Q8R536 · SPRE_MERUN
- ProteinSepiapterin reductase
- GeneSPR
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids262 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Catalyzes the final one or two reductions in tetra-hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin. The enzyme also catalyzes the reduction of benzil to (S)-benzoin.
Catalytic activity
- L-erythro-7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH + H+
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 15-21 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GASRGFG | ||||||
Binding site | 43-44 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: RS | ||||||
Binding site | 70-71 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: DL | ||||||
Binding site | 158-159 | substrate | ||||
Sequence: SL | ||||||
Binding site | 171 | substrate | ||||
Sequence: Y | ||||||
Binding site | 175 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 200 | substrate | ||||
Sequence: G | ||||||
Binding site | 202-207 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: LDTDMQ | ||||||
Binding site | 258 | substrate | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | benzil reductase [(S)-benzoin-forming] activity | |
Molecular Function | sepiapterin reductase (NADP+) activity | |
Biological Process | tetrahydrobiopterin biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSepiapterin reductase
- EC number
- Short namesSPR
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Gerbillinae > Meriones
Accessions
- Primary accessionQ8R536
Subcellular Location
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000327642 | 1-262 | Sepiapterin reductase | |||
Sequence: MESGGLGCAVCVLTGASRGFGRALAPRLAQLLAPGSVLLLCARSDSALRRLEEELGAQQPGLRVVRAAADLGTEAGLRQVLRAVRELPKPEGLQRLLLINNAGTLGDVSKGVLNVNDPAEVNNYWALNLTSMLCLTSGTLNAFPDSPGLSKTVVNISSLCALQPFKGWGLYCTGKAARDMLCQVLAAEEPSVRVLSYAPGPLDTDMQQLARETSMDPELRNRLQRLKSEGELVDCGTSAQKLLNLLQKDTFQSGAHVDFYDN | ||||||
Modified residue | 46 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 196 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 214 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length262
- Mass (Da)28,007
- Last updated2002-06-01 v1
- Checksum72A1A83D198CE633