Q9Y9D8 (PYRE_AERPE) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 62.
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 |
| ||||
| Organism | Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 272557 [NCBI] | ||||
| Taxonomic lineage | Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum |
Protein attributes
| Sequence length | 186 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyrimidine biosynthesis |
| Ligand | Magnesium |
| Molecular function | Glycosyltransferase Transferase |
| Technical term | 3D-structure 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 – 186 | 186 | Orotate phosphoribosyltransferase HAMAP MF_01208 | PRO_0000110776 | ||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||
| Region | 121 – 129 | 9 | 5-phosphoribose 1-diphosphate binding By similarity | |||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||
| Binding site | 96 | 1 | 5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity | |||||||||||||||||||||||||||||||||
| Binding site | 100 | 1 | 5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity | |||||||||||||||||||||||||||||||||
| Binding site | 102 | 1 | 5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity | |||||||||||||||||||||||||||||||||
| Binding site | 125 | 1 | Orotate By similarity | |||||||||||||||||||||||||||||||||
| Binding site | 153 | 1 | Orotate By similarity | |||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||
| Helix | 10 – 16 | 7 | ||||||||||||||||||||||||||||||||||
| Beta strand | 19 – 26 | 8 | ||||||||||||||||||||||||||||||||||
| Beta strand | 32 – 37 | 6 | ||||||||||||||||||||||||||||||||||
| Helix | 39 – 42 | 4 | ||||||||||||||||||||||||||||||||||
| Helix | 46 – 66 | 21 | ||||||||||||||||||||||||||||||||||
| Beta strand | 68 – 73 | 6 | ||||||||||||||||||||||||||||||||||
| Turn | 74 – 77 | 4 | ||||||||||||||||||||||||||||||||||
| Helix | 78 – 88 | 11 | ||||||||||||||||||||||||||||||||||
| Beta strand | 92 – 95 | 4 | ||||||||||||||||||||||||||||||||||
| Beta strand | 114 – 127 | 14 | ||||||||||||||||||||||||||||||||||
| Helix | 128 – 139 | 12 | ||||||||||||||||||||||||||||||||||
| Beta strand | 143 – 152 | 10 | ||||||||||||||||||||||||||||||||||
| Helix | 157 – 162 | 6 | ||||||||||||||||||||||||||||||||||
| Turn | 163 – 165 | 3 | ||||||||||||||||||||||||||||||||||
| Beta strand | 167 – 173 | 7 | ||||||||||||||||||||||||||||||||||
| Helix | 174 – 180 | 7 | ||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1." Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. Kikuchi H.DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | BA000002 Genomic DNA. Translation: BAA81362.2. | ||||||||||||
| PIR | B72463. | ||||||||||||
| RefSeq | NP_148558.2. NC_000854.2. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q9Y9D8. | ||||||||||||
| SMR | Q9Y9D8. Positions 9-185. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 1445367. | ||||||||||||
| GenomeReviews | Gene locus APE_2349.1 in contig BA000002_GR. | ||||||||||||
| KEGG | ape:APE_2349.1. | ||||||||||||
| NMPDR | fig|272557.1.peg.1666. | ||||||||||||
Organism-specific databases | |||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | HBG404341. | ||||||||||||
| ProtClustDB | PRK00455. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | APER272557:APE2349-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. False negative. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | PYRE_AERPE | ||||||||
| Accession | Primary (citable) accession number: Q9Y9D8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with