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Information on EC 1.1.1.193 - 5-amino-6-(5-phosphoribosylamino)uracil reductase and Organism(s) Bacillus subtilis and UniProt Accession P17618

for references in articles please use BRENDA:EC1.1.1.193
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Bacillus subtilis
UNIPROT: P17618 not found.
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The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
riboflavin biosynthesis protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminodioxyphosphoribosylaminopyrimidine reductase
-
-
-
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HTP reductase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
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-
-
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reduction
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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 hide
69020-28-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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+
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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+
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene ribG or ribD
UniProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
domain structure, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K151A
-
inactive
K151D
-
inactive
K151E
-
inactive
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ribG, i.e. ribD, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team