P32746 · PYRD_ARATH
- ProteinDihydroorotate dehydrogenase (quinone), mitochondrial
- GenePYRD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids460 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic activity
- (S)-dihydroorotate + a quinone = orotate + a quinol
Cofactor
Note: Binds 1 FMN per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
40 μM | dihydroorotate | |||||
112 μM | decylubiquinone |
pH Dependence
Optimum pH is 7.5.
Pathway
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 141-145 | FMN (UniProtKB | ChEBI) | ||||
Sequence: AGFDK | ||||||
Binding site | 145 | substrate | ||||
Sequence: K | ||||||
Binding site | 165 | FMN (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 190-194 | substrate | ||||
Sequence: NRCGF | ||||||
Binding site | 243 | FMN (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 274 | FMN (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 274-279 | substrate | ||||
Sequence: NVSSPN | ||||||
Active site | 277 | Nucleophile | ||||
Sequence: S | ||||||
Binding site | 319 | FMN (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 347 | FMN (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 348-349 | substrate | ||||
Sequence: NT | ||||||
Binding site | 371 | FMN (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 400 | FMN (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 421-422 | FMN (UniProtKB | ChEBI) | ||||
Sequence: YT |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial inner membrane | |
Cellular Component | mitochondrion | |
Cellular Component | plastid | |
Molecular Function | dihydroorotate dehydrogenase (quinone) activity | |
Molecular Function | dihydroorotate dehydrogenase activity | |
Biological Process | 'de novo' pyrimidine nucleobase biosynthetic process | |
Biological Process | 'de novo' UMP biosynthetic process | |
Biological Process | pyrimidine ribonucleotide biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDihydroorotate dehydrogenase (quinone), mitochondrial
- EC number
- Short namesDHOdehase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionP32746
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion inner membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 53-69 | Helical | ||||
Sequence: ILTGATIGLAIAGGAYV |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-32 | Mitochondrion | ||||
Sequence: MAGRAATSSAKWAREFLFRRVSSNPLGATRNC | ||||||
Chain | PRO_0000029889 | 33-460 | Dihydroorotate dehydrogenase (quinone), mitochondrial | |||
Sequence: SSVPGASSAPKVPHFSKRGRILTGATIGLAIAGGAYVSTADEATFCGWLFNATKVVNPFFALLDAEFAHKLAVSAAARGWVPREKRPDPAILGLEVWGRKFSNPIGLAAGFDKNAEATEGLLGMGFGFVEVGSVTPVPQEGNPKPRIFRLSQEGAIINRCGFNSEGIVVVAKRLGAQHGKRMLAETSATSSSPSDDVKPGGKSGPGILGVNLGKNKTSEDAAADYVQGVHNLSQYADYLVINVSSPNTAGLRMLQGRKQLKDLVKKVQAARDEMQWGDEGPPPLLVKIAPDLSRGELEDIAAVALALHLDGLIISNTTVSRPDAVSNNPVATETGGLSGKPLFALSTNMLRDMYTLTRGKIPLIGCGGVSSGEDAYKKIRAGATLVQLYTGFAYGGPALIPQIKEELVKCLERDGFKSIHEAIGADHR |
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 213-245 | Disordered | ||||
Sequence: RMLAETSATSSSPSDDVKPGGKSGPGILGVNLG | ||||||
Compositional bias | 215-229 | Polar residues | ||||
Sequence: LAETSATSSSPSDDV |
Sequence similarities
Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length460
- Mass (Da)48,547
- Last updated2002-12-06 v2
- ChecksumE8DF1C6CCEA44FFD
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 215-229 | Polar residues | ||||
Sequence: LAETSATSSSPSDDV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X62909 EMBL· GenBank· DDBJ | CAA44695.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AF454729 EMBL· GenBank· DDBJ | AAN64025.1 EMBL· GenBank· DDBJ | mRNA | ||
AB007648 EMBL· GenBank· DDBJ | BAB11185.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002688 EMBL· GenBank· DDBJ | AED93149.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK228165 EMBL· GenBank· DDBJ | BAF00121.1 EMBL· GenBank· DDBJ | mRNA | ||
BT026524 EMBL· GenBank· DDBJ | ABH04631.1 EMBL· GenBank· DDBJ | mRNA |