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 27-MAR-2024, entry version 15.
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 OrthoDB; 3470597at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:UniProtKB.
DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 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:SF71; SUPEROXIDE DISMUTASE; 1.
DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR PRINTS; PR00068; CUZNDISMTASE.
DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 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
//
