A0A3B6VMN4 · A0A3B6VMN4_BRAPL
- ProteinMultifunctional fusion protein
- GenepyrE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids451 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic activity
- H+ + orotidine 5'-phosphate = CO2 + UMP
Cofactor
Pathway
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 17 | substrate | ||||
Sequence: D | ||||||
Binding site | 39 | substrate | ||||
Sequence: K | ||||||
Binding site | 66-75 | substrate | ||||
Sequence: DLKFHDIPNT | ||||||
Active site | 68 | Proton donor | ||||
Sequence: K | ||||||
Binding site | 125 | substrate | ||||
Sequence: T | ||||||
Binding site | 187 | substrate | ||||
Sequence: R | ||||||
Binding site | 196 | substrate | ||||
Sequence: Q | ||||||
Binding site | 216 | substrate | ||||
Sequence: G | ||||||
Binding site | 217 | substrate | ||||
Sequence: R | ||||||
Binding site | 338 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 342 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: K | ||||||
Binding site | 344 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: H | ||||||
Binding site | 364-372 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: EDLISTGGS | ||||||
Binding site | 368 | orotate (UniProtKB | ChEBI) | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | magnesium ion binding | |
Molecular Function | orotate phosphoribosyltransferase activity | |
Molecular Function | orotidine-5'-phosphate decarboxylase activity | |
Biological Process | 'de novo' pyrimidine nucleobase biosynthetic process | |
Biological Process | 'de novo' UMP biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameOrotidine 5'-phosphate decarboxylase
- EC number
- Alternative names
- Recommended nameOrotate phosphoribosyltransferase
- EC number
- Short namesOPRT ; OPRTase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Spirochaetota > Spirochaetia > Brachyspirales > Brachyspiraceae > Brachyspira
Accessions
- Primary accessionA0A3B6VMN4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-232 | Orotidine 5'-phosphate decarboxylase | ||||
Sequence: RLIVALDFNSMSEAVALIDELGDEAVFYKVGLELFLYTKGEIIEYLANKNKKVFLDLKFHDIPNTTAMASLFAAKQNVFMFNVHTSGGKKMMEKTVEEIKKLNKENLIIGVTVLTSLSENDIKNMFTSSIALKDLAVNWAKLGKEAGLDGVVCSPKEAAIIKKECGERFRTVCPGVRPKWASVDDQERIMTPKEAIENGCDYLVVGRPITRSEDRVKACRMI |
Sequence similarities
Belongs to the OMP decarboxylase family. Type 1 subfamily.
Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.
In the C-terminal section; belongs to the OMP decarboxylase family.
In the N-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length451
- Mass (Da)50,498
- Last updated2018-12-05 v1
- Checksum93F9D740F5FC5D5C
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP002873 EMBL· GenBank· DDBJ | AGA67123.1 EMBL· GenBank· DDBJ | Genomic DNA |