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UniProt functional annotation for Q46495 | ||
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| UniProt code: Q46495. |
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| Organism: | |
Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14). |
| Taxonomy: | |
Bacteria; Proteobacteria; Deltaproteobacteria; Desulfarculales; Desulfarculaceae; Desulfarculus. |
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| Function: | |
Catalyzes the one-electron reduction of superoxide anion radical to hydrogen peroxide at a nonheme ferrous iron center. Plays a fundamental role in case of oxidative stress via its superoxide detoxification activity. {ECO:0000269|PubMed:10617593}. |
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| Catalytic activity: | |
Reaction=2 H(+) + reduced [rubredoxin] + superoxide = H2O2 + oxidized [rubredoxin]; Xref=Rhea:RHEA:21324, Rhea:RHEA-COMP:10302, Rhea:RHEA- COMP:10303, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.15.1.2; Evidence={ECO:0000269|PubMed:10617593}; |
| Cofactor: | |
Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000269|PubMed:15341736}; Note=Binds 1 Fe(3+) ion per subunit. The iron ion 1 is coordinated via 4 cysteine residues. {ECO:0000269|PubMed:15341736}; |
| Cofactor: | |
Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:15341736}; Note=Binds 1 Fe(2+) ion per subunit. The iron ion 2 is coordinated via four histidines and one cysteine residue. {ECO:0000269|PubMed:15341736}; |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:10617593, ECO:0000269|PubMed:15341736}. |
| Domain: | |
Is organized in two protein domains. The N-terminal domain has a fold similar to that of desulforedoxin and contains a mononuclear Fe(3+) ion, center I. The second domain contains a different mononuclear iron center, center II, with a Fe(2+) ion. |
| Mass spectrometry: | |
Mass=14028; Mass_error=2; Method=Electrospray; Evidence={ECO:0000269|PubMed:10617593}; |
| Miscellaneous: | |
Catalysis occurs at center II. Fe(2+) ion of center II is the electron donor and is converted to the Fe(3+) form during the reaction. |
| Miscellaneous: | |
The protein sequence in PubMed:10617593 comes from protein overexpressed and processed in E.coli. |
| Similarity: | |
Belongs to the desulfoferrodoxin family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.