Q5HQA0 (PUR1_STAEQ) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 51.
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 epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 176279 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › 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 | 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. |
| 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 | glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW nucleoside metabolic processInferred 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 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_0000045304 | |||||
| Chain | 11 – 494 | 484 | Amidophosphoribosyltransferase | PRO_0000045305 | |||||
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
| [1] | "Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain." Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. Fraser C.M.J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35984 / RP62A. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000029 Genomic DNA. Translation: AAW54001.1. |
| RefSeq | YP_188240.1. NC_002976.3. |
3D structure databases | |
| ProteinModelPortal | Q5HQA0. |
| SMR | Q5HQA0. Positions 11-471. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q5HQA0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBSTAT00000042075; EBSTAP00000040618; EBSTAG00000042073. |
| GeneID | 3240495. |
| GenomeReviews | Gene locus SERP0655 in contig CP000029_GR. |
| KEGG | ser:SERP0655. |
| PATRIC | 19612183. VBIStaEpi130894_0635. |
| TIGR | SERP0655. |
Phylogenomic databases | |
| eggNOG | COG0034. |
| GeneTree | EBGT00050000023831. |
| HOGENOM | HBG392416. |
| OMA | VWAPGEE. |
| PhylomeDB | Q5HQA0. |
| ProtClustDB | PRK07272. |
Enzyme and pathway databases | |
| BioCyc | SEPI176279:SERP0655-MONOMER. |
Family and domain databases | |
| InterPro | IPR005854. Amd_phspho_trans. IPR000583. GATase_2. IPR017932. GATase_II. IPR000836. PRibTrfase. [Graphical view] |
| KO | K00764. |
| PANTHER | PTHR11907. Amd_phspho_trans. 1 hit. |
| Pfam | PF00310. GATase_2. 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_STAEQ | ||||||||
| Accession | Primary (citable) accession number: Q5HQA0 | ||||||||
| 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 |

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