D5LPR3 · D5LPR3_HEVBR
- ProteinGlutathione reductase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids496 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Maintains high levels of reduced glutathione.
Catalytic activity
- 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
Cofactor
Note: Binds 1 FAD per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 79 | FAD (UniProtKB | ChEBI) | |||
Binding site | 143 | FAD (UniProtKB | ChEBI) | |||
Binding site | 207-214 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 294 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 335 | FAD (UniProtKB | ChEBI) | |||
Active site | 469 | Proton acceptor | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | glutathione-disulfide reductase (NADPH) activity | |
Molecular Function | NADP binding | |
Biological Process | cell redox homeostasis | |
Biological Process | cellular response to oxidative stress | |
Biological Process | glutathione metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlutathione reductase
- EC number
- Short namesGRase
Organism names
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Malpighiales > Euphorbiaceae > Crotonoideae > Micrandreae > Hevea
Accessions
- Primary accessionD5LPR3
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Disulfide bond | 70↔75 | Redox-active | |||
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 23-350 | FAD/NAD(P)-binding | |||
Domain | 370-479 | Pyridine nucleotide-disulphide oxidoreductase dimerisation | |||
Sequence similarities
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length496
- Mass (Da)53,684
- Last updated2010-06-15 v1
- Checksum7473360B6D935456
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GU952813 EMBL· GenBank· DDBJ | ADE06225.1 EMBL· GenBank· DDBJ | mRNA |