Reviewed,
UniProtKB/Swiss-Prot A1KKG4 (HIS1_MYCBP)
Last modified
June 16, 2009.
Version 23.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: ATP phosphoribosyltransferase Short name=ATP-PRTase Short name=ATP-PRT EC=2.4.2.17 | ||||
| Gene names |
| ||||
| Organism | Mycobacterium bovis (strain BCG / Pasteur 1173P2) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 410289 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 284 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of hisG enzymatic activity By similarity. |
| Catalytic activity | 1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_00079 |
| Cofactor | Magnesium By similarity. |
| Enzyme regulation | Feedback inhibited by histidine By similarity. |
| Pathway | Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. HAMAP MF_00079 |
| Subunit structure | Equilibrium between an active dimeric form, an inactive hexameric form and higher aggregates. Interconversion between the various forms is largely reversible and is influenced by the natural substrates and inhibitors of the enzyme By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the ATP phosphoribosyltransferase family. Long subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Histidine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Glycosyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP phosphoribosyltransferase activityInferred from electronic annotation. Source: HAMAP magnesium ion bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 284 | 284 | ATP phosphoribosyltransferase HAMAP MF_00079 | PRO_1000004475 | |||
Sequences
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References
| [1] | "Genome plasticity of BCG and impact on vaccine efficacy." Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T. Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007) [PubMed: 17372194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AM408590 Genomic DNA. Translation: CAL72126.1. | |
| RefSeq | YP_978227.1. |
3D structure databases | |
| SMR | A1KKG4. Positions 1-284. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 4699083. |
| GenomeReviews | Gene locus BCG_2138c in contig AM408590_GR. |
| KEGG | mbb:BCG_2138c. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | A1KKG4. YLRPRDI. |
Family and domain databases | |
| HAMAP | MF_00079. [Tree] |
| InterPro | IPR001348. ATP_PRibTrfase. IPR013820. ATP_PRibTrfase_cat. IPR018198. ATP_PRibTrfase_CS. IPR013115. HisG_C. IPR015867. N-reg_PII/ATP_PRibTrfase_C. [Graphical view] |
| Gene3D | G3DSA:3.30.70.120. PII_glnB. 1 hit. |
| PANTHER | PTHR21403. ATP_phspho_trans. 1 hit. |
| Pfam | PF01634. HisG. 1 hit. PF08029. HisG_C. 1 hit. [Graphical view] |
| ProDom | PD003516. ATP_phspho_trans. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR00070. hisG. 1 hit. TIGR03455. HisG_C-term. 1 hit. |
| PROSITE | PS01316. ATP_P_PHORIBOSYLTR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HIS1_MYCBP | ||||||||
| Accession | Primary (citable) accession number: A1KKG4 | ||||||||
| 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 |

Clusters with


