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Database: UniProt
Entry: I1JRI7_SOYBN
LinkDB: I1JRI7_SOYBN
Original site: I1JRI7_SOYBN 
ID   I1JRI7_SOYBN            Unreviewed;       152 AA.
AC   I1JRI7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   10-APR-2019, entry version 44.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=GLYMA_03G242900 {ECO:0000313|EMBL:KRH68646.1};
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:KRH68647, ECO:0000313|Proteomes:UP000008827};
RN   [1] {ECO:0000313|EMBL:KRH68646.1, ECO:0000313|EnsemblPlants:KRH68647, ECO:0000313|Proteomes:UP000008827}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH68647,
RC   ECO:0000313|Proteomes:UP000008827};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH68646.1};
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:KRH68647}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH68647};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH68646.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH68646.1};
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; CM000836; KRH68646.1; -; Genomic_DNA.
DR   EMBL; CM000836; KRH68647.1; -; Genomic_DNA.
DR   UniGene; Gma.31145; -.
DR   STRING; 3847.GLYMA03G40280.1; -.
DR   EnsemblPlants; KRH68646; KRH68646; GLYMA_03G242900.
DR   EnsemblPlants; KRH68647; KRH68647; GLYMA_03G242900.
DR   Gramene; KRH68646; KRH68646; GLYMA_03G242900.
DR   Gramene; KRH68647; KRH68647; GLYMA_03G242900.
DR   OMA; HKGDIGN; -.
DR   Proteomes; UP000008827; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; 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   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       12    148       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   152 AA;  15236 MW;  C604A62327C9E537 CRC64;
     MVKAVAVLGS SEGVTGTIHF VQEGSGPTTV TGSLAGLKPG LHGFHVHALG DTTNGCLSTG
     SHFNPNNKEH GAPEDENRHA GDLGNVNVGD DGTVSFTITD SQIPLTGPNN IIGRAVVVHA
     DPDDLGKGGH ELSKTTGNAG GRVACGIIGL QG
//
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