Reviewed,
UniProtKB/Swiss-Prot O26742 (PUR1_METTH)
Last modified
November 3, 2009.
Version 76.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names 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 | Methanobacterium thermoautotrophicum [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 187420 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter |
Protein attributes
| Sequence length | 474 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. Binds 1 4Fe-4S cluster per subunit By similarity. |
| 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 | 4Fe-4S Iron Iron-sulfur 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 | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW amidophosphoribosyltransferase activityInferred from electronic annotation. Source: EC iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW magnesium 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_0000029275 | |||||
| Chain | 11 – 474 | 464 | Amidophosphoribosyltransferase | PRO_0000029276 | |||||
Regions | |||||||||
| Domain | 11 – 234 | 224 | Glutamine amidotransferase type-2 | ||||||
Sites | |||||||||
| Active site | 11 | 1 | For GATase activity By similarity | ||||||
| Metal binding | 250 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 297 | 1 | Magnesium By similarity | ||||||
| Metal binding | 359 | 1 | Magnesium By similarity | ||||||
| Metal binding | 360 | 1 | Magnesium By similarity | ||||||
| Metal binding | 396 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 447 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 450 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
Sequences
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References
| [1] | "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics." Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. Reeve J.N.J. Bacteriol. 179:7135-7155(1997) [PubMed: 9371463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Delta H. |
Cross-references
Sequence databases | |
|---|---|
| AE000666 Genomic DNA. Translation: AAB85151.1. | |
| PIR | H69185. |
| RefSeq | NP_275788.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1AO0 based on UniProtKB P00497. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | O26742. |
Protein family/group databases | |
| MEROPS | C44.001. |
Genome annotation databases | |
| GeneID | 1470607. |
| GenomeReviews | Gene locus MTH_646 in contig AE000666_GR. |
| KEGG | mth:MTH646. |
| NMPDR | fig|187420.1.peg.643. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | O26742. |
| OMA | GIPFELG. |
Enzyme and pathway databases | |
| BioCyc | MTHE187420:MTH646-MON. |
| BRENDA | 2.4.2.14. 270. |
Family and domain databases | |
| InterPro | IPR005854. Amd_phspho_trans. IPR000583. GATase_2. IPR017932. GATase_II. IPR002375. Pr/py_Pribosyl_transf_CS. IPR000836. PRibTrfase. [Graphical view] |
| 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_METTH | ||||||||
| Accession | Primary (citable) accession number: O26742 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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