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 27-MAR-2024, entry version 130.
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}.
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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.P28759; -.
DR PaxDb; 3847-GLYMA20G33880-2; -.
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; EETIRYH; -.
DR OrthoDB; 4839at2759; -.
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; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 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 PANTHER; PTHR42769; SUPEROXIDE DISMUTASE; 1.
DR PANTHER; PTHR42769:SF3; SUPEROXIDE DISMUTASE [FE] 2, CHLOROPLASTIC; 1.
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; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 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
//
