O94178 · SODC_COLGL
- ProteinSuperoxide dismutase [Cu-Zn]
- GeneSOD1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids154 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic activity
- 2 H+ + 2 superoxide = H2O2 + O2
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 copper ion per subunit.
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 47 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 49 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 64 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 64 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: H | ||||||
Binding site | 72 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: H | ||||||
Binding site | 81 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: H | ||||||
Binding site | 84 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: D | ||||||
Binding site | 121 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 144 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | copper ion binding | |
Molecular Function | superoxide dismutase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSuperoxide dismutase [Cu-Zn]
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Glomerellales > Glomerellaceae > Colletotrichum > Colletotrichum gloeosporioides species complex
Accessions
- Primary accessionO94178
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000164115 | 2-154 | Superoxide dismutase [Cu-Zn] | |||
Sequence: VKAVCVVRGDSKVTGSIVFEQESESAPTKITWDISGNDANAKRGMHIHTFGDNTNGCTSAGPHFNPHNKTHGAPEDSNRHVGDLGNIETDANGNSKGTVTDSHVKLIGPESVIGRTIVVHGGTDDLGKGDNEESLKTGNAGPRPACGVIGISN | ||||||
Disulfide bond | 58↔147 | |||||
Sequence: CTSAGPHFNPHNKTHGAPEDSNRHVGDLGNIETDANGNSKGTVTDSHVKLIGPESVIGRTIVVHGGTDDLGKGDNEESLKTGNAGPRPAC |
Keywords
- PTM
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 124-144 | Disordered | ||||
Sequence: TDDLGKGDNEESLKTGNAGPR |
Sequence similarities
Belongs to the Cu-Zn superoxide dismutase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length154
- Mass (Da)15,966
- Last updated2007-01-23 v3
- Checksum177F4962166699AC