ID   SODC_CANAX              Reviewed;         154 AA.
AC   O59924;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1 {ECO:0000250|UniProtKB:P85978};
GN   Name=SOD1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10216241; DOI=10.1016/s0304-4165(99)00020-3;
RA   Hwang C.S., Rhie G., Kim S.T., Kim Y.R., Huh W.K., Baek Y.U., Kang S.O.;
RT   "Copper- and zinc-containing superoxide dismutase and its gene from Candida
RT   albicans.";
RL   Biochim. Biophys. Acta 1427:245-255(1999).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000250|UniProtKB:P00442}.
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         Evidence={ECO:0000250|UniProtKB:P85978};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:P00445};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P00445};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P00445};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00445};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P85978}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00445}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; AF046872; AAC12872.1; -; Genomic_DNA.
DR   AlphaFoldDB; O59924; -.
DR   SMR; O59924; -.
DR   CGD; CAL0000185037; SOD1.
DR   VEuPathDB; FungiDB:C4_02320C_A; -.
DR   VEuPathDB; FungiDB:CAWG_03562; -.
DR   OMA; AQRGFHI; -.
DR   PhylomeDB; O59924; -.
DR   PHI-base; PHI:271; -.
DR   GO; GO:0005829; C:cytosol; IDA:CGD.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IDA:CGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:CGD.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:CGD.
DR   GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR   GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
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   3: Inferred from homology;
KW   Antioxidant; Copper; Cytoplasm; Disulfide bond; Metal-binding;
KW   Oxidoreductase; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   CHAIN           2..154
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /id="PRO_0000164112"
FT   BINDING         47
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   BINDING         49
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   BINDING         64
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   BINDING         81
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   BINDING         121
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   DISULFID        58..147
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
SQ   SEQUENCE   154 AA;  16146 MW;  22EEC7F03341BE46 CRC64;
     MVKAVAVVRG DSKVQGTVHF EQESESAPTT ISWEIEGNDP NALRGFHIHQ FGDNTNGCTS
     AGPHFNPFGK QHGAPEDDER HVGDLGNIST DGNGVAKGTK QDLLIKLIGK DSILGRTIVV
     HAGTDDYGKG GFEDSKTTGH AGARPACGVI GLTQ