J1JRX3 · J1JRX3_BARVI
- ProteinGlutathione reductase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids463 (go to sequence)
- Protein existenceInferred from homology
- 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.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
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
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Bartonellaceae > Bartonella
Accessions
- Primary accessionJ1JRX3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 43↔48 | Redox-active | ||||
Sequence: CVIRGC |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-319 | FAD/NAD(P)-binding | ||||
Sequence: FDLFVIGSGSGGVRAARLAGGLGKRVAIAEEYRVGGTCVIRGCVPKKLYVYASQYAKEFRKSVGFGWQYADPVFSWEKLVAAKNTEISRLEGLYRKGLQDNNVHIYESRASFVDDHTLELSGTGERVSAEKILIATGAKIAPNTAIKGSDMCLTSNEIFDLEKLPKSIVIVGGGYIGVEFANIFHELGVKTILLHRGDLILRNFDYDLRQLLHDAMVEKGISIIYGAAVSKIQASGNCYDVILSSGQTITTDQVMLATGRVPNTTGLKLERAGVKVNEFGAVVVDERMTTNVPHIWAVGDVTGHVQLTPVAIHD | ||||||
Domain | 341-448 | Pyridine nucleotide-disulphide oxidoreductase dimerisation | ||||
Sequence: TTAVFSQPEIGTVGLSEEDALHRYKRLEIYRTVFRPMRNVLSGSSEKMFMKLIVDGESRIVVGAHILGENAGEIAQLIGISLKGKLTKDIFDETMAVHPTIAEEIVTM |
Sequence similarities
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length463
- Mass (Da)50,841
- Last updated2012-10-03 v1
- ChecksumD0A9A08578385806
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AILZ01000030 EMBL· GenBank· DDBJ | EJF87597.1 EMBL· GenBank· DDBJ | Genomic DNA |