ID SODM_NICPL Reviewed; 228 AA.
AC P11796;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=SODA;
OS Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4092;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. P2;
RX PubMed=2540959; DOI=10.1002/j.1460-2075.1989.tb03345.x;
RA Bowler C., Alliotte T., de Loose M., van Montagu M., Inze D.;
RT "The induction of manganese superoxide dismutase in response to stress in
RT Nicotiana plumbaginifolia.";
RL EMBO J. 8:31-38(1989).
RN [2]
RP PROTEIN SEQUENCE OF 25-47.
RX PubMed=16578810; DOI=10.1073/pnas.84.14.4806;
RA Bauw G., de Loose M., Inze D., van Montagu M., Vandekerckhove J.;
RT "Alterations in the phenotype of plant cells studied by NH2-terminal amino
RT acid-sequence analysis of proteins electroblotted from two-dimensional gel-
RT separated total extracts.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:4806-4810(1987).
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=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; X14482; CAA32643.1; -; mRNA.
DR PIR; I28027; I28027.
DR PIR; S03639; S03639.
DR AlphaFoldDB; P11796; -.
DR SMR; P11796; -.
DR BRENDA; 1.15.1.1; 3640.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
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; PTHR11404:SF44; SUPEROXIDE DISMUTASE; 1.
DR PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 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 1: Evidence at protein level;
KW Direct protein sequencing; Manganese; Metal-binding; Mitochondrion;
KW Oxidoreductase; Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:16578810"
FT CHAIN 25..228
FT /note="Superoxide dismutase [Mn], mitochondrial"
FT /id="PRO_0000032899"
FT BINDING 52
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
SQ SEQUENCE 228 AA; 25504 MW; 9F4D75B2ADDAD7F6 CRC64;
MALRTLVSRR TLATGLGFRQ QLRGLQTFSL PDLPYDYGAL EPAISGDIMQ LHHQNHHQTY
VTNYNKALEQ LHDAISKGDA PTVAKLHSAI KFNGGGHINH SIFWKNLAPV REGGGEPPKG
SLGWAIDTNF GSLEALVQKM NAEGAALQGS GWVWLGVDKE LKRLVIETTA NQDPLVSKGA
NLVPLLGIDV WEHAYYLQYK NVRPDYLKNI WKVMNWKYAN EVYEKECP
//
