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Q3BV46 (NADK_XANC5) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 54. 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:XCV1636
OrganismXanthomonas campestris pv. vesicatoria (strain 85-10) [Complete proteome] [HAMAP]
Taxonomic identifier316273 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length258 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 – 258258NAD kinase HAMAP-Rule MF_00361
PRO_0000229713

Regions

Nucleotide binding45 – 462NAD By similarity
Nucleotide binding117 – 1182NAD By similarity
Nucleotide binding158 – 1636NAD By similarity

Sites

Active site451Proton acceptor By similarity
Binding site1471NAD By similarity
Binding site1551NAD; via carbonyl oxygen By similarity
Binding site1821NAD; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3BV46 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 40C5249B0B5FEF9C

FASTA25828,428
        10         20         30         40         50         60 
MTAPPRIAFL ASPAEPAVAA RARLTQRYGD HALDSADIVC ALGGDGFMLQ TLHRHGAADK 

        70         80         90        100        110        120 
PVFGMKLGSV GFLMNQYRDN EDDLLERLQR AEPAYLRPLE MQVQTESGAS AGSLAYNEVS 

       130        140        150        160        170        180 
LLRQTRQAAH LSVDLNGQTR IAELIGDGVM VATPAGSTAY NYSAHGPILP LGSHTLALTP 

       190        200        210        220        230        240 
IAPYRPRRWR GAILKADTEV RFRVLDPYKR PVSVTADSHE IRDVVEVTIR ESTQRQVTLL 

       250 
FDPEHNLEER IFSEQFAV 

« Hide

References

[1]"Insights into genome plasticity and pathogenicity of the plant pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete genome sequence."
Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D., Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C., Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H., Niesbach-Kloesgen U. expand/collapse author list , Patschkowski T., Rueckert C., Rupp O., Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D., Kaiser O.
J. Bacteriol. 187:7254-7266(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 85-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM039952 Genomic DNA. Translation: CAJ23307.1.
RefSeqYP_363367.1. NC_007508.1.

3D structure databases

ProteinModelPortalQ3BV46.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316273.XCV1636.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ23307; CAJ23307; XCV1636.
GeneID3732989.
KEGGxcv:XCV1636.
PATRIC24092778. VBIXanCam71633_1882.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000139847.
KOK00858.
OMAHESTVSI.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycXCAM316273:GJF8-1679-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_XANC5
AccessionPrimary (citable) accession number: Q3BV46
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 22, 2005
Last modified: July 9, 2014
This is version 54 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