Q1B389 (Q1B389_MYCSS) Unreviewed, UniProtKB/TrEMBL
Last modified
January 25, 2012.
Version 45.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Amidophosphoribosyltransferase PIRNR PIRNR000485 Short name=ATase PIRNR PIRNR000485 EC=2.4.2.14 PIRNR PIRNR000485 Alternative name(s): Glutamine phosphoribosylpyrophosphate amidotransferase PIRNR PIRNR000485 | ||
| Gene names |
| ||
| Organism | Mycobacterium sp. (strain MCS) [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 164756 [NCBI] | ||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium |
Protein attributes
| Sequence length | 511 AA. |
| Sequence status | Complete. |
| 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. PIRNR PIRNR000485 |
| Cofactor | Binds 1 4Fe-4S cluster per subunit By similarity. PIRSR PIRSR000485-3 Binds 1 magnesium ion per subunit By similarity. PIRNR PIRNR000485 |
| Pathway | Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. PIRNR PIRNR000485 |
| Sequence similarities | In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family. PIRNR PIRNR000485 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Purine biosynthesis PIRNR PIRNR000485 |
| Ligand | Iron Iron-sulfur PIRSR PIRSR000485-3 Magnesium PIRNR PIRNR000485 Metal-binding |
| Molecular function | Glycosyltransferase PIRNR PIRNR000485 EMBL ABG10645.1 Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | nucleoside metabolic process Inferred 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 iron-sulfur cluster bindingInferred from electronic annotation. Source: UniProtKB-KW 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 | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Active site | 17 | 1 | For GATase activity By similarity PIRSR PIRSR000485-1 | ||||||
| Metal binding | 258 | 1 | Iron-sulfur (4Fe-4S) By similarity PIRSR PIRSR000485-3 | ||||||
| Metal binding | 404 | 1 | Iron-sulfur (4Fe-4S) By similarity PIRSR PIRSR000485-3 | ||||||
| Metal binding | 460 | 1 | Iron-sulfur (4Fe-4S) By similarity PIRSR PIRSR000485-3 | ||||||
| Metal binding | 463 | 1 | Iron-sulfur (4Fe-4S) By similarity PIRSR PIRSR000485-3 | ||||||
Sequences
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References
| [1] | "Complete sequence of chromosome of Mycobacterium sp. MCS." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. Richardson P.Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MCS. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000384 Genomic DNA. Translation: ABG10645.1. |
| RefSeq | YP_641701.1. NC_008146.1. |
3D structure databases | |
| ProteinModelPortal | Q1B389. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q1B389. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000062920; EBMYCP00000061087; EBMYCG00000062915. |
| GeneID | 4113370. |
| GenomeReviews | Gene locus Mmcs_4541 in contig CP000384_GR. |
| KEGG | mmc:Mmcs_4541. |
| PATRIC | 18119468. VBIMycSp106721_4655. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0034. |
| GeneTree | EBGT00050000016850. |
| HOGENOM | HBG392416. |
| OMA | VWAPGEE. |
| ProtClustDB | PRK07847. |
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. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | Q1B389_MYCSS | ||||||||
| Accession | Primary (citable) accession number: Q1B389 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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