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 31-JUL-2019, entry version 95. 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) (Cryophytum OS crystallinum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; OC Pentapetalae; Caryophyllales; Aizoaceae; Mesembryanthemum; Cryophytum. 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: CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:18421; EC=1.15.1.1; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250}; CC Note=Binds 1 copper ion per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U80069; AAB40394.1; -; mRNA. DR SMR; P93258; -. DR PRIDE; P93258; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC. DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1. DR Gene3D; 2.60.40.200; -; 1. DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf. DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone. DR InterPro; IPR018152; SOD_Cu/Zn_BS. DR InterPro; IPR001424; SOD_Cu_Zn_dom. DR PANTHER; PTHR10003; PTHR10003; 1. DR Pfam; PF00080; Sod_Cu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR SUPFAM; SSF49329; SSF49329; 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; Disulfide bond; Metal-binding; KW Oxidoreductase; Zinc. FT CHAIN 1 152 Superoxide dismutase [Cu-Zn] 1. FT /FTId=PRO_0000164144. FT METAL 45 45 Copper; catalytic. {ECO:0000250}. FT METAL 47 47 Copper; catalytic. {ECO:0000250}. FT METAL 62 62 Copper; catalytic. {ECO:0000250}. FT METAL 62 62 Zinc; structural. {ECO:0000250}. FT METAL 70 70 Zinc; structural. {ECO:0000250}. FT METAL 79 79 Zinc; structural. {ECO:0000250}. FT METAL 82 82 Zinc; structural. {ECO:0000250}. FT METAL 119 119 Copper; catalytic. {ECO:0000250}. FT DISULFID 56 145 {ECO:0000250}. SQ SEQUENCE 152 AA; 15173 MW; 44771D3714ADB19C CRC64; MVKAVVVLSS SEGVSGTVQF TQEGSGPTTV TGNVSGLRPG LHGFHVHALG DTTNGCMSTG PHFNPAGKEH GAPEDETRHA GDLGNITVGD DGTATFTIID SQIPLTGPNS IVGRAVVVHA DPDDLGRGGH ELSKATGNAG GRVACGVIGL QG //