A0A317VG17 · A0A317VG17_ASPEC
- ProteinNADH-cytochrome b5 reductase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids305 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
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 | 110 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 112 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 127 | FAD (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 129 | FAD (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 136 | FAD (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 137 | FAD (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 178 | FAD (UniProtKB | ChEBI) | ||||
Sequence: T |
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
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionA0A317VG17
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion outer membrane ; Single-pass membrane protein
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 58-161 | FAD-binding FR-type | ||||
Sequence: GDFQHFTLKEKNDISHNVTVYRFALPRPTDILGLPIGQHISLAATIGGKEVVRSYTPISSDNEAGYFDLLVKAYPQGNISKYLTTLEVGQTMKVRGPKGAMVYT |
Sequence similarities
Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length305
- Mass (Da)33,486
- Last updated2018-10-10 v1
- ChecksumC013EECF90582E44