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Database: UniProt
Entry: B6TAX5_MAIZE
LinkDB: B6TAX5_MAIZE
Original site: B6TAX5_MAIZE 
ID   B6TAX5_MAIZE            Unreviewed;       163 AA.
AC   B6TAX5;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   13-FEB-2019, entry version 73.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=100282741 {ECO:0000313|EnsemblPlants:Zm00001d028232_P004};
GN   ORFNames=ZEAMMB73_Zm00001d028232 {ECO:0000313|EMBL:ONL95140.1};
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|EMBL:ACG34258.1};
RN   [1] {ECO:0000313|EMBL:ACG34258.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA   Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E.,
RA   Tatarinova T.V., Zhang H., Swaller T.J., Lu Y.P., Bouck J.,
RA   Flavell R.B., Feldmann K.A.;
RT   "Insights into corn genes derived from large-scale cDNA sequencing.";
RL   Plant Mol. Biol. 69:179-194(2009).
RN   [2] {ECO:0000313|EMBL:ONL95140.1, ECO:0000313|EnsemblPlants:Zm00001d028232_P004, ECO:0000313|Proteomes:UP000007305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001d028232_P004,
RC   ECO:0000313|Proteomes:UP000007305};
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONL95140.1};
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   [3] {ECO:0000313|EnsemblPlants:Zm00001d028232_P004}
RP   IDENTIFICATION.
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001d028232_P004};
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; EU962140; ACG34258.1; -; mRNA.
DR   EMBL; CM007647; ONL95140.1; -; Genomic_DNA.
DR   RefSeq; NP_001149119.1; NM_001155647.1.
DR   UniGene; Zm.95194; -.
DR   STRING; 4577.GRMZM5G891739_P01; -.
DR   EnsemblPlants; Zm00001d028232_T004; Zm00001d028232_P004; Zm00001d028232.
DR   GeneID; 100282741; -.
DR   Gramene; Zm00001d028232_T004; Zm00001d028232_P004; Zm00001d028232.
DR   KEGG; zma:100282741; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263447; -.
DR   KO; K04565; -.
DR   OMA; HIHEATE; -.
DR   OrthoDB; 1574423at2759; -.
DR   Proteomes; UP000007305; Chromosome 1.
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   2: Evidence at transcript level;
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       19    157       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   163 AA;  16819 MW;  D810F685475AADF6 CRC64;
     MAGKAGGLKG VALIGGSANS TVAGVIHFFE DPSTRYTEVR GKVTGLTPGR HGFHIHVFGD
     TTNGCNSTGP HFNPHNKPHG APFDDERHLG DLGNIVANED GDAEVFIRDL QISLSGPHSI
     LGRAVVVHAD PDDLGRGGHE LSKSTGNAGA RIGCGIIGIQ SSV
//
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