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Catalytic Site Atlas

CSA LITERATURE entry for 1uw8

E.C. nameoxalate decarboxylase
SpeciesBacillus subtilis (Bacteria)
E.C. Number (IntEnz)
CSA Homologues of 1uw8
CSA Entries With UniProtID O34714
CSA Entries With EC Number
PDBe Entry 1uw8
PDBSum Entry 1uw8
MACiE Entry M0231

Literature Report

IntroductionOxalate decarboxylase (OxdC), isolated from Bacillus subtilus, catalyses the conversion of oxalate into formate and carbon dioxide. OxdC is part of the bicupin subset of the cupin superfamily. The enzymes requires Mn(II) and dioxygen as cofactors. The enzyme contains two manganese binding sites but it is currently thought that only the N-terminal site I possesses catalytic activity and that the C-terminal site II is structural. However, the matter is the subject of ongoing debate.
MechansimMono-protonated oxalate binds to the Mn(II) ion in site I. Dioxygen coordinates to the metal to form a Mn(III)-superoxo species. The carboxylic acid of oxalate is deprotonated by Glu162 with concomitant electron transfer to Mn(III) to form the Mn(II)-bound oxalate radical anion. This intermediate decarboxylates to form the Mn(II)-bound formyl carbon-centred radical intermediate. This intermediate is then protonated by Glu162 with concomitant electron transfer from Mn(II) to form Mn(III)-bound formate. Formate and dioxygen dissociate to leave the enzyme in the resting state.

Catalytic Sites for 1uw8

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ArgA9292macie:sideChainArg92 polarises the Mn-bound carbonyl group of formate, which increases the rate of decarboxylation. It might also stabilise a negative charge supported by this oxygen during the reaction.
GluA162162macie:sideChainGlu162 removes a proton from the carboxylic acid of Mn(III)-bound oxalate leading to the formation of the Mn(II)-bound oxalate radical anion intermediate. After decarboxylation it donates the proton to the Mn(II)-bound formyl radical to produce Mn(III)-bound formate.

Literature References