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A6LN85 (NADK_THEM4) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 48. 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:Tmel_1541
OrganismThermosipho melanesiensis (strain BI429 / DSM 12029) [Complete proteome] [HAMAP]
Taxonomic identifier391009 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermosipho

Protein attributes

Sequence length251 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 – 251251NAD kinase HAMAP-Rule MF_00361
PRO_1000005452

Regions

Nucleotide binding51 – 522NAD By similarity
Nucleotide binding113 – 1142NAD By similarity
Nucleotide binding153 – 1586NAD By similarity

Sites

Active site511Proton acceptor By similarity
Binding site561NAD By similarity
Binding site1241NAD By similarity
Binding site1401NAD By similarity
Binding site1421NAD By similarity
Binding site1771NAD; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A6LN85 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 913D3822AAA77512

FASTA25128,453
        10         20         30         40         50         60 
MKVLGIFHKP SLKSVAEKFS EILFDENFHV EYVGSEIPSI EVDLTLVLGG DGTFLKAAHK 

        70         80         90        100        110        120 
VRNPLVGFKG GRLGFLSSYT LGDFDKFLED LKNENFERDI RYFLKAGDFY TLNEVLLIRD 

       130        140        150        160        170        180 
PVQKMVDIQI FFQDGDFYFH ADGLIISTPT GSTGYSLSLG GPIMLPNVNS FVITPVAPQF 

       190        200        210        220        230        240 
LASRSIIVPD DEEIIVRIDQ EINLILDGMD FGKVREVNLK KSRRRIVILR PKDYNFSKSI 

       250 
KEKLGYGKRF L 

« Hide

References

[1]"Complete sequence of Thermosipho melanesiensis BI429."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , 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: BI429 / DSM 12029.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000716 Genomic DNA. Translation: ABR31386.1.
RefSeqYP_001306771.1. NC_009616.1.

3D structure databases

ProteinModelPortalA6LN85.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391009.Tmel_1541.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR31386; ABR31386; Tmel_1541.
GeneID5297193.
KEGGtme:Tmel_1541.
PATRIC23924371. VBITheMel19269_1600.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227222.
KOK00858.
OMAGPIMLPN.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycTMEL391009:GHM1-1602-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_THEM4
AccessionPrimary (citable) accession number: A6LN85
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 24, 2007
Last modified: July 9, 2014
This is version 48 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