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Q30Y32 (NADK_DESAG) 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:Dde_2618
OrganismDesulfovibrio alaskensis (strain G20) (Desulfovibrio desulfuricans (strain G20)) [Complete proteome] [HAMAP]
Taxonomic identifier207559 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length292 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 – 292292NAD kinase HAMAP-Rule MF_00361
PRO_0000229633

Regions

Nucleotide binding64 – 652NAD By similarity
Nucleotide binding138 – 1392NAD By similarity
Nucleotide binding179 – 1846NAD By similarity

Sites

Active site641Proton acceptor By similarity
Binding site1491NAD By similarity
Binding site1661NAD By similarity
Binding site1681NAD By similarity
Binding site2381NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q30Y32 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: ED4AEEE194F3CE98

FASTA29230,944
        10         20         30         40         50         60 
MHRELKRVFI VTKQAHAGAA ALAADMQAWF AARGIEAATE ENDTASALPD FARSASCIMV 

        70         80         90        100        110        120 
LGGDGTMLSV SRRAVGLDVP LLGVNLGKVG FLAEVSAAGW QQAFTRLAEN GLTCSERLAL 

       130        140        150        160        170        180 
HFAVSREGRC VFEGTAVNDV VLHRGVLARV INLGLGVDGE WLGDLRADGL IVSTPTGATG 

       190        200        210        220        230        240 
YAVSAGGPLV HPDMSVYAIT PICPFLNNFH PMVLAGSMRF EIRILEGPQE VYVTQDGQEC 

       250        260        270        280        290 
FALQAGDLVT VTQASRGLLF VAVEGSTYFT RLRAKGFVRD PRGRGRAVPA SS 

« Hide

References

[1]"Complete genome sequence and updated annotation of Desulfovibrio alaskensis G20."
Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L., Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S., Nolan M. expand/collapse author list , Lapidus A.L., Palumbo A.V., Wall J.D.
J. Bacteriol. 193:4268-4269(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G20.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000112 Genomic DNA. Translation: ABB39414.1.
RefSeqYP_389109.1. NC_007519.1.

3D structure databases

ProteinModelPortalQ30Y32.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING207559.Dde_2618.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB39414; ABB39414; Dde_2618.
GeneID3757640.
KEGGdde:Dde_2618.
PATRIC21744179. VBIDesDes50040_2586.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227222.
KOK00858.
OMAICPFLNN.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycDALA207559:GH1L-2343-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_DESAG
AccessionPrimary (citable) accession number: Q30Y32
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: December 6, 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