFI GLHTGHLGFY TDYRDFELDK LVTNLQLDTG ARVSYPVLNV KVFLENGEVK 

       130        140        150        160        170        180 
IFRALNEASI RRSDRTMVAD IVINGVPFER FRGDGLTVST PTGSTAYNKS LGGAVLHPTI 

       190        200        210        220        230        240 
EALQLTEIAS LNNRVYRTLG SSIIVPKKDK IELIPTRNDY HTISVDNSVY SFRNIERIEY 

       250        260        270 
QIDHHKIHFV ATPSHTSFWN RVKDAFIGEV DE 

« Hide

References

[1]"Annotated draft genomic sequence from a Streptococcus pneumoniae type 19F clinical isolate."
Dopazo J., Mendoza A., Herrero J., Caldara F., Humbert Y., Friedli L., Guerrier M., Grand-Schenk E., Gandin C., de Francesco M., Polissi A., Buell G., Feger G., Garcia E., Peitsch M., Garcia-Bustos J.F.
Microb. Drug Resist. 7:99-125(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G54.
[2]"Pneumococcal beta glucoside metabolism investigated by whole genome comparison."
Mulas L., Trappetti C., Hakenbeck R., Iannelli F., Pozzi G., Davidsen T.M., Tettelin H., Oggioni M.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G54.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001015 Genomic DNA. Translation: ACF55804.1.
RefSeqYP_002037728.1. NC_011072.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING512566.SPG_1018.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF55804; ACF55804; SPG_1018.
GeneID6480792.
KEGGspx:SPG_1018.
PATRIC19687642. VBIStrPne77426_1073.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000275803.
KOK00858.
OMAIQMSEIA.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycSPNE512566:GCA3-1018-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_STRP4
AccessionPrimary (citable) accession number: B5E4L2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: October 14, 2008
Last modified: July 9, 2014
This is version 43 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