A0A090CSU6 · A0A090CSU6_PODAN
- ProteinNADH-cytochrome b5 reductase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids309 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
NADH-dependent reductase for DPH3 and cytochrome b5. Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase, predominantly CBR1. By reducing DPH3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), mediated by the elongator complex. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes.
Catalytic activity
- 2 Fe3+-[Dph3] + NADH = 2 Fe2+-[Dph3] + NAD+ + H+This reaction proceeds in the forward direction.
Cofactor
Pathway
Protein modification; peptidyl-diphthamide biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 117 | FAD (UniProtKB | ChEBI) | |||
Binding site | 119 | FAD (UniProtKB | ChEBI) | |||
Binding site | 134 | FAD (UniProtKB | ChEBI) | |||
Binding site | 136 | FAD (UniProtKB | ChEBI) | |||
Binding site | 143 | FAD (UniProtKB | ChEBI) | |||
Binding site | 144 | FAD (UniProtKB | ChEBI) | |||
Binding site | 185 | FAD (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | mitochondrial outer membrane | |
Molecular Function | cytochrome-b5 reductase activity, acting on NAD(P)H | |
Molecular Function | transferase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNADH-cytochrome b5 reductase
- EC number
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Sordariales > Podosporaceae > Podospora > Podospora anserina
Accessions
- Primary accessionA0A090CSU6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion outer membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 32-49 | Helical | |||
Keywords
- Cellular component
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 60-168 | FAD-binding FR-type | |||
Sequence similarities
Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length309
- Mass (Da)33,747
- Last updated2014-11-26 v1
- ChecksumD054DC16F946A315
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FO904942 EMBL· GenBank· DDBJ | CDP31905.1 EMBL· GenBank· DDBJ | Genomic DNA |