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Information on EC 1.1.1.302 - 2,5-diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5'-phosphate reductase
for references in articles please use BRENDA:EC1.1.1.302
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.302 2,5-diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5'-phosphate reductase
IUBMB Comments
The reaction proceeds in the opposite direction. A step in riboflavin biosynthesis, NADPH and NADH function equally well as reductant. Differs from EC 1.1.1.193 [5-amino-6-(5-phosphoribosylamino)uracil reductase] since it does not catalyse the reduction of 5-amino-6-ribosylaminopyrimidine-2,4(1H,3H)-dione 5′-phosphate .
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
showSynonyms
mj0671, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate synthase
2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase
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arfC
MJ0671
2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate synthase
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2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate synthase
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2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate synthase
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2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate synthase
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2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NAD(P)+ = 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NAD(P)H + H+
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NAD(P)+ = 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NAD(P)H + H+
the reaction proceeds in the opposite direction
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2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NAD(P)+ = 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NAD(P)H + H+
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
flavin biosynthesis II (archaea), flavin biosynthesis III (fungi)
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SYSTEMATIC NAME
IUBMB Comments
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one:NAD(P)+ oxidoreductase
The reaction proceeds in the opposite direction. A step in riboflavin biosynthesis, NADPH and NADH function equally well as reductant. Differs from EC 1.1.1.193 [5-amino-6-(5-phosphoribosylamino)uracil reductase] since it does not catalyse the reduction of 5-amino-6-ribosylaminopyrimidine-2,4(1H,3H)-dione 5'-phosphate [1].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,5-diamino-6-(1-D-ribosylamino)-4(3H)-pyrimidinone 5'-phosphate + NADH + H+
2,5-diamino-6-(1-D-ribitylamino)-4(3H)-pyrimidinone 5'-phosphate + NAD+
2,5-diamino-6-(1-D-ribosylamino)-4(3H)-pyrimidinone 5'-phosphate + NADPH + H+
2,5-diamino-6-(1-D-ribitylamino)-4(3H)-pyrimidinone 5'-phosphate + NADP+
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NADPH + H+
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NADP+
2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + NADH + H+
2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate + NAD+
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Substrates: step in riboflavin biosynthesis, NADPH and NADH function equally well as reductant
Products: -
Products: -
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2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + NADPH + H+
2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate + NADP+
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Substrates: step in riboflavin biosynthesis, NADPH and NADH function equally well as reductant
Products: -
Products: -
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additional information
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Substrates: the enzyme does not catalyze the pyrimidine nucleotide-dependent reduction of 5-amino-6-ribosylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate to 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate
Products: -
Products: -
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2,5-diamino-6-(1-D-ribosylamino)-4(3H)-pyrimidinone 5'-phosphate + NADH + H+
2,5-diamino-6-(1-D-ribitylamino)-4(3H)-pyrimidinone 5'-phosphate + NAD+
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Substrates: NADPH and NADH function equally well as reductant
Products: -
Products: -
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2,5-diamino-6-(1-D-ribosylamino)-4(3H)-pyrimidinone 5'-phosphate + NADH + H+
2,5-diamino-6-(1-D-ribitylamino)-4(3H)-pyrimidinone 5'-phosphate + NAD+
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Substrates: step in riboflavin biosynthesis, NADPH and NADH function equally well as reductant
Products: -
Products: -
?
2,5-diamino-6-(1-D-ribosylamino)-4(3H)-pyrimidinone 5'-phosphate + NADPH + H+
2,5-diamino-6-(1-D-ribitylamino)-4(3H)-pyrimidinone 5'-phosphate + NADP+
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Substrates: -
Products: -
Products: -
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2,5-diamino-6-(1-D-ribosylamino)-4(3H)-pyrimidinone 5'-phosphate + NADPH + H+
2,5-diamino-6-(1-D-ribitylamino)-4(3H)-pyrimidinone 5'-phosphate + NADP+
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Substrates: NADPH and NADH function equally well as reductant
Products: -
Products: -
?
