P0A763 (NDK_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 78.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·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 | Escherichia coli (strain K12) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 143 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| 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-Rule MF_00451 |
| Catalytic activity | ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. HAMAP-Rule MF_00451 |
| Cofactor | Magnesium By similarity. HAMAP-Rule MF_00451 |
| Subunit structure | Homotetramer. |
| Subcellular location | |
| 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 Direct protein sequencing Reference 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 metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW nucleoside diphosphate kinase activityInferred from direct assay PubMed 214126. Source: EcoCyc |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| ung | P12295 | 3 | EBI-370139,EBI-559403 | |
| ygfA | P0AC28 | 3 | EBI-370139,EBI-555094 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.5 Ref.7 Ref.8 | ||||||||||||||||||||||||||||||||||
| Chain | 2 – 143 | 142 | Nucleoside diphosphate kinase HAMAP-Rule MF_00451 | PRO_0000136978 | |||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||
| Active site | 117 | 1 | Pros-phosphohistidine intermediate | ||||||||||||||||||||||||||||||||||
| Binding site | 11 | 1 | ATP By similarity | ||||||||||||||||||||||||||||||||||
| Binding site | 59 | 1 | ATP By similarity | ||||||||||||||||||||||||||||||||||
| Binding site | 87 | 1 | ATP By similarity | ||||||||||||||||||||||||||||||||||
| Binding site | 93 | 1 | ATP By similarity | ||||||||||||||||||||||||||||||||||
| Binding site | 104 | 1 | ATP By similarity | ||||||||||||||||||||||||||||||||||
| Binding site | 114 | 1 | ATP By similarity | ||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||
| Modified residue | 119 | 1 | Phosphoserine HAMAP-Rule MF_00451 | ||||||||||||||||||||||||||||||||||
| Modified residue | 121 | 1 | Phosphoserine HAMAP-Rule MF_00451 | ||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||
| Beta strand | 3 – 10 | 8 | |||||||||||||||||||||||||||||||||||
| Helix | 12 – 16 | 5 | |||||||||||||||||||||||||||||||||||
| Helix | 20 – 29 | 10 | |||||||||||||||||||||||||||||||||||
| Beta strand | 33 – 40 | 8 | |||||||||||||||||||||||||||||||||||
| Helix | 44 – 50 | 7 | |||||||||||||||||||||||||||||||||||
| Helix | 52 – 54 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 60 – 67 | 8 | |||||||||||||||||||||||||||||||||||
| Beta strand | 72 – 80 | 9 | |||||||||||||||||||||||||||||||||||
| Helix | 82 – 90 | 9 | |||||||||||||||||||||||||||||||||||
| Turn | 95 – 97 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 103 – 107 | 5 | |||||||||||||||||||||||||||||||||||
| Beta strand | 109 – 111 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 115 – 118 | 4 | |||||||||||||||||||||||||||||||||||
| Helix | 122 – 132 | 11 | |||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Nucleoside diphosphate kinase from Escherichia coli; its overproduction and sequence comparison with eukaryotic enzymes." Hama H., Almaula N., Lerner C.G., Inouye S., Inouye M. Gene 105:31-36(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12. |
| [2] | "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. Horiuchi T.DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [3] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [4] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [5] | "Nucleoside diphosphokinase: a functional link between intermediary metabolism and nucleic acid synthesis." Ray N.B., Mathews C.K. Curr. Top. Cell. Regul. 33:343-357(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-46. |
| [6] | "Nucleoside diphosphate kinase from Escherichia coli." Almaula N., Lu Q., Delgado J., Belkin S., Inouye M. J. Bacteriol. 177:2524-2529(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, PARTIAL PROTEIN SEQUENCE. |
| [7] | Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F. Submitted (FEB-1996) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-12. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [8] | "Identification of phosphoproteins in Escherichia coli." Freestone P., Grant S., Toth I., Norris V. Mol. Microbiol. 15:573-580(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11, PHOSPHORYLATION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | X57555 Genomic DNA. Translation: CAA40780.1. U00096 Genomic DNA. Translation: AAC75571.1. AP009048 Genomic DNA. Translation: BAA16405.1. | ||||||||||||
| PIR | JH0495. | ||||||||||||
| RefSeq | NP_417013.1. NC_000913.2. YP_490746.1. NC_007779.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P0A763. | ||||||||||||
| SMR | P0A763. Positions 2-143. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP-31870N. | ||||||||||||
| IntAct | P0A763. 6 interactions. | ||||||||||||
| MINT | MINT-1255778. | ||||||||||||
| STRING | 511145.b2518. | ||||||||||||
PTM databases | |||||||||||||
| PhosSite | P0809416. | ||||||||||||
2D gel databases | |||||||||||||
| SWISS-2DPAGE | P0A763. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | P0A763. | ||||||||||||
| PRIDE | P0A763. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | AAC75571; AAC75571; b2518. BAA16405; BAA16405; BAA16405. | ||||||||||||
| GeneID | 12930715. 945611. | ||||||||||||
| KEGG | ecj:Y75_p2471. eco:b2518. | ||||||||||||
| PATRIC | 32120429. VBIEscCol129921_2617. | ||||||||||||
Organism-specific databases | |||||||||||||
| EchoBASE | EB0644. | ||||||||||||
| EcoGene | EG10650. ndk. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0105. | ||||||||||||
| HOGENOM | HOG000224565. | ||||||||||||
| KO | K00940. | ||||||||||||
| OMA | FRVVAMK. | ||||||||||||
| ProtClustDB | PRK00668. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | EcoCyc:NUCLEOSIDE-DIP-KIN-MONOMER. ECOL316407:JW2502-MONOMER. MetaCyc:NUCLEOSIDE-DIP-KIN-MONOMER. | ||||||||||||
Gene expression databases | |||||||||||||
| Genevestigator | P0A763. | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 3.30.70.141. 1 hit. | ||||||||||||
| HAMAP | MF_00451. NDP_kinase. | ||||||||||||
| InterPro | IPR001564. Nucleoside_diP_kinase. IPR023005. Nucleoside_diP_kinase_AS. [Graphical view] | ||||||||||||
| PANTHER | PTHR11349. PTHR11349. 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... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P0A763. | ||||||||||||
Entry information
| Entry name | NDK_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P0A763 Secondary accession number(s): P24233 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
