P99164 (PUR1_STAAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 71.
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 |
| ||||
| Organism | Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 158879 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus › ![]() |
Protein attributes
| Sequence length | 494 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
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. |
| 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 | 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 | amidophosphoribosyltransferase activity Inferred 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 | By similarity | PRO_0000029265 | |||||
| Chain | 11 – 494 | 484 | Amidophosphoribosyltransferase | PRO_0000029266 | |||||
Regions | |||||||||
| Domain | 11 – 231 | 221 | Glutamine amidotransferase type-2 | ||||||
Sites | |||||||||
| Active site | 11 | 1 | For GATase activity By similarity | ||||||
| Metal binding | 356 | 1 | Magnesium By similarity | ||||||
| Metal binding | 357 | 1 | Magnesium By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. Hiramatsu K.Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: N315. |
| [2] | "Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth." Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J. J. Microbiol. Methods 60:247-257(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. Strain: N315. |
| [3] | "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315." Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F. Submitted (OCT-2007) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: N315. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000018 Genomic DNA. Translation: BAB42167.1. |
| PIR | D89876. |
| RefSeq | NP_374189.1. NC_002745.2. |
3D structure databases | |
| ProteinModelPortal | P99164. |
| SMR | P99164. Positions 11-461. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 158879.SA0922. |
2D gel databases | |
| SWISS-2DPAGE | P99164. |
Proteomic databases | |
| PRIDE | P99164. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAB42167; BAB42167; BAB42167. |
| GeneID | 1123745. |
| KEGG | sau:SA0922. |
| PATRIC | 19574032. VBIStaAur116463_0986. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0034. |
| HOGENOM | HOG000033688. |
| KO | K00764. |
| OMA | GIPFELG. |
| ProtClustDB | PRK07272. |
Enzyme and pathway databases | |
| BioCyc | SAUR158879:GJCB-974-MONOMER. |
| 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_STAAN | ||||||||
| Accession | Primary (citable) accession number: P99164 Secondary accession number(s): Q99V27 | ||||||||
| 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