2,5-diamino-6-(1-D-ribosylamino)-4(3H)-pyrimidinone 5'-phosphate + NADPH + H+
2,5-diamino-6-(1-D-ribitylamino)-4(3H)-pyrimidinone 5'-phosphate + NADP+
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Substrates: the substrate, 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, is modeled into the putative active site. The model suggests the transfer of the pro-R hydrogen of C-4 of NADPH to C-1' of the substrate
Products: -
Products: -
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2,5-diamino-6-(1-D-ribosylamino)-4(3H)-pyrimidinone 5'-phosphate + NADPH + H+
2,5-diamino-6-(1-D-ribitylamino)-4(3H)-pyrimidinone 5'-phosphate + NADP+
-
Substrates: step in riboflavin biosynthesis, NADPH and NADH function equally well as reductant
Products: -
Products: -
?
2,5-diamino-6-(1-D-ribosylamino)-4(3H)-pyrimidinone 5'-phosphate + NADPH + H+
2,5-diamino-6-(1-D-ribitylamino)-4(3H)-pyrimidinone 5'-phosphate + NADP+
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Substrates: NADPH and NADH function equally well as reductant
Products: -
Products: -
?
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NADPH + H+
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NADP+
Substrates: biosynthesis of riboflavin
Products: -
Products: -
?
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NADPH + H+
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NADP+
Substrates: the beta anomer is the authentic substrate, and the alpha anomer can serve as substrate subsequent to spontaneous anomerisation
Products: -
Products: -
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2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NADPH + H+
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NADP+
Substrates: biosynthesis of riboflavin
Products: -
Products: -
?
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NADPH + H+
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NADP+
Substrates: the beta anomer is the authentic substrate, and the alpha anomer can serve as substrate subsequent to spontaneous anomerisation. The enzyme is an A-type reductase catalysing the transfer of deuterium from the 4(R) position of NADPH to the 1' (S) position of the substrate
Products: -
Products: -
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2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NADPH + H+
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NADP+
Substrates: biosynthesis of riboflavin
Products: -
Products: -
?
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NADPH + H+
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NADP+
Substrates: the beta anomer is the authentic substrate, and the alpha anomer can serve as substrate subsequent to spontaneous anomerisation. The enzyme is an A-type reductase catalysing the transfer of deuterium from the 4(R) position of NADPH to the 1' (S) position of the substrate
Products: -
Products: -
?
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NADPH + H+
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NADP+
Substrates: biosynthesis of riboflavin
Products: -
Products: -
?
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NADPH + H+
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NADP+
Substrates: the beta anomer is the authentic substrate, and the alpha anomer can serve as substrate subsequent to spontaneous anomerisation. The enzyme is an A-type reductase catalysing the transfer of deuterium from the 4(R) position of NADPH to the 1' (S) position of the substrate
Products: -
Products: -
?
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NADPH + H+
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NADP+
Substrates: biosynthesis of riboflavin
Products: -
Products: -
?
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NADPH + H+
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NADP+
Substrates: the beta anomer is the authentic substrate, and the alpha anomer can serve as substrate subsequent to spontaneous anomerisation. The enzyme is an A-type reductase catalysing the transfer of deuterium from the 4(R) position of NADPH to the 1' (S) position of the substrate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,5-diamino-6-(1-D-ribosylamino)-4(3H)-pyrimidinone 5'-phosphate + NADH + H+
2,5-diamino-6-(1-D-ribitylamino)-4(3H)-pyrimidinone 5'-phosphate + NAD+
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Substrates: step in riboflavin biosynthesis, NADPH and NADH function equally well as reductant
Products: -
Products: -
?
