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Q5E3A4 (NADK_VIBF1) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 56. 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:VF_1997
OrganismVibrio fischeri (strain ATCC 700601 / ES114) [Reference proteome] [HAMAP]
Taxonomic identifier312309 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

Protein attributes

Sequence length297 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 – 297297NAD kinase HAMAP-Rule MF_00361
PRO_0000229710

Regions

Nucleotide binding77 – 782NAD By similarity
Nucleotide binding151 – 1522NAD By similarity
Nucleotide binding192 – 1976NAD By similarity

Sites

Active site771Proton acceptor By similarity
Binding site1621NAD By similarity
Binding site1791NAD By similarity
Binding site1811NAD By similarity
Binding site2521NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5E3A4 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: EAA30205EC28070A

FASTA29733,071
        10         20         30         40         50         60 
MMDMKRAFNV IAIIGKPRDP NAIKTHLSIY HWLTDQNYTV LLDDRLREAL PEIPADRFNH 

        70         80         90        100        110        120 
LLKLGELADL AIVVGGDGNM LGAARVLSRF DISVIGVNRG NLGFLTDLDP DNFEEPLQAV 

       130        140        150        160        170        180 
LNGDFVKEER FLLEAEVHRH GQVKSHNSAF NEVVLHPGQV AHMIEFEVYI DDTFAFSQRS 

       190        200        210        220        230        240 
DGLIISTPTG STAYSLSGGG PILSPNLNAI SIVPMFPHTL SSRPLVVEGK RHIKLCISPE 

       250        260        270        280        290 
NRTTLEVSCD GQVSLPVSPG DEVHIFQSPS RLKLIHPKDY SYYHILRNKL GWSSKLF 

« Hide

References

[1]"Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with pathogenic congeners."
Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., Stevens A., Visick K., Whistler C., Greenberg E.P.
Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700601 / ES114.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000020 Genomic DNA. Translation: AAW86492.1.
RefSeqYP_205380.1. NC_006840.2.

3D structure databases

ProteinModelPortalQ5E3A4.
SMRQ5E3A4. Positions 7-297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING312309.VF_1997.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW86492; AAW86492; VF_1997.
GeneID3279125.
KEGGvfi:VF_1997.
PATRIC20114686. VBIVibFis127983_2024.

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227221.
KOK00858.
OMATHEMLYH.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycAFIS312309:GIWP-2099-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_VIBF1
AccessionPrimary (citable) accession number: Q5E3A4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: March 15, 2005
Last modified: July 9, 2014
This is version 56 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