Q8R536 · SPRE_MERUN

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

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site15-21NADP+ (UniProtKB | ChEBI)
Binding site43-44NADP+ (UniProtKB | ChEBI)
Binding site70-71NADP+ (UniProtKB | ChEBI)
Binding site158-159substrate
Binding site171substrate
Binding site175NADP+ (UniProtKB | ChEBI)
Binding site200substrate
Binding site202-207NADP+ (UniProtKB | ChEBI)
Binding site258substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionbenzil reductase [(S)-benzoin-forming] activity
Molecular Functionsepiapterin reductase (NADP+) activity
Biological Processtetrahydrobiopterin biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Sepiapterin reductase
  • EC number
  • Short names
    SPR
  • Alternative names
    • Benzil reductase ((S)-benzoin forming) (EC:1.1.1.320) . EC:1.1.1.320 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      SPR

Organism names

Accessions

  • Primary accession
    Q8R536

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue, chain.

TypeIDPosition(s)Description
Modified residue1N-acetylmethionine
ChainPRO_00003276421-262Sepiapterin reductase
Modified residue46Phosphoserine
Modified residue196Phosphoserine
Modified residue214Phosphoserine

Keywords

Interaction

Subunit

Homodimer.

Structure

Family & Domains

Sequence similarities

Belongs to the sepiapterin reductase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    262
  • Mass (Da)
    28,007
  • Last updated
    2002-06-01 v1
  • Checksum
    72A1A83D198CE633
MESGGLGCAVCVLTGASRGFGRALAPRLAQLLAPGSVLLLCARSDSALRRLEEELGAQQPGLRVVRAAADLGTEAGLRQVLRAVRELPKPEGLQRLLLINNAGTLGDVSKGVLNVNDPAEVNNYWALNLTSMLCLTSGTLNAFPDSPGLSKTVVNISSLCALQPFKGWGLYCTGKAARDMLCQVLAAEEPSVRVLSYAPGPLDTDMQQLARETSMDPELRNRLQRLKSEGELVDCGTSAQKLLNLLQKDTFQSGAHVDFYDN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB048357
EMBL· GenBank· DDBJ
BAB86000.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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