ID C4J094_MAIZE Unreviewed; 210 AA.
AC C4J094;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN Name=542260 {ECO:0000313|EnsemblPlants:Zm00001eb330020_P005};
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:ACR34594.1};
RN [1] {ECO:0000313|EMBL:ACR34594.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B73 {ECO:0000313|EMBL:ACR34594.1};
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [2] {ECO:0000313|EnsemblPlants:Zm00001eb330020_P005, ECO:0000313|Proteomes:UP000007305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb330020_P005,
RC ECO:0000313|Proteomes:UP000007305};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:Zm00001eb330020_P005}
RP IDENTIFICATION.
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb330020_P005};
RG EnsemblPlants;
RL Submitted (MAY-2021) to UniProtKB.
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; BT084241; ACR34594.1; -; mRNA.
DR RefSeq; XP_008651854.1; XM_008653632.1.
DR AlphaFoldDB; C4J094; -.
DR EnsemblPlants; Zm00001eb330020_T005; Zm00001eb330020_P005; Zm00001eb330020.
DR GeneID; 542260; -.
DR Gramene; Zm00001eb330020_T005; Zm00001eb330020_P005; Zm00001eb330020.
DR HOGENOM; CLU_056632_1_2_1; -.
DR OrthoDB; 3470597at2759; -.
DR Proteomes; UP000007305; Chromosome 7.
DR ExpressionAtlas; C4J094; 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 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:SF83; SUPEROXIDE DISMUTASE [CU-ZN] 2; 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 {ECO:0000256|ARBA:ARBA00022862};
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000393};
KW Metal-binding {ECO:0000256|RuleBase:RU000393};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000393};
KW Proteomics identification {ECO:0007829|PeptideAtlas:C4J094};
KW Reference proteome {ECO:0000313|Proteomes:UP000007305};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000393}.
FT DOMAIN 72..206
FT /note="Superoxide dismutase copper/zinc binding"
FT /evidence="ECO:0000259|Pfam:PF00080"
SQ SEQUENCE 210 AA; 21918 MW; BAC9A89AFA4F92F3 CRC64;
MDIGCVDDLC GDAFSYGMLT RHAAEFWFFS TSDLNILPPC PLEMNFFPFV GFWWQITETM
VKAVAVLAGT DVKGTIFFSQ EGDGPTTVTG SISGLKPGLH GFHVHALGDT TNGCMSTGPH
FNPVGKEHGA PEDEDRHAGD LGNVTAGEDG VVNVNITDSQ IPLAGPHSII GRAVVVHADP
DDLGKGGHEL SKSTGNAGGR VACGIIGLQG
//
