The C-terminal domain of Gallate Dioxygenase, which catalyzes the oxidization and subsequent ring-opening of gallate
Gallate Dioxygenase catalyzes the oxidization and subsequent ring-opening of gallate, an intermediate in the degradation of the aromatic compound, syringate. The reaction product of gallate dioxygenase is 4-oxalomesaconate. The amino acid sequence of the N-terminal and C-terminal regions of gallate dioxygenase exhibits homology with the sequence of the PCA 4,5-dioxygenase B (catalytic) and A subunits, respectively. This model represents the C-terminal domain, which is similar to the A subunit of PCA 4,5-dioxygenase (or LigAB). The enzyme is estimated to be a homodimer according to the Escherichia coli enzyme. Since enzymes in this subfamily have fused A and B subunits, the dimer interface may resemble the tetramer interface of classical LigAB enzymes. This enzyme belongs to the class III extradiol dioxygenase family, composed of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon.
Feature 1:putative N- and C-terminal domain interface [polypeptide binding site]
Evidence:
Comment:based on similarity to other members of the family
Comment:The interface between the N- and C-terminal domains of this subfamily may be equivalent to the dimer interface of Sphingomonas paucimobilis LigAB.
Comment:The active site may be located at the interface between the N- and C-terminal domains for members of this subfamily. Most active site residues are from the N-terminal domain (similar to the B subunit of Sphingomonas paucimobilis LigAB).
Jiyao W et al.(2023). "The conserved domain database in 2023.",