Q63G24 (Q63G24_BACCZ) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 56.
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: Orotate phosphoribosyltransferase 1 HAMAP MF_01208 Short name=OPRT 1 HAMAP MF_01208 Short name=OPRTase 1 HAMAP MF_01208 EC=2.4.2.10 HAMAP MF_01208 | ||||||
| Gene names |
| ||||||
| Organism | Bacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP] EMBL AAU19709.1 | ||||||
| Taxonomic identifier | 288681 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 180 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 SAAS SAAS004467 |
| Catalytic activity | Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_01208 SAAS SAAS023031 |
| 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 SAAS SAAS023031 |
| Subunit structure | Homodimer By similarity. HAMAP MF_01208 SAAS SAAS004467 |
| Sequence similarities | Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily. HAMAP MF_01208 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyrimidine biosynthesis SAAS SAAS023031 HAMAP MF_01208 |
| Ligand | Magnesium HAMAP MF_01208 |
| Molecular function | Glycosyltransferase HAMAP MF_01208 SAAS SAAS023031 EMBL AAU19709.1 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: HAMAP |
| Molecular function | magnesium ion binding Inferred from electronic annotation. Source: HAMAP orotate phosphoribosyltransferase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Region | 114 – 122 | 9 | 5-phosphoribose 1-diphosphate binding By similarity HAMAP MF_01208 | ||||||
Sites | |||||||||
| Binding site | 23 | 1 | 5-phosphoribose 1-diphosphate By similarity HAMAP MF_01208 | ||||||
| Binding site | 88 | 1 | 5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity HAMAP MF_01208 | ||||||
| Binding site | 89 | 1 | 5-phosphoribose 1-diphosphate By similarity HAMAP MF_01208 | ||||||
| Binding site | 92 | 1 | 5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity HAMAP MF_01208 | ||||||
| Binding site | 118 | 1 | Orotate By similarity HAMAP MF_01208 | ||||||
Sequences
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References
| [1] | "Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. Gilna P.J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000001 Genomic DNA. Translation: AAU19709.1. |
| RefSeq | YP_082138.1. NC_006274.1. |
3D structure databases | |
| ProteinModelPortal | Q63G24. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q63G24. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000042946; EBBACP00000041847; EBBACG00000042937. |
| GeneID | 3022622. |
| GenomeReviews | Gene locus BCE33L0532 in contig CP000001_GR. |
| KEGG | bcz:BCZK0532. |
| PATRIC | 18884402. VBIBacCer95304_0564. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0461. |
| GeneTree | EBGT00050000002725. |
| HOGENOM | HBG404341. |
| OMA | QTCLVIN. |
| PhylomeDB | Q63G24. |
| ProtClustDB | CLSK925627. |
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. |
| ProtoNet | Search... |
Entry information
| Entry name | Q63G24_BACCZ | ||||||||
| Accession | Primary (citable) accession number: Q63G24 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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