Q58085 · RIB7_METJA
- Protein2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase
- GenearfC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids224 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes an early step in riboflavin biosynthesis, the NAD(P)H-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate. The beta anomer is the authentic substrate, and the alpha anomer can serve as substrate subsequent to spontaneous anomerization. NADPH and NADH function equally well as the reductants. Does not catalyze the reduction of 5-amino-6-(5-phospho-D-ribosylamino)uracil to 5-amino-6-(5-phospho-D-ribitylamino)uracil.
Miscellaneous
The protein sequence in PubMed:16730025 comes from protein expressed and processed in E.coli.
Using chirally deuterated NADPH, the enzyme was shown to be A-type reductase catalyzing the transfer of deuterium from the 4(R) position of NADPH to the 1' (S) position of the substrate.
Catalytic activity
- 2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-phosphate + NADP+ = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + NADPH + H+
Pathway
Cofactor biosynthesis; riboflavin biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 16 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 57 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 61 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 83-86 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SKLR | ||||||
Binding site | 134 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 156-159 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GGTL |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | NAD binding | |
Molecular Function | NADP binding | |
Molecular Function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor | |
Molecular Function | protein dimerization activity | |
Biological Process | riboflavin biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase
- EC number
- Short namesDAROPP reductase; DARP reductase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Methanomada group > Methanococci > Methanococcales > Methanocaldococcaceae > Methanocaldococcus
Accessions
- Primary accessionQ58085
Proteomes
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000135944 | 2-224 | 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase | |||
Sequence: VMVMEKKPYIISNVGMTLDGKLATINNDSRISCEEDLIRVHKIRANVDGIMVGIGTVLKDDPRLTVHKIKSDRNPVRIVVDSKLRVPLNARVLNKDAKTIIATTEDTNEEKEKKIKILEDMGVEVVKCGRGKVDLKKLMDILYDKGIKSILLEGGGTLNWGMFKEGLVDEVSVYIAPKIFGGKEAPTYVDGEGFKTVDECVKLELKNFYRLGEGIVLEFKVKK |
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length224
- Mass (Da)25,037
- Last updated1996-11-01 v1
- Checksum4D8C15CE291E89D8
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L77117 EMBL· GenBank· DDBJ | AAB98665.1 EMBL· GenBank· DDBJ | Genomic DNA |