| IED ID | IndEnz0002015536 |
| Enzyme Type ID | protease015536 |
| Protein Name |
Nucleoside diphosphate kinase NDK NDP kinase EC 2.7.4.6 Nucleoside-2-P kinase |
| Gene Name | ndk PA3807 |
| Organism | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas aeruginosa group Pseudomonas aeruginosa Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Enzyme Sequence | MALQRTLSIIKPDAVSKNVIGEILTRFEKAGLRVVAAKMVQLSEREAGGFYAEHKERPFFKDLVSFMTSGPVVVQVLEGEDAIAKNRELMGATDPKKADAGTIRADFAVSIDENAVHGSDSEASAAREIAYFFAATEVCERIR |
| Enzyme Length | 143 |
| Uniprot Accession Number | Q59636 |
| Absorption | |
| Active Site | ACT_SITE 117; /note=Pros-phosphohistidine intermediate; /evidence=ECO:0000255|HAMAP-Rule:MF_00451 |
| Activity Regulation | |
| Binding Site | BINDING 11; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00451; BINDING 59; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00451; BINDING 87; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00451; BINDING 93; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00451; BINDING 104; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00451; BINDING 114; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00451 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00451, ECO:0000269|PubMed:8606147, ECO:0000269|PubMed:8955392}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00451, ECO:0000269|PubMed:8606147, ECO:0000269|PubMed:8955392}; |
| DNA Binding | |
| EC Number | 2.7.4.6 |
| Enzyme Function | 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. The 12-kDa membrane-associated form synthesizes GTP in preference to other nucleoside triphosphates. Important for alginate synthesis. {ECO:0000269|PubMed:8606147, ECO:0000269|PubMed:8955392}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (6); Chain (1); Mutagenesis (11); Sequence conflict (3) |
| Keywords | ATP-binding;Cytoplasm;Kinase;Magnesium;Metal-binding;Nucleotide metabolism;Nucleotide-binding;Phosphoprotein;Reference proteome;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00451, ECO:0000269|PubMed:8606147}. Note=Ndk is predominantly cytoplasmic. The 12-kDa form is predominantly membrane-associated. {ECO:0000269|PubMed:8606147}. |
| Modified Residue | |
| Post Translational Modification | PTM: An intracellular protease cleaves Ndk to a truncated 12-kDa form that undergoes autophosphorylation almost as efficiency as Ndk does. {ECO:0000269|PubMed:8606147}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 15,592 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:44640; RHEA:18113 |
| Cross Reference Brenda | 2.7.4.6; |