SODC5_MAIZE
ID SODC5_MAIZE Reviewed; 152 AA.
AC P23346;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Superoxide dismutase [Cu-Zn] 4AP;
DE EC=1.15.1.1;
GN Name=SODCC.2; Synonyms=SOD4AP;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
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 -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; X17565; CAB57992.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001105704.1; NM_001112234.1.
DR RefSeq; NP_001307761.1; NM_001320832.1.
DR RefSeq; XP_008660153.1; XM_008661931.1.
DR AlphaFoldDB; P23346; -.
DR SMR; P23346; -.
DR STRING; 4577.GRMZM2G058522_P06; -.
DR PaxDb; P23346; -.
DR EnsemblPlants; Zm00001eb394700_T001; Zm00001eb394700_P001; Zm00001eb394700.
DR EnsemblPlants; Zm00001eb394700_T002; Zm00001eb394700_P002; Zm00001eb394700.
DR EnsemblPlants; Zm00001eb394700_T003; Zm00001eb394700_P003; Zm00001eb394700.
DR EnsemblPlants; Zm00001eb394700_T005; Zm00001eb394700_P005; Zm00001eb394700.
DR EnsemblPlants; Zm00001eb394700_T006; Zm00001eb394700_P006; Zm00001eb394700.
DR EnsemblPlants; Zm00001eb394700_T007; Zm00001eb394700_P007; Zm00001eb394700.
DR GeneID; 103639134; -.
DR GeneID; 542722; -.
DR Gramene; Zm00001eb394700_T001; Zm00001eb394700_P001; Zm00001eb394700.
DR Gramene; Zm00001eb394700_T002; Zm00001eb394700_P002; Zm00001eb394700.
DR Gramene; Zm00001eb394700_T003; Zm00001eb394700_P003; Zm00001eb394700.
DR Gramene; Zm00001eb394700_T005; Zm00001eb394700_P005; Zm00001eb394700.
DR Gramene; Zm00001eb394700_T006; Zm00001eb394700_P006; Zm00001eb394700.
DR Gramene; Zm00001eb394700_T007; Zm00001eb394700_P007; Zm00001eb394700.
DR KEGG; zma:103639134; -.
DR KEGG; zma:542722; -.
DR MaizeGDB; 47586; -.
DR eggNOG; KOG0441; Eukaryota.
DR HOGENOM; CLU_056632_4_1_1; -.
DR OMA; EHGFNNP; -.
DR OrthoDB; 1574423at2759; -.
DR Proteomes; UP000007305; Chromosome 9.
DR ExpressionAtlas; P23346; baseline and differential.
DR Genevisible; P23346; ZM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Antioxidant; Copper; Cytoplasm; Disulfide bond; Metal-binding;
KW Oxidoreductase; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..152
FT /note="Superoxide dismutase [Cu-Zn] 4AP"
FT /id="PRO_0000164143"
FT BINDING 45
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 56..145
FT /evidence="ECO:0000250"
SQ SEQUENCE 152 AA; 15071 MW; C1A373B76C533BB7 CRC64;
MVKAVAVLGS SDGVKGTIFF TQEGDGPTAV TGSVSGLKPG LHGFHVHALG DTTNGCMSTG
PHYNPASKEH GAPEDENRHA GDLGNVTAGA DGVANINVTD SQIPLTGPNS IIGRAVVVHA
DPDDLGKGGH ELSKSTGNAG GRVACGIIGL QG
