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Q47HJ4 (NADK_DECAR) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 56. 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:Daro_0931
OrganismDechloromonas aromatica (strain RCB) [Complete proteome] [HAMAP]
Taxonomic identifier159087 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas

Protein attributes

Sequence length309 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 – 309309NAD kinase HAMAP-Rule MF_00361
PRO_0000229629

Regions

Nucleotide binding89 – 902NAD By similarity
Nucleotide binding163 – 1642NAD By similarity
Nucleotide binding204 – 2096NAD By similarity

Sites

Active site891Proton acceptor By similarity
Binding site1741NAD By similarity
Binding site1911NAD By similarity
Binding site1931NAD By similarity
Binding site2621NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q47HJ4 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 4B88B76E14A82C13

FASTA30934,363
        10         20         30         40         50         60 
MQEFDPMNRG FASYRSPRTI ALVGKYHSLE IAESLRRLAE YLYERGVSVF IERETAEHIG 

        70         80         90        100        110        120 
KIVDLSRWVT CGFNDIGAHA DLAIVLGGDG TMLNAARRLA RYCVPLVGVN QGRLGFMTDI 

       130        140        150        160        170        180 
ARDDMLTCMD DLLDGRFAPE NRMLLAAEVT RDGKEVASNM ALNDVVVDKG AIGRMIEFEL 

       190        200        210        220        230        240 
FIDGEFIYNL RSDGLIVSTP TGSTAYSMSA GGPILNPTLT GIALVPLCPH ALSNRPIIVN 

       250        260        270        280        290        300 
DNTDIELRIV NADDPRVHFD GQVTLDLERG DCVRLRRSEH TICFLHPPGY SYFAMLRQKL 


QWSERPKGP 

« Hide

References

[1]"Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: indications of a surprisingly complex life-style and cryptic anaerobic pathways for aromatic degradation."
Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., Lapidus A.
BMC Genomics 10:351-351(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RCB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000089 Genomic DNA. Translation: AAZ45687.1.
RefSeqYP_284157.1. NC_007298.1.

3D structure databases

ProteinModelPortalQ47HJ4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING159087.Daro_0931.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ45687; AAZ45687; Daro_0931.
GeneID3570245.
KEGGdar:Daro_0931.
PATRIC21600492. VBIDecAro89105_0930.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227221.
KOK00858.
OMAIRRASCA.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycDARO159087:GI5B-965-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_DECAR
AccessionPrimary (citable) accession number: Q47HJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: September 13, 2005
Last modified: July 9, 2014
This is version 56 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