ID   SODC1_MESCR             Reviewed;         152 AA.
AC   P93258;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-NOV-2008, entry version 56.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] 1;
DE            EC=1.15.1.1;
GN   Name=SODCC.1; Synonyms=SOD, SOD1;
OS   Mesembryanthemum crystallinum (Common ice plant).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   Caryophyllales; Aizoaceae; Mesembryanthemum.
OX   NCBI_TaxID=3544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Michalowski C.B., Quigley-Landreau F., Bohnert H.J.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR: Binds 1 copper ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
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DR   EMBL; U80069; AAB40394.1; -; mRNA.
DR   HSSP; P00441; 1OZU.
DR   SMR; P93258; 3-150.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
DR   InterPro; IPR001424; SOD_Cu_Zn.
DR   Gene3D; G3DSA:2.60.40.200; SOD_Cu_Zn; 1.
DR   PANTHER; PTHR10003; SOD_Cu_Zn; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   ProDom; PD000469; SOD_CU_ZN; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   2: Evidence at transcript level;
KW   Antioxidant; Copper; Cytoplasm; Metal-binding; Oxidoreductase; Zinc.
FT   CHAIN         1    152       Superoxide dismutase [Cu-Zn] 1.
FT                                /FTId=PRO_0000164144.
FT   METAL        45     45       Copper; catalytic (By similarity).
FT   METAL        47     47       Copper; catalytic (By similarity).
FT   METAL        62     62       Copper; catalytic (By similarity).
FT   METAL        62     62       Zinc; structural (By similarity).
FT   METAL        70     70       Zinc; structural (By similarity).
FT   METAL        79     79       Zinc; structural (By similarity).
FT   METAL        82     82       Zinc; structural (By similarity).
FT   METAL       119    119       Copper; catalytic (By similarity).
FT   DISULFID     56    145       By similarity.
SQ   SEQUENCE   152 AA;  15173 MW;  44771D3714ADB19C CRC64;
     MVKAVVVLSS SEGVSGTVQF TQEGSGPTTV TGNVSGLRPG LHGFHVHALG DTTNGCMSTG
     PHFNPAGKEH GAPEDETRHA GDLGNITVGD DGTATFTIID SQIPLTGPNS IVGRAVVVHA
     DPDDLGRGGH ELSKATGNAG GRVACGVIGL QG
//