2,5-diamino-6-(1-D-ribosylamino)-4(3H)-pyrimidinone 5'-phosphate + NADPH + H+
2,5-diamino-6-(1-D-ribitylamino)-4(3H)-pyrimidinone 5'-phosphate + NADP+
-
Substrates: step in riboflavin biosynthesis, NADPH and NADH function equally well as reductant
Products: -
Products: -
?
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NADPH + H+
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NADP+
2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + NADH + H+
2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate + NAD+
-
Substrates: step in riboflavin biosynthesis, NADPH and NADH function equally well as reductant
Products: -
Products: -
?
2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + NADPH + H+
2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate + NADP+
-
Substrates: step in riboflavin biosynthesis, NADPH and NADH function equally well as reductant
Products: -
Products: -
?
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NADPH + H+
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NADP+
Substrates: biosynthesis of riboflavin
Products: -
Products: -
?
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NADPH + H+
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NADP+
Substrates: biosynthesis of riboflavin
Products: -
Products: -
?
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NADPH + H+
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NADP+
Substrates: biosynthesis of riboflavin
Products: -
Products: -
?
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NADPH + H+
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NADP+
Substrates: biosynthesis of riboflavin
Products: -
Products: -
?
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NADPH + H+
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NADP+
Substrates: biosynthesis of riboflavin
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
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the substrate, 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, is modeled into the putative active site. The model suggests the transfer of the pro-R hydrogen of C-4 of NADPH to C-1' of the substrate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.2
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
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key enzymes for xylitol production in yeasts are xylose reductase and xylitol dehydrogenase, EC 1.1.1.9, overview
physiological function
Show AA Sequence and Transmembrane Helices (3247 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homodimer
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2 * 25037, calculated mass of the full-length protein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapour diffusion method. The structure of the enzyme in complex with the cofactor nicotinamide adenine dinucleotide phosphate is determined by X-ray crystallography at a resolution of 2.5 A
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli using a synthetic gene, the synthetic open reading frame is optimized for expression in Escherichia coli. The hypothetical open reading frame MJ0671 of Methanocaldococcus jannaschii predicts a protein of 224 amino acid residues. Because MJ0671 contains numerous codons that are poorly translated in Escherichia coli, a synthetic gene is designed that is optimized for the Escherichia coli codon usage. Approximately 31% (69 of 224) of the codons are replaced, and 14 singular restriction sites are introduced. The DNA sequence is assembled from 16 synthetic oligonucleotides by a sequence of eight PCR steps. The synthetic gene is transcribed efficiently in a recombinant Escherichia coli strain, affording approximately 30% of cellular protein
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expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hollander, I.; Brown, G.M.
Biosynthesis of riboflavin: reductase and deaminase of Ashbya gossypii
Biochem. Biophys. Res. Commun.
89
759-763
1979
Eremothecium gossypii
brenda
Graupner, M.; Xu, H.; White, R.H.
The pyrimidine nucleotide reductase step in riboflavin and F(420) biosynthesis in archaea proceeds by the eukaryotic route to riboflavin
J. Bacteriol.
184
1952-1957
2002
Methanocaldococcus jannaschii, Methanosarcina thermophila
brenda
Chatwell, L.; Krojer, T.; Fidler, A.; Römisch, W.; Eisenreich, W.; Bacher, A.; Huber, R.; Fischer, M.J.
Biosynthesis of riboflavin: structure and properties of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase of Methanocaldococcus jannaschii
Mol. Biol.
359
1334-1351
2006
Methanocaldococcus jannaschii
brenda
Römisch-Margl, W.; Eisenreich, W.; Haase, I.; Bacher, A.; Fischer, M.
2,5-Diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate synthases of fungi and archaea
FEBS J.
275
4403-4414
2008
Aquifex aeolicus (O66747), Methanocaldococcus jannaschii (Q58085), Methanocaldococcus jannaschii DSM 2661 (Q58085), [Candida] glabrata (Q6FU96), [Candida] glabrata ATCC 2001 (Q6FU96)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.302)
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Release 2023.1 (January 2023)
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