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Q6A7W9 (NADK_PROAC) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 59. 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:PPA1395
OrganismPropionibacterium acnes (strain KPA171202 / DSM 16379) [Complete proteome] [HAMAP]
Taxonomic identifier267747 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium

Protein attributes

Sequence length318 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 – 318318NAD kinase HAMAP-Rule MF_00361
PRO_0000229676

Regions

Nucleotide binding84 – 852NAD By similarity
Nucleotide binding159 – 1602NAD By similarity
Nucleotide binding200 – 2056NAD By similarity

Sites

Active site841Proton acceptor By similarity
Binding site891NAD By similarity
Binding site1701NAD By similarity
Binding site1891NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6A7W9 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: FD155F9C1DA16E6A

FASTA31834,945
        10         20         30         40         50         60 
MGRYCGLVND TSPSRYVVVV THATRDDAFD AAAEFISEMA GRDIGCAVPD DQAKPMSSKL 

        70         80         90        100        110        120 
PGIDLESLGE FAHEAEVVVV FGGDGTILRA AEWSLPRHVP MIGVNLGHVG FLAELERSDM 

       130        140        150        160        170        180 
ADLVNKVCSR DYTVEDRLVL KTTVTEHSGQ HRWSSFAVNE LSLEKAARRR MLDVLASVDE 

       190        200        210        220        230        240 
LPVQRWSCDG ILVSTPTGST AYAFSAGGPV MWPDLDAMLM VPLSAHALFA RPLVMSPAAR 

       250        260        270        280        290        300 
VDLDIQPDGS ESAVLWCDGR RSCTVRPGER ITVVRHPDRL RIARLAAQPF TSRLVKKFEL 

       310 
PVSGWRQGRD RHHLEETS 

« Hide

References

[1]"The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
Science 305:671-673(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017283 Genomic DNA. Translation: AAT83146.1.
RefSeqYP_056104.1. NC_006085.1.

3D structure databases

ProteinModelPortalQ6A7W9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267747.PPA1395.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT83146; AAT83146; PPA1395.
GeneID2931825.
KEGGpac:PPA1395.
PATRIC23037555. VBIProAcn64440_1440.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227223.
KOK00858.
OMAGVLWCDG.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycPACN267747:GHO9-1417-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_PROAC
AccessionPrimary (citable) accession number: Q6A7W9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: September 13, 2004
Last modified: July 9, 2014
This is version 59 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