Function and Biology

2.1 Angstrom structure of wild type Glyoxylate/Hydroxypyruvate reductase A from Escherichia Coli in complex with glyoxylate and NADP

Source organism: Escherichia coli
Biochemical function: hydroxypyruvate reductase (NADPH) activity
Biological process: cellular response to stress
Cellular component: cytosol

EC 1.1.1.81: Hydroxypyruvate reductase

Reaction catalysed:
D-glycerate + NAD(P)(+) = hydroxypyruvate + NAD(P)H
Systematic name:
D-glycerate:NADP(+) 2-oxidoreductase
Alternative Name(s):
  • Beta-hydroxypyruvate reductase
  • D-glycerate dehydrogenase
  • NADH:hydroxypyruvate reductase

EC 1.1.1.79: Glyoxylate reductase (NADP(+))

Reaction catalysed:
Glycolate + NADP(+) = glyoxylate + NADPH
Systematic name:
Glycolate:NADP(+) oxidoreductase
Alternative Name(s):
  • NADPH-glyoxylate reductase

Sequence family

Pfam Protein family (Pfam)
PF02826
Domain description: D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain
Occurring in:
  1. Glyoxylate/hydroxypyruvate reductase A
The deposited structure of PDB entry 6ovl contains 1 copy of Pfam domain PF02826 (D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain) in Glyoxylate/hydroxypyruvate reductase A. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR029753
Domain description: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domain conserved site
Occurring in:
  1. Glyoxylate/hydroxypyruvate reductase A
IPR006140
Domain description: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domain
Occurring in:
  1. Glyoxylate/hydroxypyruvate reductase A
IPR036291
Domain description: NAD(P)-binding domain superfamily
Occurring in:
  1. Glyoxylate/hydroxypyruvate reductase A
IPR023514
Domain description: Glyoxylate/hydroxypyruvate reductase A, Enterobacterales
Occurring in:
  1. Glyoxylate/hydroxypyruvate reductase A