A0A3P6HTM8 · A0A3P6HTM8_MESCO
- ProteinDihydropyrimidine dehydrogenase [NADP(+)]
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids662 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine.
Catalytic activity
- 5,6-dihydrouracil + NADP+ = H+ + NADPH + uracil
Cofactor
Protein has several cofactor binding sites:
Note: Binds 4 [4Fe-4S] clusters. Contains approximately 16 iron atoms per subunit.
Pathway
Amino-acid biosynthesis; beta-alanine biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | dihydropyrimidine dehydrogenase (NADP+) activity | |
Molecular Function | NADP binding | |
Molecular Function | uracil binding | |
Biological Process | beta-alanine biosynthetic process | |
Biological Process | thymine catabolic process | |
Biological Process | uracil catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDihydropyrimidine dehydrogenase [NADP(+)]
- EC number
- Short namesDHPDHase ; DPD
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Spiralia > Lophotrochozoa > Platyhelminthes > Cestoda > Eucestoda > Cyclophyllidea > Mesocestoididae > Mesocestoides
Accessions
- Primary accessionA0A3P6HTM8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-301 | FAD/NAD(P)-binding | ||||
Sequence: IGCGPASISCATYLARLGYRNVHIFERDSRVGGLSTSEIPQFRLPGSAVNFEVQLLLDLGVKIFTNRAFSASEANGITLSSLRKEGYKAIFLGFGLPNAHSTSVFSGLTPDQGYLTSKDFLPEVSSASKGCQGCPKARLPDFSGKRVVVLGAGDTAFDCATSALRCGAKRVTVSFRKSFTAINPVPEEMDLAWQEKCEFFPNLAPQRVKLGSDGKICEMEFIRREQNDDGSWYSDADQVIRIKTDYVITAYGSELNEPGVLKAMEGVELAPSGFSKGLPVVDLKSMRTNQEDVWCGGDLS | ||||||
Domain | 349-653 | Dihydroorotate dehydrogenase catalytic | ||||
Sequence: SVEMCGMRFENPFGLASAPPTTSSAMIRRAFEAGWGFAVTKTFGLDKELVTNVSPRIVRGPTGGHMYGPDQSGFCNIELISEKTAAYWIQSIKELKRDFPTKMVIASIMAKFDEQDWTQLTELTVKAKPDALELNLSCPHGMGERGMGLACGQDPALVRQICKWVKRAAGPNMPVFAKLTPNVSEIVEIAKAAREGGADGVTVINTVSGFMHLDSDSTPWPSVGKEKRTTYGGLSGNLIRPMALRAVSHIANKLPGFPILATGGIDSAEAGLQFLQAGASVLQVCSAIQNQDFTIIEDMVTGLKA |
Sequence similarities
Belongs to the dihydropyrimidine dehydrogenase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusFragment
- Length662
- Mass (Da)71,327
- Last updated2019-02-13 v1
- ChecksumC2D2B157A491F885
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 662 | |||||
Sequence: G |
Keywords
- Technical term