B8D418 (B8D418_DESK1) Unreviewed, UniProtKB/TrEMBL
Last modified
January 25, 2012.
Version 21.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Amidophosphoribosyltransferase PIRNR PIRNR000485 Short name=ATase PIRNR PIRNR000485 EC=2.4.2.14 PIRNR PIRNR000485 Alternative name(s): Glutamine phosphoribosylpyrophosphate amidotransferase PIRNR PIRNR000485 | ||
| Gene names |
| ||
| Organism | Desulfurococcus kamchatkensis (strain 1221n / DSM 18924) [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 490899 [NCBI] | ||
| Taxonomic lineage | Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Desulfurococcus |
Protein attributes
| Sequence length | 456 AA. |
| Sequence status | Complete. |
| 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. PIRNR PIRNR000485 |
| Cofactor | Binds 1 4Fe-4S cluster per subunit By similarity. PIRSR PIRSR000485-3 Binds 1 magnesium ion per subunit By similarity. PIRNR PIRNR000485 |
| Pathway | Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. PIRNR PIRNR000485 |
| Sequence similarities | In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family. PIRNR PIRNR000485 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Purine biosynthesis PIRNR PIRNR000485 |
| Ligand | Iron Iron-sulfur PIRSR PIRSR000485-3 Magnesium PIRNR PIRNR000485 Metal-binding |
| Molecular function | Glycosyltransferase PIRNR PIRNR000485 EMBL ACL10849.1 Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | nucleoside metabolic process Inferred from electronic annotation. Source: InterPro purine base biosynthetic processInferred from electronic annotation. Source: InterPro purine nucleotide biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | amidophosphoribosyltransferase activity Inferred from electronic annotation. Source: EC iron-sulfur cluster bindingInferred from electronic annotation. Source: UniProtKB-KW 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 | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Metal binding | 237 | 1 | Iron-sulfur (4Fe-4S) By similarity PIRSR PIRSR000485-3 | ||||||
| Metal binding | 383 | 1 | Iron-sulfur (4Fe-4S) By similarity PIRSR PIRSR000485-3 | ||||||
| Metal binding | 432 | 1 | Iron-sulfur (4Fe-4S) By similarity PIRSR PIRSR000485-3 | ||||||
| Metal binding | 435 | 1 | Iron-sulfur (4Fe-4S) By similarity PIRSR PIRSR000485-3 | ||||||
Sequences
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References
| [1] | "Complete genome sequence of the anaerobic, protein-degrading hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis." Ravin N.V., Mardanov A.V., Beletsky A.V., Kublanov I.V., Kolganova T.V., Lebedinsky A.V., Chernyh N.A., Bonch-Osmolovskaya E.A., Skryabin K.G. J. Bacteriol. 191:2371-2379(2009) [PubMed: 19114480] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001140 Genomic DNA. Translation: ACL10849.1. |
| RefSeq | YP_002428216.1. NC_011766.1. |
3D structure databases | |
| ProteinModelPortal | B8D418. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B8D418. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 7170744. |
| GenomeReviews | Gene locus DKAM_0523 in contig CP001140_GR. |
| KEGG | dka:DKAM_0523. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG392416. |
| OMA | DSMFEDQ. |
| ProtClustDB | CLSK2805609. |
Family and domain databases | |
| InterPro | IPR005854. Amd_phspho_trans. IPR017932. GATase_II. IPR000836. PRibTrfase. [Graphical view] |
| KO | K00764. |
| PANTHER | PTHR11907. Amd_phspho_trans. 1 hit. |
| Pfam | PF00156. Pribosyltran. 1 hit. [Graphical view] |
| PIRSF | PIRSF000485. Amd_phspho_trans. 1 hit. |
| PROSITE | PS51278. GATASE_TYPE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | B8D418_DESK1 | ||||||||
| Accession | Primary (citable) accession number: B8D418 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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