UniProt ID: G1K2G0 |
FUNCTION: Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residues. {ECO:0000256|RuleBase:RU365044}. CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]- dithiol + L-methionine (R)-S-oxide; Xref=Rhea:RHEA:21260, Rhea:RHEA- COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844, ChEBI:CHEBI:58773; EC=1.8.4.14; Evidence={ECO:0000256|ARBA:ARBA00000502}; CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]; Xref=Rhea:RHEA:24164, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377, ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:45764, ChEBI:CHEBI:50058; EC=1.8.4.12; Evidence={ECO:0000256|RuleBase:RU365044}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|RuleBase:RU365044}; Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU365044}; SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family. {ECO:0000256|ARBA:ARBA00007174, ECO:0000256|RuleBase:RU365044}. |
UniProt ID: Q6NW52 |
FUNCTION: Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maintenance. {ECO:0000250|UniProtKB:Q9Y3D2}. CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]; Xref=Rhea:RHEA:24164, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377, ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:45764, ChEBI:CHEBI:50058; EC=1.8.4.12; Evidence={ECO:0000250|UniProtKB:Q9JLC3}; CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]- dithiol + L-methionine (R)-S-oxide; Xref=Rhea:RHEA:21260, Rhea:RHEA- COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844, ChEBI:CHEBI:58773; EC=1.8.4.14; Evidence={ECO:0000250|UniProtKB:Q9JLC3}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family. {ECO:0000305}. |
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