Q57679 (NTPA_METJA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 96.
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: Non-canonical purine NTP pyrophosphatase EC=3.6.1.19 Alternative name(s): Non-standard purine NTP pyrophosphatase Nucleoside-triphosphate diphosphatase Nucleoside-triphosphate pyrophosphatase Short name=NTPase | ||
| Gene names |
| ||
| Organism | Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP] | ||
| Taxonomic identifier | 243232 [NCBI] | ||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus › ![]() |
Protein attributes
| Sequence length | 185 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective monophosphate derivatives. Probably excludes non-canonical purines from DNA precursor pool, thus preventing their incorporation into DNA and avoiding chromosomal lesions. Ref.2 |
| Catalytic activity | A nucleoside triphosphate + H2O = a nucleotide + diphosphate. Ref.2 |
| Cofactor | Binds 1 divalent cation ion per subunit; can use either magnesium or manganese. Ref.2 |
| Subunit structure | Homodimer. Ref.2 |
| 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. XDP or GDP are not hydrolyzed to XMP or GMP, suggesting that Mj0226 is a pyrophosphate-releasing NTPase. HAMAP-Rule MF_01405 |
| Sequence similarities | Belongs to the HAM1 NTPase family. |
| Biophysicochemical properties | Kinetic parameters: KM=0.10 mM for XTP Ref.2 KM=0.15 mM for ITP KM=1.11 mM for GTP KM=1.13 mM for dGTP Temperature dependence: Optimum temperature is 80 degrees Celsius. |
| Sequence caution | The sequence AAB98211.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Nucleotide metabolism |
| Ligand | Magnesium Manganese Metal-binding Nucleotide-binding |
| Molecular function | Hydrolase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | nucleoside triphosphate catabolic process Inferred from electronic annotation. Source: InterPro purine nucleotide metabolic processInferred from electronic annotation. Source: HAMAP |
| Molecular_function | metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside-triphosphatase activityInferred from electronic annotation. Source: InterPro nucleoside-triphosphate diphosphatase activityInferred from electronic annotation. Source: HAMAP nucleotide bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 185 | 185 | Non-canonical purine NTP pyrophosphatase HAMAP-Rule MF_01405 | PRO_0000178274 | |||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||
| Region | 7 – 12 | 6 | Substrate binding By similarity | ||||||||||||||||||||||||||||||||||||||
| Region | 65 – 66 | 2 | Substrate binding By similarity | ||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||
| Metal binding | 37 | 1 | Manganese or magnesium By similarity | ||||||||||||||||||||||||||||||||||||||
| Metal binding | 65 | 1 | Manganese or magnesium By similarity | ||||||||||||||||||||||||||||||||||||||
| Binding site | 144 | 1 | Substrate By similarity | ||||||||||||||||||||||||||||||||||||||
| Binding site | 164 | 1 | Substrate By similarity | ||||||||||||||||||||||||||||||||||||||
| Binding site | 170 | 1 | Substrate By similarity | ||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 3 – 6 | 4 | |||||||||||||||||||||||||||||||||||||||
| Helix | 10 – 19 | 10 | |||||||||||||||||||||||||||||||||||||||
| Turn | 20 – 22 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 28 – 31 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 38 – 40 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 42 – 57 | 16 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 61 – 70 | 10 | |||||||||||||||||||||||||||||||||||||||
| Helix | 71 – 73 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 81 – 87 | 7 | |||||||||||||||||||||||||||||||||||||||
| Helix | 89 – 97 | 9 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 104 – 115 | 12 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 118 – 130 | 13 | |||||||||||||||||||||||||||||||||||||||
| Helix | 142 – 145 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 146 – 149 | 4 | |||||||||||||||||||||||||||||||||||||||
| Helix | 156 – 158 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 161 – 164 | 4 | |||||||||||||||||||||||||||||||||||||||
| Turn | 165 – 167 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 169 – 182 | 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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | L77117 Genomic DNA. Translation: AAB98211.1. Different initiation. | ||||||||||||||||||
| PIR | C64328. | ||||||||||||||||||
| RefSeq | NP_247195.1. NC_000909.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| STRING | 243232.MJ0226. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| EnsemblBacteria | AAB98211; AAB98211; MJ_0226. | ||||||||||||||||||
| GeneID | 1451077. | ||||||||||||||||||
| KEGG | mja:MJ_0226. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | COG0127. | ||||||||||||||||||
| KO | K02428. | ||||||||||||||||||
| ProtClustDB | PRK14821. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| HAMAP | MF_01405. Non_canon_purine_NTPase. | ||||||||||||||||||
| InterPro | IPR002637. Ham1p-like. IPR020922. Nucleoside-triphosphatase. [Graphical view] | ||||||||||||||||||
| PANTHER | PTHR11067. PTHR11067. 1 hit. | ||||||||||||||||||
| Pfam | PF01725. Ham1p_like. 1 hit. [Graphical view] | ||||||||||||||||||
| TIGRFAMs | TIGR00042. TIGR00042. 1 hit. | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| EvolutionaryTrace | Q57679. | ||||||||||||||||||
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 program | Prokaryotic Protein Annotation Program | ||||||||
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
