ID   P93801_MAIZE            Unreviewed;       152 AA.
AC   P93801;
DT   01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1997, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=sod4A {ECO:0000313|EMBL:AAB49913.1};
GN   Synonyms=Sod4A {ECO:0000313|EMBL:CAB57993.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:AAB49913.1};
RN   [1] {ECO:0000313|EMBL:CAB57993.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2482436; DOI=10.1007/BF00261150;
RA   Cannon R.E., Scandalios J.G.;
RT   "Two cDNAs encode two nearly identical Cu/Zn superoxide dismutase proteins
RT   in maize.";
RL   Mol. Gen. Genet. 219:1-8(1989).
RN   [2] {ECO:0000313|EMBL:AAB49913.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=W64A {ECO:0000313|EMBL:AAB49913.1};
RC   TISSUE=Leaf {ECO:0000313|EMBL:AAB49913.1};
RX   PubMed=8878695;
RA   Kernodle S.P., Scandalios J.G.;
RT   "A comparison of the structure and function of the highly homologous maize
RT   antioxidant Cu/Zn superoxide dismutase genes, Sod4 and Sod4A.";
RL   Genetics 144:317-328(1996).
RN   [3] {ECO:0000313|EMBL:AAB49913.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=W64A {ECO:0000313|EMBL:AAB49913.1};
RC   TISSUE=Leaf {ECO:0000313|EMBL:AAB49913.1};
RA   Quirk P.G., Krulwich T.A.;
RL   Submitted (JUL-2018) 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       {ECO:0000256|RuleBase:RU000393}.
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:0000256|ARBA:ARBA00001605,
CC         ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00010457, ECO:0000256|RuleBase:RU000393}.
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; U34727; AAB49913.1; -; Genomic_DNA.
DR   EMBL; X17564; CAB57993.1; -; mRNA.
DR   PIR; S72235; S72235.
DR   AlphaFoldDB; P93801; -.
DR   ExpressionAtlas; P93801; baseline and differential.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042542; P:response to hydrogen peroxide; TAS:AgBase.
DR   GO; GO:0000302; P:response to reactive oxygen species; IEP:AgBase.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:AgBase.
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   2: Evidence at transcript level;
KW   Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000393};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN          14..148
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   152 AA;  15089 MW;  691DFF62F88A7623 CRC64;
     MVKAVAVLGS SDGVKGTIFF TQEGDGPTAV TGSVSGLKPG LHGFHVHALG DTTNGCMSTG
     HDYNPASKEH GAPEDENRHA GDLGNVTAGA DGVANINVTD SQIPLTGPNS IIGRAVVVHA
     DPDDLGKGGH ELSKSTGNAG GRVACGIIGL QG
//