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P73955 (NADK2_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 2

EC=2.7.1.23
Alternative name(s):
ATP-dependent NAD kinase 2
Gene names
Name:nadK2
Ordered Locus Names:sll1415
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length307 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
Reference 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 – 307307NAD kinase 2 HAMAP-Rule MF_00361
PRO_0000120679

Regions

Nucleotide binding67 – 682NAD By similarity
Nucleotide binding149 – 1502NAD By similarity
Nucleotide binding192 – 1976NAD By similarity

Sites

Active site671Proton acceptor By similarity
Binding site1601NAD By similarity
Binding site1811NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
P73955 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 64EA0964EE45F4EF

FASTA30733,776
        10         20         30         40         50         60 
MELKQVIIAH KAGHNESKTY AERCARELEA RGCKVLMGPS GIKDNPYPVF LASATEKIDL 

        70         80         90        100        110        120 
ALVLGGDGTT LAAARHLSPE GIPILSVNVG GHLGFLTEPF DVFQDTQKVW DRLNQDRYAV 

       130        140        150        160        170        180 
SQRMMLAASL FEGDRRDPQM VGETYYCLNE MCIKPASIDR MPTAIIEVEV DGELIDQYQC 

       190        200        210        220        230        240 
DGLLVATPTG STCYTSSANG PILHPGMDAI VITPICPLSL SSRPIVIPPG SSVNIWPLGD 

       250        260        270        280        290        300 
FELNTKLWTD GSLATGVWPG QRVGVWMAHR AAQFILLRES YSFYKTLRDK LQWAGARFLY 


DGNNKVN 

« Hide

References

[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / Kazusa.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000022 Genomic DNA. Translation: BAA18022.1.
PIRS75461.
RefSeqNP_441342.1. NC_000911.1.
YP_005651399.1. NC_017277.1.
YP_007451224.1. NC_020286.1.

3D structure databases

ProteinModelPortalP73955.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING1148.sll1415.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA18022; BAA18022; BAA18022.
GeneID954689.
KEGGsyn:sll1415.
syy:SYNGTS_1446.
syz:MYO_114590.
PATRIC23840058. VBISynSp132158_1589.

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227222.
KOK00858.
OMAKLHWAGS.
OrthoDBEOG6PZXDR.
PhylomeDBP73955.

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 nameNADK2_SYNY3
AccessionPrimary (citable) accession number: P73955
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 1, 1997
Last modified: July 9, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families