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B0S255 (NADK_FINM2) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 40. 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:FMG_1027
OrganismFinegoldia magna (strain ATCC 29328) (Peptostreptococcus magnus) [Complete proteome] [HAMAP]
Taxonomic identifier334413 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiales Family XI. Incertae SedisFinegoldia

Protein attributes

Sequence length273 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 – 273273NAD kinase HAMAP-Rule MF_00361
PRO_1000205417

Regions

Nucleotide binding53 – 542NAD By similarity
Nucleotide binding128 – 1292NAD By similarity
Nucleotide binding168 – 1736NAD By similarity

Sites

Active site531Proton acceptor By similarity
Binding site581NAD By similarity
Binding site1571NAD By similarity
Binding site1921NAD; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
B0S255 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 469FEEC9B9D5247F

FASTA27330,856
        10         20         30         40         50         60 
MNNNSKIINI YVNDNQKSLE TALIVKDKLE QKGFKPTFDF DENALINLCI GGDGAFLRAV 

        70         80         90        100        110        120 
HKYEFSTIPF VGINTGHLGF YQEILIPNID KFISDLINEN YGIEKISLLE SKTAIRNSSK 

       130        140        150        160        170        180 
TYTHKALNEF VVKSDDSSIV YLDVYIDDNH LESFAGDGII VSTPSGSTAY NFSAGGSVLY 

       190        200        210        220        230        240 
HGLDGFQVTP LAPINSKAYR SLLNSLVVPS KSNVTLYFRD HNFDRKSSIV LADGLNRSYD 

       250        260        270 
NVDYVNFTYS DQYINKLVFL KDWYWLNIKD KFL 

« Hide

References

[1]"Complete genome sequence of Finegoldia magna, an anaerobic opportunistic pathogen."
Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K., Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.
DNA Res. 15:39-47(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29328.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008971 Genomic DNA. Translation: BAG08445.1.
RefSeqYP_001692335.1. NC_010376.1.

3D structure databases

ProteinModelPortalB0S255.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING334413.FMG_1027.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG08445; BAG08445; FMG_1027.
GeneID6018919.
KEGGfma:FMG_1027.
PATRIC21887731. VBIFinMag33027_1232.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000221177.
KOK00858.
OMAIQMSEIA.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycFMAG334413:GJ6M-1078-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_FINM2
AccessionPrimary (citable) accession number: B0S255
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: April 8, 2008
Last modified: July 9, 2014
This is version 40 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