Q9CKF5 (NTPA_PASMU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 53.
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 | Pasteurella multocida (strain Pm70) [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 272843 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Pasteurella |
Protein attributes
| Sequence length | 202 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP/dITP to their respective monophosphate derivatives. Might exclude non-canonical purines from DNA precursor pool, thus preventing their incorporation into DNA and avoiding chromosomal lesions By similarity. HAMAP MF_01405 |
| Catalytic activity | A nucleoside triphosphate + H2O = a nucleotide + diphosphate. HAMAP MF_01405 |
| Cofactor | Binds 1 divalent metal cation ion per subunit; can use either magnesium or manganese By similarity. |
| Subunit structure | Homodimer By similarity. HAMAP MF_01405 |
| Sequence similarities | Belongs to the HAM1 NTPase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Nucleotide metabolism |
| Ligand | Magnesium Manganese Metal-binding Nucleotide-binding |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | nucleotide metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| 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: EC 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 – 202 | 202 | Non-canonical purine NTP pyrophosphatase HAMAP MF_01405 | PRO_0000178205 | |||||
Regions | |||||||||
| Region | 9 – 14 | 6 | Substrate binding By similarity | ||||||
| Region | 70 – 71 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 41 | 1 | Magnesium or manganese By similarity | ||||||
| Metal binding | 70 | 1 | Magnesium or manganese By similarity | ||||||
| Binding site | 160 | 1 | Substrate By similarity | ||||||
| Binding site | 180 | 1 | Substrate By similarity | ||||||
| Binding site | 186 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Complete genomic sequence of Pasteurella multocida Pm70." May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V. Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed: 11248100] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Pm70. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE004439 Genomic DNA. Translation: AAK03750.1. |
| RefSeq | NP_246605.1. NC_002663.1. |
3D structure databases | |
| ProteinModelPortal | Q9CKF5. |
| SMR | Q9CKF5. Positions 3-197. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1245013. |
| GenomeReviews | Gene locus PM1666 in contig AE004439_GR. |
| KEGG | pmu:PM1666. |
| NMPDR | fig|272843.1.peg.1667. |
| PATRIC | 22872627. VBIPasMul88067_1686. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG697237. |
| OMA | YSKRYDQ. |
| ProtClustDB | PRK00120. |
Enzyme and pathway databases | |
| BioCyc | PMUL272843:PM1666-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01405. Non_canon_purine_NTPase. [Tree] |
| InterPro | IPR002637. Ham1p-like. IPR020922. Nucleoside-triphosphatase. [Graphical view] |
| KO | K02428. |
| PANTHER | PTHR11067. Ham1p_like. 1 hit. |
| Pfam | PF01725. Ham1p_like. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00042. TIGR00042. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | NTPA_PASMU | ||||||||
| Accession | Primary (citable) accession number: Q9CKF5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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