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Database: UniProt
Entry: I1QKG1_ORYGL
LinkDB: I1QKG1_ORYGL
Original site: I1QKG1_ORYGL 
ID   I1QKG1_ORYGL            Unreviewed;       211 AA.
AC   I1QKG1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   13-FEB-2019, entry version 39.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
OS   Oryza glaberrima (African rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA08G0191200.1, ECO:0000313|Proteomes:UP000007306};
RN   [1] {ECO:0000313|EnsemblPlants:ORGLA08G0191200.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 96717 {ECO:0000313|EnsemblPlants:ORGLA08G0191200.1};
RA   Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA   Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA   Zuccolo A.;
RT   "The complete genome of Oryza glaberrima.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORGLA08G0191200.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) 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   STRING; 4538.ORGLA08G0191200.1; -.
DR   EnsemblPlants; ORGLA08G0191200.1; ORGLA08G0191200.1; ORGLA08G0191200.
DR   Gramene; ORGLA08G0191200.1; ORGLA08G0191200.1; ORGLA08G0191200.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   OMA; MAKAVCT; -.
DR   Proteomes; UP000007306; Unassembled WGS sequence.
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:UP000007306};
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:UP000007306};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26    211       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003651605.
FT   DOMAIN       69    206       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   211 AA;  21287 MW;  5B00CD86D3485594 CRC64;
     MQAILAAAMA AQTLLFSATA PPASLFQSPS SARPFHSLRL AAGPGGAAAA RALVVADATK
     KAVAVLKGTS QVEGVVTLTQ DDQGPTTVNV RVTGLTPGLH GFHLHEFGDT TNGCISTGPH
     FNPNNLTHGA PEDEVRHAGD LGNIVANAEG VAEATIVDKQ IPLSGPNSVV GRAFVVHELE
     DDLGKGGHEL SLSTGNAGGR LACGVVGLTP L
//
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