Reviewed,
UniProtKB/Swiss-Prot P52061 (RDGB_ECOLI)
Last modified
June 16, 2009.
Version 67.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Nucleoside-triphosphatase rdgB EC=3.6.1.15 Alternative name(s): Nucleoside triphosphate phosphohydrolase Short name=NTPase | ||||||
| Gene names |
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| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 197 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Hydrolyzes O6 atom-containing purine bases deoxyinosine triphosphate (dITP) and xanthosine triphosphate (XTP) as well as 2'-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) to nucleotide monophosphate and pyrophosphate. Probably excludes non-standard purines from DNA precursor pool, preventing thus incorporation into DNA and avoiding chromosomal lesions. Ref.4 |
| Catalytic activity | NTP + H2O = NDP + phosphate. Ref.3 |
| Cofactor | Divalent cations. Maximum activity is obtained with magnesium. Activity with manganese and nickel makes up 60-75% of the maximum rate. Ref.3 |
| Subunit structure | Homodimer. Ref.3 |
| Miscellaneous | Activity toward dATP, dCTP and dTTP is less than 1% of the rate of XTP hydrolysis. Activity toward dGTP and dUTP is 10-12% lower than activity toward XTP. Modified or damaged nucleotides such as 6-chloropurine deoxyribose triphosphate, 8-Br-dGTP, 5-Br-dCTP, 5-Br-dUTP, 7-deaza-dGTP, 7-methyl-GTP, N6-etheno-ATP, NAD, NADH, FAD, ADP-ribose, UPD-glucose, AppA and ApppA are not hydrolyzed. HAMAP MF_01405 |
| Sequence similarities | Belongs to the HAM1 NTPase family. |
| biophysicochemical properties | Kinetic parameters: Vmax values are similar for XTP, dITP and ITP. KM=0.33 mM for XTP HAMAP MF_01405 KM=0.36 mM for dITP KM=0.41 mM for ITP KM=16.5 µM for dHAPTP pH dependence: Optimum pH is 10-10.5. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Magnesium Manganese Nickel |
| Molecular function | Hydrolase |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Molecular function | magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion bindingInferred from electronic annotation. Source: UniProtKB-KW nickel ion bindingInferred from electronic annotation. Source: UniProtKB-KW nucleoside-triphosphatase 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 – 197 | 197 | Nucleoside-triphosphatase rdgB HAMAP MF_01405 | PRO_0000178164 | ||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 2 – 7 | 6 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 11 – 21 | 11 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 22 – 24 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 26 – 30 | 5 | ||||||||||||||||||||||||||||||||||||||||||
| Turn | 31 – 35 | 5 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 46 – 61 | 16 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 65 – 74 | 10 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 75 – 77 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 82 – 87 | 6 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 95 – 106 | 12 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 111 – 113 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 115 – 127 | 13 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 134 – 144 | 11 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 152 – 154 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 157 – 159 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 163 – 165 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 166 – 168 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 169 – 171 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 174 – 180 | 7 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 182 – 193 | 12 | ||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "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. |
| [2] | "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. |
| [3] | "Identification of the dITP- and XTP-hydrolyzing protein from Escherichia coli." Chung J.H., Park H.-Y., Lee J.H., Jang Y. J. Biochem. Mol. Biol. 35:403-408(2002) [PubMed: 12297000] [Abstract] Cited for: CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. |
| [4] | "Substrate specificity of RdgB protein, a deoxyribonucleoside triphosphate pyrophosphohydrolase." Burgis N.E., Cunningham R.P. J. Biol. Chem. 282:3531-3538(2007) [PubMed: 17090528] [Abstract] Cited for: SUBSTRATE SPECIFICITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. |
| [5] | "Putative ribosomal protein." Midwest center for structural genomics (MCSG) Submitted (JAN-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS). |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| U28377 Genomic DNA. Translation: AAA69121.1. U00096 Genomic DNA. Translation: AAC75991.1. AP009048 Genomic DNA. Translation: BAE77017.1. | |||||||||||||||||||||||||
| PIR | A65081. | ||||||||||||||||||||||||
| RefSeq | AP_003511.1. NP_417429.1. | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||
| DIP | DIP:12197N. | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| GeneID | 947429. | ||||||||||||||||||||||||
| GenomeReviews | Gene locus JW2921 in contig AP009048_GR. Gene locus b2954 in contig U00096_GR. | ||||||||||||||||||||||||
| KEGG | ecj:JW2921. eco:b2954. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| EchoBASE | EB2807. | ||||||||||||||||||||||||
| EcoGene | EG12982. rdgB. | ||||||||||||||||||||||||
| CMR | Search... | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| HOGENOM | P52061. | ||||||||||||||||||||||||
| OMA | P52061. VYTADWA. | ||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||
| BioCyc | EcoCyc:G7530-MON. MetaCyc:G7530-MON. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| HAMAP | MF_01405. [Tree] | ||||||||||||||||||||||||
| InterPro | IPR002637. Ham1p-like. [Graphical view] | ||||||||||||||||||||||||
| PANTHER | PTHR11067. Ham1p_like. 1 hit. | ||||||||||||||||||||||||
| Pfam | PF01725. Ham1p_like. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| TIGRFAMs | TIGR00042. Ham1p_like. 1 hit. | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Entry information
| Entry name | RDGB_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P52061 Secondary accession number(s): Q2M9N9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
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


