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Q5PFG7 (PPNK_SALPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:
Probable inorganic polyphosphate/ATP-NAD kinase

Short name=Poly(P)/ATP NAD kinase
EC=2.7.1.23
Gene names
Name:ppnK
Ordered Locus Names:SPA2542
OrganismSalmonella paratyphi A (strain ATCC 9150 / SARB42) [Complete proteome] [HAMAP]
Taxonomic identifier295319 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the phosphorylation of NAD to NADP. Utilizes ATP and other nucleoside triphosphates as well as inorganic polyphosphate as a source of phosphorus 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: InterPro

   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 – 292292Probable inorganic polyphosphate/ATP-NAD kinase HAMAP-Rule MF_00361
PRO_0000229686

Sequences

Sequence LengthMass (Da)Tools
Q5PFG7 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 93585C83A2EEF41C

FASTA29232,584
        10         20         30         40         50         60 
MNNHFKCIGI VGHPRHPTAL TTHEMLYRWL CDQGYEVIVE QQIAHELQLK NVPTGTLAEI 

        70         80         90        100        110        120 
GQQADLAVVV GGDGNMLGAA RTLARYDINV IGINRGNLGF LTDLDPDNAL QQLSDVLEGR 

       130        140        150        160        170        180 
YISEKRFLLE AQVCQQDRQK RISTAINEVV LHPGKVAHMI EFEVYIDETF AFSQRSDGLI 

       190        200        210        220        230        240 
ISTPTGSTAY SLSAGGPILT PSLDAITLVP MFPHTLSARP LVINSSSTIR LRFSHRRSDL 

       250        260        270        280        290 
EISCDSQIAL PIQEGEDVLI RRCDYHLNLI HPKDYSYFNT LSTKLGWSKK LF 

« Hide

References

[1]"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid."
McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. expand/collapse author list , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K.
Nat. Genet. 36:1268-1274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000026 Genomic DNA. Translation: AAV78411.1.
RefSeqYP_151723.1. NC_006511.1.

3D structure databases

ProteinModelPortalQ5PFG7.
SMRQ5PFG7. Positions 4-292.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING295319.SPA2542.

Proteomic databases

PRIDEQ5PFG7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV78411; AAV78411; SPA2542.
PATRIC32354597. VBISalEnt134188_2701.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227221.
OMAGMVELRV.
OrthoDBEOG6PZXDR.
ProtClustDBPRK03378.

Enzyme and pathway databases

BioCycSENT295319:GJBZ-2541-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_prd.
[Graphical view]
PANTHERPTHR20275. PTHR20275. 1 hit.
PfamPF01513. NAD_kinase. 1 hit.
[Graphical view]
SUPFAMSSF111331. SSF111331. 1 hit.
ProtoNetSearch...

Entry information

Entry namePPNK_SALPA
AccessionPrimary (citable) accession number: Q5PFG7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 4, 2005
Last modified: February 19, 2014
This is version 54 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