CATH Classification
Level | CATH Code | Description |
---|---|---|
2 | Mainly Beta | |
2.40 | Beta Barrel | |
2.40.30 | Elongation Factor Tu (Ef-tu); domain 3 | |
2.40.30.10 | Translation factors |
Domain Context
CATH Clusters
Superfamily | Translation factors |
Functional Family | NAD(P)H-flavin reductase |
Enzyme Information
1.5.1.29 |
Transferred entry: 1.5.1.38, 1.5.1.39 and 1.5.1.41.
based on mapping to UniProt P0AEN1
|
1.16.1.3 |
Aquacobalamin reductase.
based on mapping to UniProt P0AEN1
2 cob(II)alamin + NAD(+) + 2 H(2)O = 2 aquacob(III)alamin + NADH.
-!- Formerly EC 1.6.99.8.
|
1.6.8.- |
With a flavin as acceptor.
based on mapping to UniProt P0AEN1
|
1.5.1.41 |
Riboflavin reductase (NAD(P)H).
based on mapping to UniProt P0AEN1
Reduced riboflavin + NAD(P)(+) = riboflavin + NAD(P)H.
-!- Catalyzes the reduction of soluble flavins by reduced pyridine nucleotides. -!- Highest activity with riboflavin. -!- When NADH is used as acceptor, the enzyme can also utilize FMN and FAD as substrates, with lower activity than riboflavin. -!- When NADPH is used as acceptor, the enzyme has a very low activity with FMN and no activity with FAD. -!- Formerly EC 1.5.1.29 and EC 1.6.8.1.
|
1.5.1.- |
With NAD(+) or NADP(+) as acceptor.
based on mapping to UniProt P0AEN1
|
UniProtKB Entries (1)
P0AEN1 |
FRE_ECOLI
Escherichia coli K-12
NAD(P)H-flavin reductase
|
PDB Structure
PDB | 1QFJ |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli.
Biochemistry
|