ID   SODC_ZINOF              Reviewed;         152 AA.
AC   C0HK70;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000303|PubMed:28185046};
DE            EC=1.15.1.1 {ECO:0000269|PubMed:28185046};
OS   Zingiber officinale (Ginger) (Amomum zingiber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Zingiberaceae;
OC   Zingiber.
OX   NCBI_TaxID=94328 {ECO:0000303|PubMed:28185046};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-152, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Rhizome {ECO:0000303|PubMed:28185046};
RX   PubMed=28185046; DOI=10.1007/s10930-017-9700-7;
RA   Nishiyama Y., Fukamizo T., Yoneda K., Araki T.;
RT   "Complete amino acid sequence of a copper/zinc-superoxide dismutase from
RT   ginger rhizome.";
RL   Protein J. 36:98-107(2017).
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:0000269|PubMed:28185046};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:P07505};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P07505};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P07505};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P07505};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Active between pH 5 and 10. {ECO:0000269|PubMed:28185046};
CC       Temperature dependence:
CC         Active between 10 and 60 degrees Celsius.
CC         {ECO:0000269|PubMed:28185046};
CC   -!- SUBUNIT: Homodimer (Probable). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8L5E0}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; C0HK70; -.
DR   SMR; C0HK70; -.
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; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Antioxidant; Copper; Cytoplasm; Direct protein sequencing; Metal-binding;
KW   Oxidoreductase; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000305|PubMed:28185046"
FT   CHAIN           2..152
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /evidence="ECO:0000269|PubMed:28185046"
FT                   /id="PRO_0000438148"
FT   REGION          61..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         45
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P07505"
FT   BINDING         47
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P07505"
FT   BINDING         62
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P07505"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P07505"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P07505"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P07505"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P07505"
FT   BINDING         119
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P07505"
SQ   SEQUENCE   152 AA;  15127 MW;  3CF6EBA4C1371246 CRC64;
     MVKAVAVLGS SEGVKGTIYF VQEGDGPTTV TGSITGLKPG LHGFHVHALG DTTNGCMSTG
     PHFNPAGKEH GAPEDENRHA GDLGNATAGE DGIVTVSVVD SQIPLSGPNS IIGRAVVVHA
     DPDDLGKGGH ELSKTTGNAG GRVACGIIGL QG