A0A4R2NHU5 · A0A4R2NHU5_RHOAD
- ProteinGlutathione reductase (NADPH)
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids449 (go to sequence)
- Protein existenceInferred from homology
- Annotation score1/5
Function
Cofactor
Note: Binds 1 FAD per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 51 | FAD (UniProtKB | ChEBI) | |||
Binding site | 172-179 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 196 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 263 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 303 | FAD (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | nucleotide binding | |
Molecular Function | oxidoreductase activity |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Paracoccaceae > Rhodovulum
Accessions
- Primary accessionA0A4R2NHU5
Proteomes
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Disulfide bond | 42↔47 | Redox-active | |||
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 5-319 | FAD/NAD(P)-binding | |||
Domain | 340-445 | Pyridine nucleotide-disulphide oxidoreductase dimerisation | |||
Sequence similarities
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length449
- Mass (Da)47,649
- Last updated2019-07-31 v1
- MD5 ChecksumCA098CDCBF34478AC2E47A73AC063F1F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
SLXL01000016 EMBL· GenBank· DDBJ | TCP20822.1 EMBL· GenBank· DDBJ | Genomic DNA |