P11964 · SODCP_PEA
- ProteinSuperoxide dismutase [Cu-Zn], chloroplastic
- GeneSODCP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids202 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
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 | 94 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 96 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 111 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 111 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: H | ||||||
Binding site | 119 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: H | ||||||
Binding site | 128 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: H | ||||||
Binding site | 131 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: D | ||||||
Binding site | 168 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
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], chloroplastic
- EC number
Gene names
Organism names
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > Hologalegina > IRL clade > Fabeae > Pisum
Accessions
- Primary accessionP11964
Subcellular Location
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 55 | |||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-48 | Chloroplast | ||||
Sequence: MASQTLVSPSPLSSHSLLRTSFSGVSVKLAPQFSTLATSNFKPLTVVA | ||||||
Chain | PRO_0000032848 | 49-202 | Superoxide dismutase [Cu-Zn], chloroplastic | |||
Sequence: AAKKAVSVLKGTSAVEGVVTLTQDDEGPTTVNVRITGLTPGLHGFHLHEYGDTTNGCISTGPHFNPNKLTHGAPEDEIRHAGDLGNIVANAEGVAEATIVDNQIPLTGPNSVVGRALVVHELQDDLGKGGHELSLSTGNAGGRLACGVVGLTPV | ||||||
Disulfide bond | 105↔194 | |||||
Sequence: CISTGPHFNPNKLTHGAPEDEIRHAGDLGNIVANAEGVAEATIVDNQIPLTGPNSVVGRALVVHELQDDLGKGGHELSLSTGNAGGRLAC |
Keywords
- PTM
Interaction
Subunit
Homotetramer.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length202
- Mass (Da)20,626
- Last updated1989-10-01 v1
- Checksum677BF4F185533A31