SODF2_ORYSJ
ID SODF2_ORYSJ Reviewed; 255 AA.
AC Q5VSB7; A0A0P0WSV1; Q9ZWM8;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Superoxide dismutase [Fe] 2, chloroplastic {ECO:0000305};
DE EC=1.15.1.1 {ECO:0000269|PubMed:10192910};
DE AltName: Full=Iron-superoxide dismutase {ECO:0000303|PubMed:10192910};
DE Flags: Precursor;
GN OrderedLocusNames=Os06g0143000 {ECO:0000312|EMBL:BAS96109.1},
GN LOC_Os06g05110 {ECO:0000305};
GN ORFNames=P0535G04.31 {ECO:0000312|EMBL:BAD67658.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], COFACTOR, FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND INDUCTION BY LIGHT.
RC STRAIN=cv. Nipponbare;
RX PubMed=10192910; DOI=10.1271/bbb.63.302;
RA Kaminaka H., Morita S., Tokumoto M., Yokoyama H., Masumura T., Tanaka K.;
RT "Molecular cloning and characterization of a cDNA for an iron-superoxide
RT dismutase in rice (Oryza sativa L.).";
RL Biosci. Biotechnol. Biochem. 63:302-308(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC {ECO:0000269|PubMed:10192910}.
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:0000269|PubMed:10192910};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697;
CC Evidence={ECO:0000269|PubMed:10192910};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:10192910};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:10192910};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8IAY6}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in the stems of the young
CC seedlings, etiolated seedlings and embryogenic calli, but only
CC minimally expressed in the leaves and the roots.
CC {ECO:0000269|PubMed:10192910}.
CC -!- INDUCTION: By light. {ECO:0000269|PubMed:10192910}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AB014056; BAA37131.1; -; mRNA.
DR EMBL; AP000399; BAD67658.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF18688.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS96109.1; -; Genomic_DNA.
DR EMBL; AK062073; BAG88209.1; -; mRNA.
DR EMBL; AK071301; BAG92419.1; -; mRNA.
DR PIR; JG0179; JG0179.
DR RefSeq; XP_015642495.1; XM_015787009.1.
DR RefSeq; XP_015642496.1; XM_015787010.1.
DR AlphaFoldDB; Q5VSB7; -.
DR SMR; Q5VSB7; -.
DR STRING; 4530.OS06T0143000-01; -.
DR PaxDb; Q5VSB7; -.
DR PRIDE; Q5VSB7; -.
DR EnsemblPlants; Os06t0143000-01; Os06t0143000-01; Os06g0143000.
DR GeneID; 4340091; -.
DR Gramene; Os06t0143000-01; Os06t0143000-01; Os06g0143000.
DR KEGG; osa:4340091; -.
DR eggNOG; KOG0876; Eukaryota.
DR HOGENOM; CLU_031625_0_0_1; -.
DR InParanoid; Q5VSB7; -.
DR OMA; YLHSIFW; -.
DR OrthoDB; 1353361at2759; -.
DR PlantReactome; R-OSA-1119403; Removal of superoxide radicals.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q5VSB7; OS.
DR GO; GO:0042644; C:chloroplast nucleoid; IBA:GO_Central.
DR GO; GO:0009579; C:thylakoid; IEA:EnsemblPlants.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:UniProtKB.
DR Gene3D; 1.10.287.990; -; 1.
DR Gene3D; 3.55.40.20; -; 1.
DR InterPro; IPR001189; Mn/Fe_SOD.
DR InterPro; IPR019833; Mn/Fe_SOD_BS.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR019831; Mn/Fe_SOD_N.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Iron; Metal-binding; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..32
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 33..255
FT /note="Superoxide dismutase [Fe] 2, chloroplastic"
FT /id="PRO_0000421268"
FT BINDING 67
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q8IAY6"
FT BINDING 119
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q8IAY6"
FT BINDING 203
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q8IAY6"
FT BINDING 207
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q8IAY6"
FT CONFLICT 170
FT /note="W -> L (in Ref. 1; BAA37131)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="F -> L (in Ref. 1; BAA37131)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 29477 MW; C1231959CBD2ACF8 CRC64;
MAAFASALRV LPSPPAAVPR RLRSREQRQG CRSRRYSKVV AYYALTTPPY KLDALEPYIS
KRTVELHWGK HQQDYVDSLN KQLATSMFYG YTLEELIKEA YNNGNPLPEY NNAAQVWNHH
FFWESMQPEG GGSPGRGVLQ QIEKDFGSFT NFREEFIRSA LSLLGSGWVW LVLKRKERKF
SVVHTQNAIS PLALGDIPLI NLDLWEHAYY LDYKDDRRMY VTNFIDHLVS WDTVTLRMMR
AEAFVNLGEP NIPVA
