Q7WEU9 (PYRE_BORBR) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 53.
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: Orotate phosphoribosyltransferase Short name=OPRT Short name=OPRTase EC=2.4.2.10 | ||||
| Gene names |
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| Organism | Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 257310 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella |
Protein attributes
| Sequence length | 224 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP) By similarity. HAMAP MF_01208 |
| Catalytic activity | Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_01208 |
| Cofactor | Magnesium By similarity. HAMAP MF_01208 |
| Pathway | Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. HAMAP MF_01208 |
| Subunit structure | Homodimer By similarity. HAMAP MF_01208 |
| Sequence similarities | Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily. |
| Sequence caution | The sequence CAE34896.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyrimidine biosynthesis |
| Ligand | Magnesium |
| Molecular function | Glycosyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | nucleoside metabolic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | orotate phosphoribosyltransferase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 224 | 224 | Orotate phosphoribosyltransferase HAMAP MF_01208 | PRO_0000110675 | |||||
Regions | |||||||||
| Region | 37 – 38 | 2 | Orotate binding By similarity | ||||||
| Region | 75 – 76 | 2 | 5-phosphoribose 1-diphosphate binding By similarity | ||||||
| Region | 130 – 138 | 9 | 5-phosphoribose 1-diphosphate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 29 | 1 | 5-phosphoribose 1-diphosphate By similarity | ||||||
| Binding site | 105 | 1 | 5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity | ||||||
| Binding site | 106 | 1 | 5-phosphoribose 1-diphosphate By similarity | ||||||
| Binding site | 109 | 1 | 5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity | ||||||
| Binding site | 111 | 1 | 5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity | ||||||
| Binding site | 134 | 1 | Orotate By similarity | ||||||
| Binding site | 162 | 1 | Orotate By similarity | ||||||
Sequences
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References
| [1] | "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. Maskell D.J.Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-588 / NCTC 13252 / RB50. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX640450 Genomic DNA. Translation: CAE34896.1. Different initiation. |
3D structure databases | |
| ProteinModelPortal | Q7WEU9. |
| SMR | Q7WEU9. Positions 8-224. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GenomeReviews | Gene locus BB4533 in contig BX470250_GR. |
| KEGG | bbr:BB4533. |
| NMPDR | fig|257310.1.peg.4514. |
| PATRIC | 21142538. VBIBorBro124907_4614. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG404341. |
| PhylomeDB | Q7WEU9. |
| ProtClustDB | PRK00455. |
Enzyme and pathway databases | |
| BioCyc | BBRO257310:BB4533-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01208. PyrE. [Tree] |
| InterPro | IPR004467. Or_phspho_trans_clade-1. IPR023031. Orotate_PribosylTferase. IPR000836. PRibTrfase. [Graphical view] |
| KO | K00762. |
| Pfam | PF00156. Pribosyltran. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00336. PyrE. 1 hit. |
| PROSITE | PS00103. PUR_PYR_PR_TRANSFER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PYRE_BORBR | ||||||||
| Accession | Primary (citable) accession number: Q7WEU9 | ||||||||
| 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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