D5LPR3 · D5LPR3_HEVBR

Function

function

Maintains high levels of reduced glutathione.

Catalytic activity

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Note: Binds 1 FAD per subunit.

Features

Showing features for binding site, active site.

149650100150200250300350400450
Type
IDPosition(s)Description
Binding site79FAD (UniProtKB | ChEBI)
Binding site143FAD (UniProtKB | ChEBI)
Binding site207-214NAD+ (UniProtKB | ChEBI)
Binding site294NAD+ (UniProtKB | ChEBI)
Binding site335FAD (UniProtKB | ChEBI)
Active site469Proton acceptor

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentmitochondrion
Molecular Functionflavin adenine dinucleotide binding
Molecular Functionglutathione-disulfide reductase (NADPH) activity
Molecular FunctionNADP binding
Biological Processcell redox homeostasis
Biological Processcellular response to oxidative stress
Biological Processglutathione metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glutathione reductase
  • EC number
  • Short names
    GRase

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Malpighiales > Euphorbiaceae > Crotonoideae > Micrandreae > Hevea

Accessions

  • Primary accession
    D5LPR3

Subcellular Location

PTM/Processing

Features

Showing features for disulfide bond.

TypeIDPosition(s)Description
Disulfide bond70↔75Redox-active

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain23-350FAD/NAD(P)-binding
Domain370-479Pyridine nucleotide-disulphide oxidoreductase dimerisation

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    496
  • Mass (Da)
    53,684
  • Last updated
    2010-06-15 v1
  • Checksum
    7473360B6D935456
MARKMLIDGEVNQSNEQESHYDFDLFVIGAGSGGVRASRFSANYGAKVAICELPFHPISSEVVGGVGGTCVLRGCVPKKILVYGASFGGDIEDARNYGWEINEKVEFNWKKLLQKKTDEITRLNGIYKRLLSNAGVKLLEGEGKVVGPNEVEVTQLDGTKLSYSAKHILISTGNRAQRPNIPGQELAITSDEALSLEDMPKRAVVLGGGYIAVEFASIWRGMGATVDLVFRKELPLRGFDDEMRAVVARNLEGRGINLHPRTTLTQLIKTENGIKVSTDHGEEFLADVVLFATGRAPYTKRLNLETAGVELDSTGAIKVDEYSRTNIPSIWAVGDVTNRMNLTPVALMEGTCFAKTVFGGQPCKPDYRDVPSAVFSIPPLSVVGLSEEQAIEQAKNDILVFTSTFNPMKNTISGRQEKTVMKLVVDAETDKVLGASMCGPDAPEIIQGIAVALKCGATKAQLDSTVGIHPSTAEEFVTMRSLTRRITAGSKPKTSL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GU952813
EMBL· GenBank· DDBJ
ADE06225.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp