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Database: UniProt
Entry: P11796
LinkDB: P11796
Original site: P11796 
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   05-DEC-2018, entry version 91.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; lamiids; Solanales; Solanaceae;
OC   Nicotianoideae; Nicotianeae; Nicotiana.
OX   NCBI_TaxID=4092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. P2;
RX   PubMed=2540959;
RA   Bowler C., Alliotte T., de Loose M., van Montagu M., Inze D.;
RT   "The induction of manganese superoxide dismutase in response to stress
RT   in 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
RT   amino acid-sequence analysis of proteins electroblotted from two-
RT   dimensional gel-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
CC       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
CC       family. {ECO:0000305}.
DR   EMBL; X14482; CAA32643.1; -; mRNA.
DR   PIR; I28027; I28027.
DR   PIR; S03639; S03639.
DR   ProteinModelPortal; P11796; -.
DR   SMR; P11796; -.
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; -; 1.
DR   Gene3D; 2.40.500.20; -; 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   Direct protein sequencing; Manganese; Metal-binding; Mitochondrion;
KW   Oxidoreductase; Transit peptide.
FT   TRANSIT       1     24       Mitochondrion.
FT                                {ECO:0000269|PubMed:16578810}.
FT   CHAIN        25    228       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000032899.
FT   METAL        52     52       Manganese. {ECO:0000250}.
FT   METAL       100    100       Manganese. {ECO:0000250}.
FT   METAL       189    189       Manganese. {ECO:0000250}.
FT   METAL       193    193       Manganese. {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
//
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