Reviewed,
UniProtKB/Swiss-Prot Q57679 (NTPA_METJA)
Last modified
February 9, 2010.
Version 74.
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 EC=3.6.1.15 Alternative name(s): Nucleoside triphosphate phosphohydrolase Short name=NTPase | ||
| Gene names |
| ||
| Organism | Methanocaldococcus jannaschii (Methanococcus jannaschii) [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 2190 [NCBI] | ||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus |
Protein attributes
| Sequence length | 193 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Hydrolyzes non-standard nucleotides such as XTP and ITP to nucleotide monophosphate and pyrophosphate. Probably excludes non-standard purines from DNA precursor pool, preventing thus incorporation into DNA and avoiding chromosomal lesions. HAMAP MF_01405 |
| Catalytic activity | NTP + H2O = NDP + phosphate. Ref.2 |
| Cofactor | Magnesium or manganese. Ref.2 |
| Subunit structure | Homodimer. HAMAP MF_01405 |
| Miscellaneous | XTP is the best substrate, followed by ITP, GTP or dGTP, both of which are hydrolyzed 100-fold less efficiently than XTP, and finally ATP, CTP and TTP which are hydrolyzed the least well. HAMAP MF_01405 |
| Sequence similarities | Belongs to the HAM1 NTPase family. |
| Biophysicochemical properties | Kinetic parameters: KM=0.10 mM for XTP HAMAP MF_01405 KM=0.15 mM for ITP KM=1.11 mM for GTP Temperature dependence: Optimum temperature is 80 degrees Celsius. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Magnesium Manganese |
| 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 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 – 193 | 193 | Nucleoside-triphosphatase HAMAP MF_01405 | PRO_0000178274 | |||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 11 – 14 | 4 | |||||||||||||||||||||||||||||||||||||||
| Helix | 18 – 27 | 10 | |||||||||||||||||||||||||||||||||||||||
| Turn | 28 – 30 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 36 – 39 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 46 – 48 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 50 – 65 | 16 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 69 – 78 | 10 | |||||||||||||||||||||||||||||||||||||||
| Helix | 79 – 81 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 89 – 95 | 7 | |||||||||||||||||||||||||||||||||||||||
| Helix | 97 – 105 | 9 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 112 – 123 | 12 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 126 – 138 | 13 | |||||||||||||||||||||||||||||||||||||||
| Helix | 150 – 153 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 154 – 157 | 4 | |||||||||||||||||||||||||||||||||||||||
| Helix | 164 – 166 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 169 – 172 | 4 | |||||||||||||||||||||||||||||||||||||||
| Turn | 173 – 175 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 177 – 190 | 14 | |||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. Venter J.C.Science 273:1058-1073(1996) [PubMed: 8688087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440. |
| [2] | "Structure-based identification of a novel NTPase from Methanococcus jannaschii." Hwang K.Y., Chung J.H., Kim S.-H., Han Y.S., Cho Y. Nat. Struct. Biol. 6:691-696(1999) [PubMed: 10404228] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | L77117 Genomic DNA. Translation: AAB98211.1. | ||||||||||||||||||
| PIR | C64328. | ||||||||||||||||||
| RefSeq | NP_247195.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ModBase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| GeneID | 1451077. | ||||||||||||||||||
| GenomeReviews | Gene locus MJ0226 in contig L77117_GR. | ||||||||||||||||||
| KEGG | mja:MJ0226. | ||||||||||||||||||
| NMPDR | fig|243232.1.peg.232. | ||||||||||||||||||
| TIGR | MJ0226. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOGENOM | HBG697237. | ||||||||||||||||||
| OMA | FAYDSIF. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BRENDA | 3.6.1.15. 256362. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| HAMAP | MF_01405. Nucleoside_triphosp. Divergent sequence. [Tree] | ||||||||||||||||||
| InterPro | IPR002637. Ham1p-like. IPR020922. Nucleoside-triphosphatase. [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 | NTPA_METJA | ||||||||
| Accession | Primary (citable) accession number: Q57679 | ||||||||
| 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
| Methanococcus jannaschii Methanococcus jannaschii: entries and gene names |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


