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Q83IC3 (NADK_TROW8) 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:TW112
OrganismTropheryma whipplei (strain TW08/27) (Whipple's bacillus) [Complete proteome] [HAMAP]
Taxonomic identifier218496 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeTropheryma

Protein attributes

Sequence length305 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 – 305305NAD kinase HAMAP-Rule MF_00361
PRO_0000120684

Regions

Nucleotide binding88 – 892NAD By similarity
Nucleotide binding162 – 1632NAD By similarity
Nucleotide binding203 – 2086NAD By similarity

Sites

Active site881Proton acceptor By similarity
Binding site931NAD By similarity
Binding site1731NAD By similarity
Binding site1921NAD By similarity
Binding site2621NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83IC3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: C53563B959052E5D

FASTA30533,273
        10         20         30         40         50         60 
MRVYIAHNGC LEAEPIYGTI CELVAQRKMS VITDPHARNN ESARNTDSGV VSLNQAGRNK 

        70         80         90        100        110        120 
YLDQETTSPA TSRSINVPFC AGISIGGDGT FLRMARDLKN TGTPLFGVNM GRMGFLVDIE 

       130        140        150        160        170        180 
PEDIVNLVEN IVKGEYTEEK RLPITASVQR GGKKIHDEWA VNEITIERKV EGKVVDIEVF 

       190        200        210        220        230        240 
VDGCRVMDIS CNGIIIATAT GSTAYSFSSG GPIVWPEMKV TLVVPVSPHE LFAKPIVLPD 

       250        260        270        280        290        300 
NRSILLKVTS RDNKVVLCSD GQVRLCLQSG DEIACHVGKV PVVFGRVKKG CFAEHLVKKF 


NLQTA 

« Hide

References

[1]"Sequencing and analysis of the genome of the Whipple's disease bacterium Tropheryma whipplei."
Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G., Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A., Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J., Relman D.A.
Lancet 361:637-644(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW08/27.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX251410 Genomic DNA. Translation: CAD66795.1.
RefSeqNP_789058.1. NC_004551.1.

3D structure databases

ProteinModelPortalQ83IC3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING218496.TW112.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD66795; CAD66795; TW112.
GeneID1064410.
KEGGtws:TW112.
PATRIC23998574. VBITroWhi42739_0133.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000115663.
KOK00858.
OMAGVLWCDG.
OrthoDBEOG6PZXDR.

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_TROW8
AccessionPrimary (citable) accession number: Q83IC3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: June 1, 2003
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