CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.360 | Dihydrodipicolinate Reductase; domain 2 |
|
3.30.360.10 | Dihydrodipicolinate Reductase; domain 2 |
Domain Context
CATH Clusters
| Superfamily | Dihydrodipicolinate Reductase; domain 2 |
| Functional Family |
Enzyme Information
| 1.1.1.335 |
UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase.
based on mapping to UniProt G3XD23
UDP-N-acetyl-2-amino-2-deoxy-alpha-D-glucuronate + NAD(+) = UDP-2- acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + NADH.
-!- This enzyme participates in the biosynthetic pathway for UDP-alpha-D- ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronic acid), an important precursor of B-band lipopolysaccharide. -!- The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the the enzyme catalyzing the next step the pathway (EC 2.6.1.98). -!- The enzyme also possesses an EC 1.1.99.2 activity, and utilizes the 2-oxoglutarate produced by EC 2.6.1.98 to regenerate the tightly bound NAD(+). -!- The enzymes from Bordetella pertussis and Chromobacterium violaceum do not bind NAD(+) as tightly and do not require 2-oxoglutarate to function.
|
UniProtKB Entries (1)
| G3XD23 |
WBPB_PSEAE
Pseudomonas aeruginosa PAO1
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate oxidase
|
PDB Structure
| PDB | 3OA2 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural and Functional Studies of WlbA: A Dehydrogenase Involved in the Biosynthesis of 2,3-Diacetamido-2,3-dideoxy-d-mannuronic Acid .
Biochemistry
|
