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Entry: I1LKZ3_SOYBN
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ID   I1LKZ3_SOYBN            Unreviewed;       204 AA.
AC   I1LKZ3;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   10-APR-2019, entry version 43.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=100815376 {ECO:0000313|EnsemblPlants:KRH30558};
GN   ORFNames=GLYMA_11G192700 {ECO:0000313|EMBL:KRH30558.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
OC   50 kb inversion clade; NPAAA clade; indigoferoid/millettioid clade;
OC   Phaseoleae; Glycine; Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH30558, ECO:0000313|Proteomes:UP000008827};
RN   [1] {ECO:0000313|EMBL:KRH30558.1, ECO:0000313|EnsemblPlants:KRH30558, ECO:0000313|Proteomes:UP000008827}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH30558,
RC   ECO:0000313|Proteomes:UP000008827};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH30558.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U.,
RA   May G.D., Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K.,
RA   Sandhu D., Valliyodan B., Lindquist E., Peto M., Grant D., Shu S.,
RA   Goodstein D., Barry K., Futrell-Griggs M., Abernathy B., Du J.,
RA   Tian Z., Zhu L., Gill N., Joshi T., Libault M., Sethuraman A.,
RA   Zhang X.-C., Shinozaki K., Nguyen H.T., Wing R.A., Cregan P.,
RA   Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.C.,
RA   Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH30558}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH30558};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH30558.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH30558.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D., Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L.,
RA   Gill N., Joshi T., Libault M., Sethuraman A., Zhang X., Shinozaki K.,
RA   Nguyen H., Wing R., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R., Jackson S.;
RT   "WGS assembly of Glycine max.";
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|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; CM000844; KRH30558.1; -; Genomic_DNA.
DR   RefSeq; XP_003538169.1; XM_003538121.2.
DR   UniGene; Gma.6384; -.
DR   EnsemblPlants; KRH30558; KRH30558; GLYMA_11G192700.
DR   GeneID; 100815376; -.
DR   Gramene; KRH30558; KRH30558; GLYMA_11G192700.
DR   KEGG; gmx:100815376; -.
DR   KO; K04565; -.
DR   OrthoDB; 1574423at2759; -.
DR   Proteomes; UP000008827; Chromosome 11.
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:UP000008827};
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:UP000008827};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       62    199       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   204 AA;  20888 MW;  7DE281B67E7A6796 CRC64;
     MQLAMAANAV VSPSPFRPQP FLRSSFSGVS VKLTPQSITL SRSKPLTVFA ATKKAVAVLK
     GTSAVEGVAT LIQEDDGPTT VSVRITGLTP GLHGFHLHEY GDTTNGCIST GAHFNPNKLT
     HGAPEDEVRH AGDLGNIVAN AEGVAEATIV DNQIPLSGPN SVVGRALVVH ELEDDLGKGG
     HELSLTTGNA GGRLACGVVG LTPA
//
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