Enzyme

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EC Tree
     1. Oxidoreductases
        1.16 Oxidizing metal ions
            1.16.3 With oxygen as acceptor
ID:1.16.3.3
Description:Manganese oxidase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.16.3.3
BRENDA Enzyme Link: BRENDA 1.16.3.3
KEGG Enzyme Link: KEGG1.16.3.3
BioCyc Enzyme Link: BioCyc 1.16.3.3
ExPASy Enzyme Link: ExPASy1.16.3.3
EC2PDB Enzyme Link: EC2PDB 1.16.3.3
ExplorEnz Enzyme Link: ExplorEnz 1.16.3.3
PRIAM enzyme-specific profiles Link: PRIAM 1.16.3.3
IntEnz Enzyme Link: IntEnz 1.16.3.3
MEDLINE Enzyme Link: MEDLINE 1.16.3.3
MSA:

1.16.3.3;

Phylogenetic Tree:

1.16.3.3;

Uniprot:
M-CSA:
RHEA:52240 2 H2O + 2 Mn(2+) + O2 = 4 H(+) + 2 MnO2
RULE(radius=1) [Mn+2;H0:1].[Mn+2;H0:2].[O;H0;+0:3]=[O;H0;+0:4].[OH2;+0:5].[OH2;+0:6]>>[O;H0;+0:3]=[Mn;H0;+0:1]=[O;H0;+0:4].[O;H0;+0:5]=[Mn;H0;+0:2]=[O;H0;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
CotA, a multicopper oxidase from Bacillus pumilus WH4, exhibits manganese-oxidase activity.Su J, Bao P, Bai T, Deng L, Wu H, Liu F, He J201323577125
Elimination of manganese(II,III) oxidation in Pseudomonas putida GB-1 by a double knockout of two putative multicopper oxidase genes.Geszvain K, McCarthy JK, Tebo BM2013 Jan23124227
A multicopper oxidase is essential for manganese oxidation and laccase-like activity in Pedomicrobium sp. ACM 3067.Ridge JP, Lin M, Larsen EI, Fegan M, McEwan AG, Sly LI2007 Apr17359266
Localization of Mn(II)-oxidizing activity and the putative multicopper oxidase, MnxG, to the exosporium of the marine Bacillus sp. strain SG-1.Francis CA, Casciotti KL, Tebo BM2002 Dec12420165