Q9PMS6 (NTPA_CAMJE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 65.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·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 | Campylobacter jejuni | ||
| Taxonomic identifier | 197 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 200 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/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 Reference 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 protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| dcd | Q9PN07 | 3 | EBI-1271444,EBI-1271615 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 200 | 200 | Non-canonical purine NTP pyrophosphatase HAMAP MF_01405 | PRO_0000178145 | |||||
Regions | |||||||||
| Region | 7 – 12 | 6 | Substrate binding By similarity | ||||||
| Region | 73 – 74 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 38 | 1 | Magnesium or manganese By similarity | ||||||
| Metal binding | 73 | 1 | Magnesium or manganese By similarity | ||||||
| Binding site | 157 | 1 | Substrate By similarity | ||||||
| Binding site | 177 | 1 | Substrate By similarity | ||||||
| Binding site | 183 | 1 | Substrate By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 120 | 1 | Y → H in AAD10059. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning of a multidrug-efflux transporter homolog from Campylobacter jejuni." Gilbert M., Michniewicz J., Wakarchuk W.W. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: OH4384 / Serotype O:19. |
| [2] | "The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. Barrell B.G.Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF113952 Genomic DNA. Translation: AAD10059.1. AL111168 Genomic DNA. Translation: CAL35486.1. |
| PIR | C81282. |
| RefSeq | YP_002344762.1. NC_002163.1. |
3D structure databases | |
| ProteinModelPortal | Q9PMS6. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9PMS6. 41 interactions. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 905667. |
| GenomeReviews | Gene locus Cj1374c in contig AL111168_GR. |
| KEGG | cje:Cj1374c. |
| PATRIC | 20059713. VBICamJej33762_1355. |
Phylogenomic databases | |
| HOGENOM | HBG697237. |
| OMA | GVYTADW. |
| ProtClustDB | PRK00120. |
Enzyme and pathway databases | |
| BioCyc | CJEJ192222:CJ1374C-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_CAMJE | ||||||||
| Accession | Primary (citable) accession number: Q9PMS6 Secondary accession number(s): Q0P8N5, Q9ZF65 | ||||||||
| 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 |

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