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Entry: A0A1D6INM9_MAIZE
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Original site: A0A1D6INM9_MAIZE 
ID   A0A1D6INM9_MAIZE        Unreviewed;       165 AA.
AC   A0A1D6INM9;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   13-FEB-2019, entry version 15.
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:Zm00001d022505_P008};
GN   ORFNames=ZEAMMB73_Zm00001d022505 {ECO:0000313|EMBL:ONM60861.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae;
OC   PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae;
OC   Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EnsemblPlants:Zm00001d022505_P008, ECO:0000313|Proteomes:UP000007305};
RN   [1] {ECO:0000313|EMBL:ONM60861.1, ECO:0000313|EnsemblPlants:Zm00001d022505_P008, ECO:0000313|Proteomes:UP000007305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001d022505_P008,
RC   ECO:0000313|Proteomes:UP000007305};
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM60861.1};
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   [2] {ECO:0000313|EnsemblPlants:Zm00001d022505_P008}
RP   IDENTIFICATION.
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001d022505_P008};
RG   EnsemblPlants;
RL   Submitted (MAY-2017) 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|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.
CC       {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.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; CM007650; ONM60861.1; -; Genomic_DNA.
DR   RefSeq; XP_008651855.1; XM_008653633.1.
DR   UniGene; Zm.25; -.
DR   EnsemblPlants; Zm00001d022505_T008; Zm00001d022505_P008; Zm00001d022505.
DR   GeneID; 542260; -.
DR   Gramene; Zm00001d022505_T008; Zm00001d022505_P008; Zm00001d022505.
DR   OrthoDB; 1574423at2759; -.
DR   Proteomes; UP000007305; Chromosome 7.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; -; 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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007305};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007305};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       25    161       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   165 AA;  16654 MW;  D5F64ED2DE382C58 CRC64;
     MIYAVMHSAT ITETMVKAVA VLAGTDVKGT IFFSQEGDGP TTVTGSISGL KPGLHGFHVH
     ALGDTTNGCM STGPHFNPVG KEHGAPEDED RHAGDLGNVT AGEDGVVNVN ITDSQIPLAG
     PHSIIGRAVV VHADPDDLGK GGHELSKSTG NAGGRVACGI IGLQG
//
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