CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.40 | 3-Layer(aba) Sandwich | |
3.40.50 | Rossmann fold | |
3.40.50.880 | Class I glutamine amidotransferase (GATase) domain |
Domain Context
CATH Clusters
Superfamily | 3.40.50.880 |
Functional Family |
Enzyme Information
4.2.1.130 |
D-lactate dehydratase.
based on mapping to UniProt P31658
(R)-lactate = methylglyoxal + H(2)O.
-!- The enzyme, described from the fungi Candida albicans and Schizosaccharomyces pombe, converts 2-oxopropanal to (R)-lactate in a single glutathione (GSH)-independent step. -!- The other known route for this conversion is the two-step GSH- dependent pathway catalyzed by EC 4.4.1.5 and EC 3.1.2.6.
|
3.1.2.- |
Thiolester hydrolases.
based on mapping to UniProt P31658
|
3.5.1.124 |
Protein deglycase.
based on mapping to UniProt P31658
(1) An N(omega)-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H(2)O = a [protein]-L-arginine + lactate. (2) An N(6)-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H(2)O = a [protein]-L-lysine + lactate. (3) An S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H(2)O = a [protein]-L-cysteine + lactate.
-!- The enzyme, previously thought to be a glyoxalase, acts on glycated L-arginine, L-lysine, and L-cysteine residues within proteins that have been attacked and modified by glyoxal or 2-oxopropanal. -!- The attack forms hemithioacetal in the case of cysteines and aminocarbinols in the case of arginines and lysines. -!- The enzyme repairs the amino acids, releasing glycolate or lactate (70-80% (S)-lactate and 20-30% (R)-lactate), depending on whether the attacking agent was glyoxal or 2-oxopropanal, respectively.
|
3.5.1.- |
In linear amides.
based on mapping to UniProt P31658
|
UniProtKB Entries (1)
P31658 |
HCHA_ECOLI
Escherichia coli K-12
Protein/nucleic acid deglycase 1
|
PDB Structure
PDB | 1IZZ |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain
J.Biol.Chem.
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