Protein Information

General Information
MoonProt ID96
First appeared in release1.0
Name(s)Superoxide dismutase Mn-SOD SOD-A
UniProt IDP53647
GO termsGO:0004784 superoxide dismutase activity GO:0016491 oxidoreductase activity GO:0046872 metal ion binding GO:0006801 superoxide metabolic process GO:0019430 removal of superoxide radicals GO:0055114 oxidation-reduction process GO:0005576 extracellular region GO:0098631 cell adhesion mediator
Organisms for which functions have been demonstratedMycobacterium avium
Sequence length207 aa
FASTA sequence>sp|P53647|SODM_MYCPA Superoxide dismutase [Mn] OS=Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10) GN=sodA PE=1 SV=3 MAEYTLPDLDWDYAALEPHISGQINEIHHTKHHATYVKGVNDALAKLEEARANEDHAAIFLNEKNLAFHLGGHVNHSIWWKNLSPDGGDKPTGELAAAIDDAFGSFDKFRAQFSAAANGLQGSGWAVLGYDTVGSRLLTFQLYDQQANVPLGIIPLLQVDMWEHAFYLQYKNVKADYVKAFWNVVNWADVQKRYAAATSKAQGLIFG
Structure Information
PDB ID
Quaternary structure
Function 1
Function descriptionSuperoxide dismutase, enzyme antioxidant convert superoxide anion radicals into O2 and H2O2
References for functionMayer, B. K., and J. O. Falkinham. "Superoxide dismutase activity of Mycobacterium avium, M. intracellulare, and M. scrofulaceum." Infection and immunity 53.3 (1986): 631-635.
E.C. number1.15.1.1
Location of functional site(s)Metal binding site:28,164,160,76
Cellular location of functioncytoplasm
Comments
Function 2
Function descriptionadhesin
References for functionReddy VM, Suleman FG. Mycobacterium avium-superoxide dismutase binds to epithelial cell aldolase, glyceraldehyde-3-phosphate dehydrogenase and cyclophilin A. Microb Pathog. 2004 Feb. PMID: 14687559
E.C. numberN/A
Location of functional site(s)
Cellular location of functioncell surface
Comments