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A5ILH3 (NADK_THEP1) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 49. 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:Tpet_1028
OrganismThermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995) [Complete proteome] [HAMAP]
Taxonomic identifier390874 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

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_1000005453

Regions

Nucleotide binding51 – 522NAD By similarity
Nucleotide binding119 – 1202NAD By similarity
Nucleotide binding160 – 1656NAD By similarity

Sites

Active site511Proton acceptor By similarity
Binding site561NAD By similarity
Binding site1301NAD By similarity
Binding site1491NAD By similarity
Binding site1841NAD; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A5ILH3 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 45EBBE2A1C5790AB

FASTA25829,241
        10         20         30         40         50         60 
MKIAILYREE REKEGKFLKE KISKEHEVIE FGEANAPGRV TADLIVVVGG DGTVLKAAKK 

        70         80         90        100        110        120 
AADGTPMVGF KAGRLGFLTS YTLDEIDRFL EDLRNWNFRE ETRWFIQIES ELGNHLALND 

       130        140        150        160        170        180 
VTLERDLSGK MVEIEVEVEH HSSMWFFADG VVISTPTGST AYSLSIGGPI IFPECEVLEI 

       190        200        210        220        230        240 
SPIAPQFFLT RSVVIPSNFK VVVESQRDIN MLVDGVLTGK TKRIEVKKSR RYVRILRPPE 

       250 
YDYVTVIRDK LGYGRRIE 

« Hide

References

[1]"Complete sequence of Thermotoga petrophila RKU-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RKU-1 / ATCC BAA-488 / DSM 13995.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000702 Genomic DNA. Translation: ABQ47046.1.
RefSeqYP_001244622.1. NC_009486.1.

3D structure databases

ProteinModelPortalA5ILH3.
SMRA5ILH3. Positions 1-256.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING390874.Tpet_1028.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ47046; ABQ47046; Tpet_1028.
GeneID5170299.
KEGGtpt:Tpet_1028.
PATRIC23944852. VBIThePet65348_1039.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227222.
KOK00858.
OMAHPSIPGW.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycTPET390874:GHJI-1058-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_THEP1
AccessionPrimary (citable) accession number: A5ILH3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 26, 2007
Last modified: July 9, 2014
This is version 49 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