Reviewed,
UniProtKB/Swiss-Prot P31103 (NDK_BACSU)
Last modified
November 3, 2009.
Version 73.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Nucleoside diphosphate kinase Short name=NDK Short name=NDP kinase EC=2.7.4.6 Alternative name(s): Nucleoside-2-P kinase | ||||
| Gene names |
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| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1423 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 149 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. HAMAP MF_00451 |
| Catalytic activity | ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. HAMAP MF_00451 |
| Cofactor | Magnesium By similarity. |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the NDK family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Nucleotide metabolism |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | CTP biosynthetic process Inferred from electronic annotation. Source: HAMAP GTP biosynthetic processInferred from electronic annotation. Source: HAMAP UTP biosynthetic processInferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: HAMAP magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW nucleoside diphosphate kinase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 149 | 149 | Nucleoside diphosphate kinase HAMAP MF_00451 | PRO_0000136946 | |||||
Sites | |||||||||
| Active site | 116 | 1 | Pros-phosphohistidine intermediate By similarity | ||||||
| Binding site | 10 | 1 | ATP By similarity | ||||||
| Binding site | 58 | 1 | ATP By similarity | ||||||
| Binding site | 86 | 1 | ATP By similarity | ||||||
| Binding site | 92 | 1 | ATP By similarity | ||||||
| Binding site | 103 | 1 | ATP By similarity | ||||||
| Binding site | 113 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 92 | 1 | Phosphothreonine Ref.3 | ||||||
| Modified residue | 123 | 1 | Phosphoserine Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequence of Bacillus subtilis dbpA, mtr(A,B), gerC(1-3), ndk, cheR, aro(B,E,F,H), trp(A-F), hisH, and tyrA genes." Henner D.J. Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [3] | "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis." Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M. Mol. Cell. Proteomics 6:697-707(2007) [PubMed: 17218307] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-92 AND SER-123, MASS SPECTROMETRY. |
Cross-references
Sequence databases | |
|---|---|
| M80245 Genomic DNA. Translation: AAA20857.1. AL009126 Genomic DNA. Translation: CAB14189.1. | |
| PIR | D69666. |
| RefSeq | NP_390154.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1NPK based on UniProtKB P22887. |
| ModBase | Search... |
PTM databases | |
| PhosSite | P31103. |
Genome annotation databases | |
| GeneID | 938997. |
| GenomeReviews | Gene locus BSU22730 in contig AL009126_GR. |
| KEGG | bsu:BSU22730. |
| NMPDR | fig|224308.1.peg.2277. |
Organism-specific databases | |
| SubtiList | BG10282. ndk. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P31103. |
| OMA | NLTGAIT. |
Enzyme and pathway databases | |
| BioCyc | BSUB224308:BSU2272-MON. |
| BRENDA | 2.7.4.6. 150. |
Family and domain databases | |
| HAMAP | MF_00451. [Tree] |
| InterPro | IPR001564. Nuc_diP_kinase_core. [Graphical view] |
| Gene3D | G3DSA:3.30.70.141. NDK. 1 hit. |
| PANTHER | PTHR11349. Nuc_diP_kinase_core. 1 hit. |
| Pfam | PF00334. NDK. 1 hit. [Graphical view] |
| PRINTS | PR01243. NUCDPKINASE. |
| ProDom | PD001018. NDK. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00562. NDK. 1 hit. [Graphical view] |
| PROSITE | PS00469. NDP_KINASES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NDK_BACSU | ||||||||
| Accession | Primary (citable) accession number: P31103 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| SIMILARITY comments Index of protein domains and families |

Clusters with


