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P22233 (SODC_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Superoxide dismutase [Cu-Zn]
EC=1.15.1.1
Gene names
Name:SODCC
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2.

Cofactor

Binds 1 copper ion per subunit By similarity.

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological_processsuperoxide metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

superoxide dismutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 152152Superoxide dismutase [Cu-Zn]
PRO_0000164157

Sites

Metal binding451Copper; catalytic By similarity
Metal binding471Copper; catalytic By similarity
Metal binding621Copper; catalytic By similarity
Metal binding621Zinc; structural By similarity
Metal binding701Zinc; structural By similarity
Metal binding791Zinc; structural By similarity
Metal binding821Zinc; structural By similarity
Metal binding1191Copper; catalytic By similarity

Amino acid modifications

Disulfide bond56 ↔ 145 By similarity

Sequences

Sequence LengthMass (Da)Tools
P22233 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 9678861CF1E6063E

FASTA15215,223
        10         20         30         40         50         60 
MGKAVVVLSS SEGVSGTVYF AQEGDGPTTV TGNVSGLKPG LHGFHVHALG DTTNGCMSTG 

        70         80         90        100        110        120 
PHYNPNGKEH GAPEDDVRHA GDLGNITVGD DGTATFTIID SQIPLSGPNS IVGRAVVVHA 

       130        140        150 
EPDDLGRGGH ELSKTTGNAG GRVACGIIGL QG

« Hide

References

[1]"Nucleotide sequence of cDNA for the cytosolic Cu/Zn-superoxide dismutase from spinach (Spinacia oleracea L.)."
Sakamoto A., Ohsuga H., Wakaura M., Mitsukawa N., Hibino T., Masumura T., Sasaki Y., Tanaka K.
Nucleic Acids Res. 18:4923-4923(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. King of Denmark.
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X53872 mRNA. Translation: CAA37866.1.
PIRDSSPCY. S12595.

3D structure databases

ProteinModelPortalP22233.
SMRP22233. Positions 1-152.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.200. 1 hit.
InterProIPR024134. SOD_Cu/Zn_/chaperones.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERPTHR10003. PTHR10003. 1 hit.
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSPR00068. CUZNDISMTASE.
SUPFAMSSF49329. SOD_Cu_Zn. 1 hit.
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSODC_SPIOL
AccessionPrimary (citable) accession number: P22233
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: April 3, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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