ID   SODF_SOYBN              Reviewed;         248 AA.
AC   P28759;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Superoxide dismutase [Fe], chloroplastic;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=SODB;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16668352; DOI=10.1104/pp.96.4.1393;
RA   Amasino R.M., Crowell D.N.;
RT   "Nucleotide sequence of an iron superoxide dismutase complementary DNA from
RT   soybean.";
RL   Plant Physiol. 96:1393-1394(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9648237; DOI=10.1271/bbb.62.1018;
RA   Arahira M., Nong V.H., Kadokura K., Kimura K., Udaka K., Fukazawa C.;
RT   "Molecular cloning and expression patterns of Cu/Zn-superoxide dismutases
RT   in developing soybean seeds.";
RL   Biosci. Biotechnol. Biochem. 62:1018-1021(1998).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological systems.
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   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M64267; AAA33960.1; -; mRNA.
DR   PIR; JW0085; JW0085.
DR   RefSeq; NP_001238486.1; NM_001251557.1.
DR   AlphaFoldDB; P28759; -.
DR   SMR; P28759; -.
DR   STRING; 3847.GLYMA20G33880.2; -.
DR   PRIDE; P28759; -.
DR   ProMEX; P28759; -.
DR   EnsemblPlants; KRG92190; KRG92190; GLYMA_20G196900.
DR   GeneID; 547823; -.
DR   Gramene; KRG92190; KRG92190; GLYMA_20G196900.
DR   KEGG; gmx:547823; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   HOGENOM; CLU_031625_0_0_1; -.
DR   InParanoid; P28759; -.
DR   OMA; KWWSLIN; -.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000008827; Chromosome 20.
DR   Genevisible; P28759; GM.
DR   GO; GO:0042644; C:chloroplast nucleoid; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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   2: Evidence at transcript level;
KW   Chloroplast; Iron; Metal-binding; Oxidoreductase; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..24
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..248
FT                   /note="Superoxide dismutase [Fe], chloroplastic"
FT                   /id="PRO_0000032890"
FT   BINDING         51
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   248 AA;  27842 MW;  BF1078AC2D3D222A CRC64;
     MASLGGLQNV SGINFLIKEG PKVNAKFELK PPPYPLNGLE PVMSQQTLEF HWGKHHKTYV
     ENLKKQVVGT ELDGKSLEEI IVTSYNKGDI LPAFNNAAQV WNHDFFWECM KPGGGGKPSG
     ELLELIERDF GSFVKFLDEF KAAAATQFGS GWAWLAYRAR KFDGENVANP PSPDEDNKLV
     VLKSPNAVNP LVWGGYYPLL TIDVWEHAYY LDFQNRRPDY ISVFMDKLVS WDAVSSRLEQ
     AKALITSA