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Q8NQM1 (PPNK_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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:Cgl1413, cg1601
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length291 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.

Sequence caution

The sequence CAF21423.1 differs from that shown. Reason: Erroneous initiation.

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: 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 – 291291Probable inorganic polyphosphate/ATP-NAD kinase HAMAP-Rule MF_00361
PRO_0000120614

Sequences

Sequence LengthMass (Da)Tools
Q8NQM1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 9F31F00986F19573

FASTA29131,155
        10         20         30         40         50         60 
MAAKLLDDAG IDVRVLINDA DDPIAEHSVL GRFTHVRHAA DAADGAELVL VLGGDGTFLR 

        70         80         90        100        110        120 
AADMAHAVDL PVLGINLGHV GFLAEWESDS LEEALKRVID RDYRIEDRMT LTVVVLDGGG 

       130        140        150        160        170        180 
EEIGRGWALN EVSIENLNRR GVLDATLEVD ARPVASFGCD GVLISTPTGS TAYAFSAGGP 

       190        200        210        220        230        240 
VLWPELDAIL VVPNNAHALF TKPLVVSPKS TVAVESNSDT SAAMAVMDGF RPIPMPPGSR 

       250        260        270        280        290 
VEVTRGERPV RWVRLDSSPF TDRLVSKLRL PVTGWRGPQK QAENKDPRSA G 

« Hide

References

[1]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAB98806.1.
BX927152 Genomic DNA. Translation: CAF21423.1. Different initiation.
RefSeqNP_600631.1. NC_003450.3.
YP_225699.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NQM1.
SMRQ8NQM1. Positions 3-277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg1601.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB98806; BAB98806; BAB98806.
CAF21423; CAF21423; cg1601.
GeneID1019388.
3342543.
KEGGcgb:cg1601.
cgl:NCgl1358.
PATRIC21494869. VBICorGlu203724_1381.

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227223.
KOK00858.
OMAGVLWCDG.
OrthoDBEOG6PZXDR.
ProtClustDBPRK03372.

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_CORGL
AccessionPrimary (citable) accession number: Q8NQM1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: October 1, 2002
Last modified: February 19, 2014
This is version 65 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