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Information on EC 1.1.1.193 - 5-amino-6-(5-phosphoribosylamino)uracil reductase
for references in articles please use BRENDA:EC1.1.1.193
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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
1.1.1.193 5-amino-6-(5-phosphoribosylamino)uracil reductase
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
riboflavin biosynthesis protein, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminodioxyphosphoribosylaminopyrimidine reductase
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-
-
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HTP reductase
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RibD
RibG
riboflavin biosynthesis protein
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5-amino-6-(5-phospho-D-ribitylamino)uracil + NADP+ = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NADPH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
flavin biosynthesis I (bacteria and plants), toxoflavin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
5-amino-6-(5-phospho-D-ribitylamino)uracil:NADP+ 1'-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY
69020-28-6
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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
5-amino-2,6-dioxy-4-(5'-phosphoribosylamino)pyrimidine + NADPH
5-amino-2,6-dioxy-4-(5'-phosphoribitylamino)pyrimidine + NADP+
5-amino-6-ribosylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADPH + H+
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADP+
5-amino-2,6-dioxy-4-(5'-phosphoribosylamino)pyrimidine + NADPH
5-amino-2,6-dioxy-4-(5'-phosphoribitylamino)pyrimidine + NADP+
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Substrates: intermediate in the biosynthesis of riboflavin
Products: -
Products: -
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5-amino-2,6-dioxy-4-(5'-phosphoribosylamino)pyrimidine + NADPH
5-amino-2,6-dioxy-4-(5'-phosphoribitylamino)pyrimidine + NADP+
Escherichia coli B / ATCC 11303
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Substrates: intermediate in the biosynthesis of riboflavin
Products: -
Products: -
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5-amino-6-ribosylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADPH + H+
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADP+
Substrates: -
Products: -
Products: -
?
5-amino-6-ribosylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADPH + H+
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADP+
Substrates: -
Products: -
Products: -
?
5-amino-6-ribosylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADPH + H+
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADP+
Substrates: -
Products: -
Products: -
?
5-amino-6-ribosylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADPH + H+
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADP+
Substrates: -
Products: -
Products: -
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additional information
?
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Substrates: the enzyme is involved in riboflavin biosynthesis, overview
Products: -
Products: -
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additional information
?
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Substrates: the enzyme is involved in riboflavin biosynthesis, overview
Products: -
Products: -
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additional information
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Substrates: the enzyme is involved in riboflavin biosynthesis, overview
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
5-amino-2,6-dioxy-4-(5'-phosphoribosylamino)pyrimidine + NADPH
5-amino-2,6-dioxy-4-(5'-phosphoribitylamino)pyrimidine + NADP+
5-amino-6-ribosylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADPH + H+
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADP+
5-amino-2,6-dioxy-4-(5'-phosphoribosylamino)pyrimidine + NADPH
5-amino-2,6-dioxy-4-(5'-phosphoribitylamino)pyrimidine + NADP+
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Substrates: intermediate in the biosynthesis of riboflavin
Products: -
Products: -
?
5-amino-2,6-dioxy-4-(5'-phosphoribosylamino)pyrimidine + NADPH
5-amino-2,6-dioxy-4-(5'-phosphoribitylamino)pyrimidine + NADP+
Escherichia coli B / ATCC 11303
-
Substrates: intermediate in the biosynthesis of riboflavin
Products: -
Products: -
?
5-amino-6-ribosylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADPH + H+
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADP+
Substrates: -
Products: -
Products: -
?
5-amino-6-ribosylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADPH + H+
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADP+
Substrates: -
Products: -
Products: -
?
5-amino-6-ribosylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADPH + H+
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADP+
Substrates: -
Products: -
Products: -
?
5-amino-6-ribosylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADPH + H+
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADP+
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in riboflavin biosynthesis, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in riboflavin biosynthesis, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in riboflavin biosynthesis, overview
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (16774 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. 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
40000
2 * 42038, calculated, 2 * 40000, SDS-PAGE, tagged recombinant protein
42038
2 * 42038, calculated, 2 * 40000, SDS-PAGE, tagged recombinant protein
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
dimer
2 * 42038, calculated, 2 * 40000, SDS-PAGE, tagged recombinant protein
dimer
-
2 * 42038, calculated, 2 * 40000, SDS-PAGE, tagged recombinant protein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
orthorhombic and tetragonal crystal forms at 2.2 and 2.0 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D33A
-
the mutant shows 0.1-0.6% activity compared to the wild type enzyme
D57N
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the mutant shows 0.1-0.6% activity compared to the wild type enzyme
N9A
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the mutant shows 0.1-0.6% activity compared to the wild type enzyme
R91A
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the mutation eliminates the endogenous NADPH binding and switches preference of the enzyme to NADH
S29A
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the mutant shows 0.1-0.6% activity compared to the wild type enzyme
S88E
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the mutation eliminates the endogenous NADPH binding and switches preference of the enzyme to NADH
additional information
additional information
a ribG mutant can be rescued by expression of ribB, overview
additional information
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a ribG mutant can be rescued by expression of ribB, overview
additional information
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a ribG mutant can be rescued by expression of ribB, overview
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ribD, i.e. ribG, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
gene ribG, i.e. ribD, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
gene ribG, ribG forms an expression unit with ribY, a monofunctional GTP cyclohydrolase II, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Richter, G.; Fischer, M.; Krieger, C.; Eberhardt, S.; Luttgen, H.; Gerstenschlger, I.; Bacher, A.
Biosynthesis of riboflavin: characterization of the bifunctional deaminase-reductase of Escherichia coli and Bacillus subtilis
J. Bacteriol.
179
2022-2028
1997
Bacillus subtilis (P17618), Escherichia coli (P25539)
brenda
Burrows, R.B.; Brown, G.M.
Presence in Escherichia coli of a deaminase and a reductase involved in biosynthesis of riboflavin
J. Bacteriol.
136
657-667
1978
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Grill, S.; Yamaguchi, H.; Wagner, H.; Zwahlen, L.; Kusch, U.; Mack, M.
Identification and characterization of two Streptomyces davawensis riboflavin biosynthesis gene clusters
Arch. Microbiol.
188
377-387
2007
Streptomyces davaonensis (Q2VCF5), Streptomyces davaonensis, Streptomyces davaonensis 768 (Q2VCF5)
brenda
Dawson, A.; Trumper, P.; Chrysostomou, G.; Hunter, W.N.
Structure of diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase from Acinetobacter baumannii
Acta Crystallogr. Sect. F
69
611-617
2013
Acinetobacter baumannii (D0CB74)
brenda
Chen, S.; Yen, T.; Chang, T.; Liaw, S.
Evolution of archaeal Rib7 and eubacterial RibG reductases in riboflavin biosynthesis Substrate specificity and cofactor preference
Biochem. Biophys. Res. Commun.
503
195-201
2018
Bacillus subtilis, Methanosarcina mazei
brenda
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