Q9PIG7 (NDK_CAMJE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 71.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 |
| ||||
| Organism | Campylobacter jejuni | ||||
| Taxonomic identifier | 197 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 137 AA. |
| Sequence status | Complete. |
| 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. HAMAP MF_00451 |
| Subunit structure | Homotetramer By similarity. HAMAP MF_00451 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00451. |
| 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 | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | CTP biosynthetic process Inferred from electronic annotation. Source: InterPro GTP biosynthetic processInferred from electronic annotation. Source: InterPro UTP biosynthetic processInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW nucleoside diphosphate kinase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 137 | 137 | Nucleoside diphosphate kinase HAMAP MF_00451 | PRO_0000136960 | |||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||
| Active site | 115 | 1 | Pros-phosphohistidine intermediate By similarity | ||||||||||||||||||||||||||||||||||
| Binding site | 9 | 1 | ATP By similarity | ||||||||||||||||||||||||||||||||||
| Binding site | 57 | 1 | ATP By similarity | ||||||||||||||||||||||||||||||||||
| Binding site | 85 | 1 | ATP By similarity | ||||||||||||||||||||||||||||||||||
| Binding site | 91 | 1 | ATP By similarity | ||||||||||||||||||||||||||||||||||
| Binding site | 102 | 1 | ATP By similarity | ||||||||||||||||||||||||||||||||||
| Binding site | 112 | 1 | ATP By similarity | ||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||
| Beta strand | 4 – 8 | 5 | |||||||||||||||||||||||||||||||||||
| Helix | 10 – 14 | 5 | |||||||||||||||||||||||||||||||||||
| Helix | 21 – 26 | 6 | |||||||||||||||||||||||||||||||||||
| Beta strand | 31 – 38 | 8 | |||||||||||||||||||||||||||||||||||
| Helix | 42 – 48 | 7 | |||||||||||||||||||||||||||||||||||
| Helix | 50 – 52 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 58 – 65 | 8 | |||||||||||||||||||||||||||||||||||
| Beta strand | 70 – 76 | 7 | |||||||||||||||||||||||||||||||||||
| Helix | 81 – 87 | 7 | |||||||||||||||||||||||||||||||||||
| Helix | 93 – 95 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 101 – 105 | 5 | |||||||||||||||||||||||||||||||||||
| Beta strand | 108 – 111 | 4 | |||||||||||||||||||||||||||||||||||
| Beta strand | 113 – 115 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 120 – 130 | 11 | |||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. Barrell B.G.Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AL111168 Genomic DNA. Translation: CAL34483.1. | ||||||||||||
| PIR | H81452. | ||||||||||||
| RefSeq | YP_002343770.1. NC_002163.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q9PIG7. | ||||||||||||
| SMR | Q9PIG7. Positions 1-136. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q9PIG7. 48 interactions. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 904656. | ||||||||||||
| GenomeReviews | Gene locus Cj0332c in contig AL111168_GR. | ||||||||||||
| KEGG | cje:Cj0332c. | ||||||||||||
| PATRIC | 20057581. VBICamJej33762_0324. | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | HBG445152. | ||||||||||||
| OMA | ERPFFGA. | ||||||||||||
| ProtClustDB | PRK00668. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | CJEJ192222:CJ0332C-MONOMER. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_00451. NDP_kinase. [Tree] | ||||||||||||
| InterPro | IPR001564. Nucleoside_diP_kinase. IPR023005. Nucleoside_diP_kinase_AS. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.30.70.141. NDK. 1 hit. | ||||||||||||
| KO | K00940. | ||||||||||||
| PANTHER | PTHR11349. Nuc_diP_kinase_core. 1 hit. | ||||||||||||
| Pfam | PF00334. NDK. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR01243. NUCDPKINASE. | ||||||||||||
| SMART | SM00562. NDK. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF54919. NDK. 1 hit. | ||||||||||||
| PROSITE | PS00469. NDP_KINASES. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | NDK_CAMJE | ||||||||
| Accession | Primary (citable) accession number: Q9PIG7 Secondary accession number(s): Q0PBH7 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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