Enzyme

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     1. Oxidoreductases
        1.3 Acting on the CH-CH group of donors
            1.3.1 With NAD+ or NADP+ as acceptor
ID:1.3.1.1
Description:Dihydrouracil dehydrogenase (NAD(+)).

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.3.1.1
BRENDA Enzyme Link: BRENDA 1.3.1.1
KEGG Enzyme Link: KEGG1.3.1.1
BioCyc Enzyme Link: BioCyc 1.3.1.1
ExPASy Enzyme Link: ExPASy1.3.1.1
EC2PDB Enzyme Link: EC2PDB 1.3.1.1
ExplorEnz Enzyme Link: ExplorEnz 1.3.1.1
PRIAM enzyme-specific profiles Link: PRIAM 1.3.1.1
IntEnz Enzyme Link: IntEnz 1.3.1.1
MEDLINE Enzyme Link: MEDLINE 1.3.1.1
MSA:

1.3.1.1;

Phylogenetic Tree:

1.3.1.1;

Uniprot:
M-CSA:
RHEA:28791 H(+) + NADH + thymine = 5,6-dihydrothymine + NAD(+)
RULE(radius=1) [*:1]-[n+;H0:2]1:[cH;+0:3]:[cH;+0:4]:[cH;+0:5]:[c;H0;+0:6](-[*:7]):[cH;+0:8]:1.[*:9]=[C;H0;+0:10]1-[NH;+0:11]-[C;H0;+0:12](=[*:13])-[CH;+0:14](-[*:15])-[CH2;+0:16]-[NH;+0:17]-1>>[*:1]-[N;H0;+0:2]1-[CH;+0:3]=[CH;+0:4]-[CH2;+0:5]-[C;H0;+0:6](-[*:7])=[CH;+0:8]-1.[*:9]=[c;H0;+0:10]1:[nH;+0:11]:[c;H0;+0:12](=[*:13]):[c;H0;+0:14](-[*:15]):[cH;+0:16]:[nH;+0:17]:1
Reaction
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References

TitleAuthorsDatePubMed ID
Purification and characterization of dihydropyrimidine dehydrogenase from Alcaligenes eutrophus.Schmitt U, Jahnke K, Rosenbaum K, Cook PF, Schnackerz KD1996 Aug 18806723
Escherichia coli dihydropyrimidine dehydrogenase is a novel NAD-dependent heterotetramer essential for the production of 5,6-dihydrouracil.Hidese R, Mihara H, Kurihara T, Esaki N2011 Feb21169495
Pyrimidine catabolism in Pseudomonas aeruginosa.Kim S, West TP1991 Jan 151903745
Reductive degradation of pyrimidines. III. Purification and properties of dihydrouracil dehydrogenase.CAMPBELL LL Jr1957 Aug13462991
Pyrimidine base catabolism in Pseudomonas putida biotype B.West TP2001 Oct11759049
Isolation and characterization of an Escherichia coli B mutant strain defective in uracil catabolism.West TP1998 Nov10030006

RHEA:20189 5,6-dihydrouracil + NAD(+) = H(+) + NADH + uracil
RULE(radius=1) [*:1]-[n+;H0:2]1:[cH;+0:3]:[cH;+0:4]:[cH;+0:5]:[c;H0;+0:6](-[*:7]):[cH;+0:8]:1.[*:9]=[C;H0;+0:10]1-[NH;+0:11]-[C;H0;+0:12](=[*:13])-[CH2;+0:14]-[CH2;+0:15]-[NH;+0:16]-1>>[*:1]-[N;H0;+0:2]1-[CH;+0:3]=[CH;+0:4]-[CH2;+0:5]-[C;H0;+0:6](-[*:7])=[CH;+0:8]-1.[*:9]=[c;H0;+0:10]1:[nH;+0:11]:[c;H0;+0:12](=[*:13]):[cH;+0:14]:[cH;+0:15]:[nH;+0:16]:1
Reaction
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Purification and characterization of dihydropyrimidine dehydrogenase from Alcaligenes eutrophus.Schmitt U, Jahnke K, Rosenbaum K, Cook PF, Schnackerz KD1996 Aug 18806723
Escherichia coli dihydropyrimidine dehydrogenase is a novel NAD-dependent heterotetramer essential for the production of 5,6-dihydrouracil.Hidese R, Mihara H, Kurihara T, Esaki N2011 Feb21169495
Pyrimidine catabolism in Pseudomonas aeruginosa.Kim S, West TP1991 Jan 151903745
Reductive degradation of pyrimidines. III. Purification and properties of dihydrouracil dehydrogenase.CAMPBELL LL Jr1957 Aug13462991
Pyrimidine base catabolism in Pseudomonas putida biotype B.West TP2001 Oct11759049
Isolation and characterization of an Escherichia coli B mutant strain defective in uracil catabolism.West TP1998 Nov10030006