Function and Biology

CRYSTAL STRUCTURE OF THE D248A mutant of 2-PYRONE-4,6-DICARBOXYLIC ACID HYDROLASE FROM SPHINGOMONAS PAUCIMOBILIS complexed with substrate at pH 6.5

Source organism: Sphingomonas paucimobilis
Biochemical function: 2-pyrone-4,6-dicarboxylate lactonase activity
Biological process: lignin catabolic process
Cellular component: not assigned

EC 3.1.1.57: 2-pyrone-4,6-dicarboxylate lactonase

Reaction catalysed:
2-oxo-2H-pyran-4,6-dicarboxylate + H(2)O = (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate
Systematic name:
2-oxo-2H-pyran-4,6-dicarboxylate lactonohydrolase
Alternative Name(s):
  • 2-pyrone-4,6-dicarboxylate hydrolase
  • 2-pyrone-4,6-dicarboxylate lactonohydrolase

Sequence family

Pfam Protein family (Pfam)
PF04909
Domain description: Amidohydrolase
Occurring in:
  1. 2-pyrone-4,6-dicarboxylate hydrolase
The deposited structure of PDB entry 4di9 contains 1 copy of Pfam domain PF04909 (Amidohydrolase) in 2-pyrone-4,6-dicarboxylate hydrolase. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR006680
Domain description: Amidohydrolase-related
Occurring in:
  1. 2-pyrone-4,6-dicarboxylate hydrolase
IPR032466
Domain description: Metal-dependent hydrolase
Occurring in:
  1. 2-pyrone-4,6-dicarboxylate hydrolase

Structure domain

CATH CATH domain
3.20.20.140
Class: Alpha Beta
Architecture: Alpha-Beta Barrel
Topology: TIM Barrel
Homology: Metal-dependent hydrolases
Occurring in:
  1. 2-pyrone-4,6-dicarboxylate hydrolase
The deposited structure of PDB entry 4di9 contains 1 copy of CATH domain 3.20.20.140 (TIM Barrel) in 2-pyrone-4,6-dicarboxylate hydrolase. Showing 1 copy in chain A.