SODC_CANGA
ID SODC_CANGA Reviewed; 154 AA.
AC Q6FWL5;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1 {ECO:0000250|UniProtKB:P85978};
GN Name=SOD1; OrderedLocusNames=CAGL0C04741g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380949; CAG58285.1; -; Genomic_DNA.
DR RefSeq; XP_445379.1; XM_445379.1.
DR AlphaFoldDB; Q6FWL5; -.
DR SMR; Q6FWL5; -.
DR STRING; 5478.XP_445379.1; -.
DR EnsemblFungi; CAG58285; CAG58285; CAGL0C04741g.
DR GeneID; 2886862; -.
DR KEGG; cgr:CAGL0C04741g; -.
DR CGD; CAL0127282; SOD1.
DR VEuPathDB; FungiDB:CAGL0C04741g; -.
DR eggNOG; KOG0441; Eukaryota.
DR HOGENOM; CLU_056632_4_2_1; -.
DR InParanoid; Q6FWL5; -.
DR OMA; AQRGFHI; -.
DR Proteomes; UP000002428; Chromosome C.
DR GO; GO:0005829; C:cytosol; IDA:CGD.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:1902693; C:superoxide dismutase complex; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IEA:EnsemblFungi.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:CGD.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IEA:EnsemblFungi.
DR GO; GO:0031505; P:fungal-type cell wall organization; IEA:EnsemblFungi.
DR GO; GO:1901856; P:negative regulation of cellular respiration; IEA:EnsemblFungi.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:EnsemblFungi.
DR GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IEA:EnsemblFungi.
DR GO; GO:0015680; P:protein maturation by copper ion transfer; IEA:EnsemblFungi.
DR GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
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; Reference proteome; 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_0000164113"
FT REGION 125..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 15750 MW; 3F2BE605B7AE55E2 CRC64;
MVKAVAVLRG SAGVSGVVTL EQASEQDPTT ITYEIAGNDP NAERGFHIHE FGDVTNGCVS
AGPHFNPFKK THGAPQDENR HVGDLGNIKT DAQGVAKGVI TDSLVKLIGP TSVVGRSVVV
HAGTDDLGKG GNEESLKTGN AGPRPACGVI GLTN
