CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.1190 | UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase |
|
3.40.1190.20 | Ribokinase |
Domain Context
CATH Clusters
| Superfamily | 3.40.1190.20 |
| Functional Family | Bifunctional NAD(P)H-hydrate repair enzyme Nnr |
Enzyme Information
| 5.1.99.6 |
NAD(P)H-hydrate epimerase.
based on mapping to UniProt Q9X024
(1) (6R)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide = (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide. (2) (6R)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate = (6S)-6-beta-hydroxy-1,4,5,6- tetrahydronicotinamide-adenine dinucleotide phosphate.
-!- The enzyme can use either (R)-NADH-hydrate or (R)-NADPH-hydrate as a substrate. -!- Its physiological role is to convert the (R) forms to the (S) forms, which could then be restored to active dinucleotides by EC 4.2.1.93.
|
| 4.2.1.136 |
ADP-dependent NAD(P)H-hydrate dehydratase.
based on mapping to UniProt Q9X024
(1) ADP + (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide adenine- dinucleotide = AMP + phosphate + NADH. (2) ADP + (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide adenine- dinucleotide phosphate = AMP + phosphate + NADPH.
-!- Acts equally well on hydrated NADH and hydrated NADPH. -!- NAD(P)H spontaneously hydrates to both the (6S)- and (6R)- isomers. -!- The enzyme from bacteria consists of two domains, one of which acts as an NAD(P)H-hydrate epimerase that interconverts the two isomers to a 60:40 ratio (cf. EC 5.1.99.6), while the other catalyzes the dehydration. -!- Hence the enzyme can restore the complete mixture of isomers into NAD(P)H. -!- The enzyme has no activity with ATP, contrary to the enzyme from eukaryotes (cf. EC 4.2.1.93).
|
UniProtKB Entries (1)
| Q9X024 |
NNR_THEMA
Thermotoga maritima MSB8
Bifunctional NAD(P)H-hydrate repair enzyme Nnr
|
PDB Structure
| PDB | 3RRE |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Identification of unknown protein function using metabolite cocktail screening.
Structure
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