P0A763 (NDK_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 66.
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 |
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| Organism | Escherichia coli (strain K12) | ||||
| 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 MF_00451 |
| Catalytic activity | ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. HAMAP MF_00451 |
| Cofactor | Magnesium By similarity. HAMAP 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: 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 identical protein bindingInferred from physical interaction Ref.6. Source: EcoCyc metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW nucleoside diphosphate kinase activityInferred from direct assay. 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 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 MF_00451 | ||||||||||||||||||||||||||||||||||
| Modified residue | 121 | 1 | Phosphoserine HAMAP 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: 1657712] [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: 9205837] [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: 9278503] [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: 16738553] [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: 1323446] [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: 7730286] [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: 7783627] [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. | ||||||||||||
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. | ||||||||||||
PTM databases | |||||||||||||
| PhosSite | P0A763. | ||||||||||||
2D gel databases | |||||||||||||
| SWISS-2DPAGE | P0A763. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | P0A763. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | EBESCT00000001479; EBESCP00000001479; EBESCG00000001230. EBESCT00000016723; EBESCP00000016014; EBESCG00000015782. | ||||||||||||
| GeneID | 945611. | ||||||||||||
| GenomeReviews | Gene locus JW2502 in contig AP009048_GR. Gene locus b2518 in contig U00096_GR. | ||||||||||||
| KEGG | ecj:JW2502. eco:b2518. | ||||||||||||
| PATRIC | 32120429. VBIEscCol129921_2617. | ||||||||||||
Organism-specific databases | |||||||||||||
| EchoBASE | EB0644. | ||||||||||||
| EcoGene | EG10650. ndk. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0105. | ||||||||||||
| GeneTree | EBGT00050000009590. | ||||||||||||
| HOGENOM | HBG445152. | ||||||||||||
| OMA | ERPFFGA. | ||||||||||||
| PhylomeDB | P0A763. | ||||||||||||
| ProtClustDB | PRK00668. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | EcoCyc:NUCLEOSIDE-DIP-KIN-MONOMER. MetaCyc:NUCLEOSIDE-DIP-KIN-MONOMER. | ||||||||||||
Gene expression databases | |||||||||||||
| Genevestigator | P0A763. | ||||||||||||
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_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 |

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