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B2SXB6 (NADK_BURPP) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 41. 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:Bphyt_0731
OrganismBurkholderia phytofirmans (strain DSM 17436 / PsJN) [Complete proteome] [HAMAP]
Taxonomic identifier398527 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length300 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 – 300300NAD kinase HAMAP-Rule MF_00361
PRO_1000120837

Regions

Nucleotide binding75 – 762NAD By similarity
Nucleotide binding149 – 1502NAD By similarity
Nucleotide binding190 – 1956NAD By similarity

Sites

Active site751Proton acceptor By similarity
Binding site1771NAD By similarity
Binding site1791NAD By similarity
Binding site2141NAD; via carbonyl oxygen By similarity
Binding site2481NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
B2SXB6 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 298D901CEA3F087F

FASTA30032,739
        10         20         30         40         50         60 
MQVTSQFKTV ALVGRNNTPG IAEPLTALAS CIAKRGFEVV FEADTAAEIG VTDYPALRPA 

        70         80         90        100        110        120 
EIGARADVAV VLGGDGTMLG IGRQLAPYRT PLIGINHGRL GFITDIPISD MREIVPQMLS 

       130        140        150        160        170        180 
GNFEREERVL LEARIMRGGN PIYHALAFND VVVNRSGFSG MAELHVSVDG RFMYNQRSDG 

       190        200        210        220        230        240 
LIVATPTGST AYALSSQGPI LHPQLQGIVL VPIAPHALSN RPIVLPDDSK VSIQIVSGRE 

       250        260        270        280        290        300 
VNVNFDMQSF TSLELGDTIE VRRSRHTVPM LHPVGYSFFT TLRKKLHWNE YPSHEEDSKP 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia phytofirmans PsJN."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Nowak J., Sessitsch A., Lazarovits G., Compant S., Barka E., Tiedje J.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17436 / PsJN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001052 Genomic DNA. Translation: ACD15155.1.
RefSeqYP_001894379.1. NC_010681.1.

3D structure databases

ProteinModelPortalB2SXB6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398527.Bphyt_0731.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD15155; ACD15155; Bphyt_0731.
GeneID6282089.
KEGGbpy:Bphyt_0731.
PATRIC19211395. VBIBurPhy117947_4486.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227221.
KOK00858.
OMAHPSIPGW.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycBPHY398527:GJEX-734-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_BURPP
AccessionPrimary (citable) accession number: B2SXB6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: July 9, 2014
This is version 41 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