Q81FQ4 (NDK_BACCR) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 74.
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 | Bacillus cereus (strain ATCC 14579 / DSM 31) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 226900 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › ![]() |
Protein attributes
| Sequence length | 148 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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 By similarity. HAMAP-Rule MF_00451 |
| Catalytic activity | ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. HAMAP-Rule 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 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 electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 148 | 148 | Nucleoside diphosphate kinase HAMAP-Rule MF_00451 | PRO_0000136940 | |||||
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 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 91 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 122 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis." Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. Kyrpides N.C.Nature 423:87-91(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 14579 / DSM 31. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016877 Genomic DNA. Translation: AAP08495.1. |
| RefSeq | NP_831294.1. NC_004722.1. |
3D structure databases | |
| ProteinModelPortal | Q81FQ4. |
| SMR | Q81FQ4. Positions 2-137. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 226900.BC1515. |
Proteomic databases | |
| PRIDE | Q81FQ4. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAP08495; AAP08495; BC_1515. |
| GeneID | 1203864. |
| KEGG | bce:BC1515. |
| PATRIC | 32598766. VBIBacCer54481_1492. |
Phylogenomic databases | |
| eggNOG | COG0105. |
| KO | K00940. |
| OMA | FRVVAMK. |
| ProtClustDB | PRK00668. |
Enzyme and pathway databases | |
| BioCyc | BCER226900:GJEU-1515-MONOMER. |
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... |
Entry information
| Entry name | NDK_BACCR | ||||||||
| Accession | Primary (citable) accession number: Q81FQ4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
