| IED ID | IndEnz0018000381 |
| Enzyme Type ID | peroxidase000381 |
| Protein Name |
Methanobactin mb-OB3b Copper-binding compound CBC Hydrogen peroxide reductase EC 1.11.1.- Superoxide dismutase EC 1.15.1.1 |
| Gene Name | mbnA MettrDRAFT_4473 |
| Organism | Methylosinus trichosporium |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Hyphomicrobiales Methylocystaceae Methylosinus Methylosinus trichosporium |
| Enzyme Sequence | MTVKIAQKKVLPVIGRAAALCGSCYPCSCM |
| Enzyme Length | 30 |
| Uniprot Accession Number | E3YBA4 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; Evidence={ECO:0000269|PubMed:18372044}; |
| DNA Binding | |
| EC Number | 1.11.1.-; 1.15.1.1 |
| Enzyme Function | FUNCTION: Chalkophore involved in scavenging, uptake and suppression of toxicity of copper. Each apo-methanobactin (apo-mb) complexes 1 Cu(2+) or Cu(1+) ion to form Cu(1+)-mb (Cu-mb) which is then taken up by the cell. Enhances growth rate in the presence of copper and reduces growth lag upon exposition to elevated levels of copper. Cu-mb contributes to the switchover from soluble methane monooxygenase (sMMO) to the membrane-bound particulate MMO (pMMO) by inducing transcription of pMMO subunit A. It also stimulates the enzymatic activity of pMMO. In the absence of copper, binds other metal ions, like Zn(2+), Ag(1+), Au(3+), Co(2+), Cd(2+), Fe(3+), Hg(2+), Mn(2+), Ni(2+), Pb(2+) or U(6+), but not Ba(2+), Ca(2+), La(2+), Mg(2+) or Sr(2+). Uptake is an active process, which may involve TonB-dependent transporters, and as such does not involve porins. Cu-Mb can be taken up by other methanotrophic bacteria but not by E.coli. Has Cu-dependent superoxide dismutase-like activity. Shows reductant-dependent oxidase and hydrogen peroxide reductase activities. Reduces copper-levels in liver in a rat model of Wilson disease. {ECO:0000269|PubMed:15361623, ECO:0000269|PubMed:15794651, ECO:0000269|PubMed:16207923, ECO:0000269|PubMed:16332035, ECO:0000269|PubMed:16445286, ECO:0000269|PubMed:17070918, ECO:0000269|PubMed:17615240, ECO:0000269|PubMed:18372044, ECO:0000269|PubMed:20817303, ECO:0000269|PubMed:20961038, ECO:0000269|PubMed:21242075, ECO:0000269|PubMed:21254756, ECO:0000269|PubMed:21900235}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Cross-link (2); Disulfide bond (1); Metal binding (2); Peptide (1); Propeptide (1) |
| Keywords | 3D-structure;Copper;Copper transport;Cytoplasm;Direct protein sequencing;Disulfide bond;Ion transport;Metal-binding;Oxidoreductase;Peroxidase;Secreted;Transport |
| Interact With | |
| Induction | INDUCTION: By low copper concentrations. {ECO:0000269|PubMed:15794651, ECO:0000269|PubMed:20817303}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. Cytoplasm. Note=Secreted as apo-mb, uptake into the cytoplasm in complex with copper as Cu-mb. In the cytoplasm, Cu-mb is associated with the cell membrane. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 2XJH; 2XJI; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 3,143 |
| Kinetics | |
| Metal Binding | METAL 21; /note="Cu(2+)"; /evidence="ECO:0000269|PubMed:15361623, ECO:0000269|PubMed:18729522, ECO:0000269|PubMed:21254756, ECO:0007744|PDB:2XJH, ECO:0007744|PDB:2XJI"; METAL 27; /note="Cu(2+)"; /evidence="ECO:0000269|PubMed:15361623, ECO:0000269|PubMed:18729522, ECO:0000269|PubMed:21254756, ECO:0007744|PDB:2XJH, ECO:0007744|PDB:2XJI" |
| Rhea ID | RHEA:20696 |
| Cross Reference Brenda |