P0AG17 (PUR1_SHIFL) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 52.
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 | Shigella flexneri [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 623 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella |
Protein attributes
| Sequence length | 505 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. |
| Pathway | |
| Subunit structure | Homotetramer By similarity. |
| 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 505 | 504 | Amidophosphoribosyltransferase | PRO_0000139642 | |||||
Regions | |||||||||
| Domain | 2 – 236 | 235 | Glutamine amidotransferase type-2 | ||||||
Sites | |||||||||
| Active site | 2 | 1 | For GATase activity By similarity | ||||||
| Metal binding | 367 | 1 | Magnesium By similarity | ||||||
| Metal binding | 368 | 1 | Magnesium By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. Yu J.Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a. |
| [2] | "Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005674 Genomic DNA. Translation: AAN43901.1. AE014073 Genomic DNA. Translation: AAP17719.1. |
| RefSeq | NP_708194.1. NC_004337.2. NP_837909.1. NC_004741.1. |
3D structure databases | |
| ProteinModelPortal | P0AG17. |
| SMR | P0AG17. Positions 2-501. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000085209; EBESCP00000082031; EBESCG00000084255. EBESCT00000092682; EBESCP00000089318; EBESCG00000091726. |
| GeneID | 1025528. 1078808. |
| GenomeReviews | Gene locus SF2388 in contig AE005674_GR. Gene locus S2523 in contig AE014073_GR. |
| KEGG | sfl:SF2388. sfx:S2523. |
| PATRIC | 18706641. VBIShiFle31049_2796. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000009003. |
| OMA | SYCTACF. |
| ProtClustDB | PRK09246. |
Enzyme and pathway databases | |
| BioCyc | SFLE198214:AAN43901.1-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. 2 hits. 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_SHIFL | ||||||||
| Accession | Primary (citable) accession number: P0AG17 Secondary accession number(s): P00496 Q59425 | ||||||||
| 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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