Q9V253 (PUR1_PYRAB) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 91.
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: Amidophosphoribosyltransferase Short name=ATase EC=2.4.2.14 Alternative name(s): Glutamine phosphoribosylpyrophosphate amidotransferase Short name=GPATase | ||||||
| Gene names |
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| Organism | Pyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 272844 [NCBI] | ||||||
| Taxonomic lineage | Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus › ![]() |
Protein attributes
| Sequence length | 447 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O. |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. Binds 1 4Fe-4S cluster per subunit By similarity. |
| Pathway | |
| Sequence similarities | In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family. Contains 1 glutamine amidotransferase type-2 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Purine biosynthesis |
| Domain | Glutamine amidotransferase |
| Ligand | 4Fe-4S Iron Iron-sulfur Magnesium Metal-binding |
| Molecular function | Glycosyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | 'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway glutamine metabolic processInferred from electronic annotation. Source: UniProtKB-KW nucleoside metabolic processInferred from electronic annotation. Source: InterPro purine nucleobase biosynthetic processInferred from electronic annotation. Source: InterPro |
| Molecular_function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW amidophosphoribosyltransferase activityInferred from electronic annotation. Source: EC metal ion 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Propeptide | 1 – 10 | 10 | Probable | PRO_0000029277 | |||||
| Chain | 11 – 447 | 437 | Amidophosphoribosyltransferase | PRO_0000029278 | |||||
Regions | |||||||||
| Domain | 11 – 224 | 214 | Glutamine amidotransferase type-2 | ||||||
Sites | |||||||||
| Active site | 11 | 1 | For GATase activity By similarity | ||||||
| Metal binding | 239 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 286 | 1 | Magnesium By similarity | ||||||
| Metal binding | 346 | 1 | Magnesium By similarity | ||||||
| Metal binding | 347 | 1 | Magnesium By similarity | ||||||
| Metal binding | 383 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 432 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 435 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi." Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P. Mol. Microbiol. 47:1495-1512(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: GE5 / Orsay. |
| [2] | "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638." Gao J., Wang J. Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: GE5 / Orsay. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ248283 Genomic DNA. Translation: CAB49145.1. HE613800 Genomic DNA. Translation: CCE69597.1. |
| PIR | B75212. |
| RefSeq | NP_125914.1. NC_000868.1. |
3D structure databases | |
| ProteinModelPortal | Q9V253. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 272844.PAB0151. |
Protein family/group databases | |
| MEROPS | C44.001. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB49145; CAB49145; PAB0151. |
| GeneID | 1495110. |
| KEGG | pab:PAB0151. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0034. |
| HOGENOM | HOG000033688. |
| KO | K00764. |
| OMA | GIPFELG. |
| ProtClustDB | PRK08341. |
Enzyme and pathway databases | |
| UniPathway | UPA00074; UER00124. |
Family and domain databases | |
| InterPro | IPR005854. Amd_phspho_trans. IPR017932. GATase_2_dom. IPR000583. GATase_dom. IPR000836. PRibTrfase_dom. [Graphical view] |
| Pfam | PF13537. GATase_7. 1 hit. PF00156. Pribosyltran. 1 hit. [Graphical view] |
| PIRSF | PIRSF000485. Amd_phspho_trans. 1 hit. |
| TIGRFAMs | TIGR01134. purF. 1 hit. |
| PROSITE | PS51278. GATASE_TYPE_2. 1 hit. PS00103. PUR_PYR_PR_TRANSFER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PUR1_PYRAB | ||||||||
| Accession | Primary (citable) accession number: Q9V253 Secondary accession number(s): G8ZG56 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
