P77935 (PUR1_RHIEC) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 79.
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 | Rhizobium etli (strain CFN 42 / ATCC 51251) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 347834 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Rhizobium › ![]() |
Protein attributes
| Sequence length | 496 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 | '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 – 21 | 21 | By similarity | PRO_0000029261 | |||||
| Chain | 22 – 496 | 475 | Amidophosphoribosyltransferase | PRO_0000029262 | |||||
Regions | |||||||||
| Domain | 22 – 241 | 220 | Glutamine amidotransferase type-2 | ||||||
Sites | |||||||||
| Active site | 22 | 1 | Nucleophile By similarity | ||||||
| Metal binding | 371 | 1 | Magnesium By similarity | ||||||
| Metal binding | 372 | 1 | Magnesium By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 193 – 194 | 2 | RD → SH in AAB06461. Ref.1 | ||||||
| Sequence conflict | 312 | 1 | P → S in AAB06461. Ref.1 | ||||||
| Sequence conflict | 315 | 1 | L → G in AAB06461. Ref.1 | ||||||
| Sequence conflict | 327 | 1 | Y → YEY in AAB06461. Ref.1 | ||||||
| Sequence conflict | 407 | 1 | P → R in AAB06461. Ref.1 | ||||||
| Sequence conflict | 412 – 417 | 6 | IDTPDA → SIRPTP in AAB06461. Ref.1 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | Soberon M., Lopez O., Girard L., Miranda J., Morera C. Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: CE3. |
| [2] | "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in seven interacting replicons." Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I., Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A., Jimenez-Jacinto V., Collado-Vides J., Davila G. Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CFN 42 / ATCC 51251. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U65392 Genomic DNA. Translation: AAB06461.1. CP000133 Genomic DNA. Translation: ABC90231.1. |
| RefSeq | YP_468958.1. NC_007761.1. |
3D structure databases | |
| ProteinModelPortal | P77935. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 347834.RHE_CH01428. |
Protein family/group databases | |
| MEROPS | C44.001. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABC90231; ABC90231; RHE_CH01428. |
| GeneID | 3892667. |
| KEGG | ret:RHE_CH01428. |
| PATRIC | 23084261. VBIRhiEtl108884_1802. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0034. |
| HOGENOM | HOG000033688. |
| KO | K00764. |
| OMA | GIPFELG. |
| ProtClustDB | PRK09123. |
Enzyme and pathway databases | |
| BioCyc | RETL347834:GJJ0-1437-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_RHIEC | ||||||||
| Accession | Primary (citable) accession number: P77935 Secondary accession number(s): Q2KAA5 | ||||||||
| Entry history |
| ||||||||
| 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
