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Q65LA2 (PPNK1_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. 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 1

Short name=Poly(P)/ATP NAD kinase 1
EC=2.7.1.23
Gene names
Name:ppnK1
Ordered Locus Names:BLi01255, BL05111
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length267 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 – 267267Probable inorganic polyphosphate/ATP-NAD kinase 1 HAMAP-Rule MF_00361
PRO_0000229604

Sequences

Sequence LengthMass (Da)Tools
Q65LA2 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 4BBC6CD6CD5EA750

FASTA26729,670
        10         20         30         40         50         60 
MMKFAVSSKG NAVSDSLKSK IQTYLLDFGL ECDEEEPDIV ISVGGDGTLL YAFHKYSGRL 

        70         80         90        100        110        120 
DKTAFVGVHT GHLGFYADWV PSEIEKLVIA IAKTPYQIVE YPVLEVIVRY NDGSDEARYL 

       130        140        150        160        170        180 
ALNECTIKSI EGTLVTDVEI KGELFETFRG DGLCLSTPSG STAYNKALGG AIIHPSIRAI 

       190        200        210        220        230        240 
QLAEMASINN RVFRTVGSPL ILPEHHTCLI KPINDVTFQV AIDHLTLLHK DVKSIQCRVA 

       250        260 
NENIRFARFR PFPFWKRVQD SFIGKGE 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[3]Berka R.M., Rey M.W., Ramaiya P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 152.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017333 Genomic DNA. Translation: AAU40162.1.
CP000002 Genomic DNA. Translation: AAU22817.2.
RefSeqYP_006712636.1. NC_006322.1.
YP_078455.2. NC_006270.3.

3D structure databases

ProteinModelPortalQ65LA2.
SMRQ65LA2. Positions 2-263.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279010.BL05111.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU22817; AAU22817; BL05111.
AAU40162; AAU40162; BLi01255.
GeneID3030258.
3098767.
KEGGbld:BLi01255.
bli:BL05111.
PATRIC18948083. VBIBacLic203714_1246.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000275803.
KOK00858.
OMAWDRVEDA.
OrthoDBEOG6PZXDR.
ProtClustDBPRK04885.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-1247-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 namePPNK1_BACLD
AccessionPrimary (citable) accession number: Q65LA2
Secondary accession number(s): Q62WP1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 25, 2004
Last modified: February 19, 2014
This is version 62 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