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Database: UniProt
Entry: O49066
LinkDB: O49066
Original site: O49066 
ID   SODM_CAPAN              Reviewed;         228 AA.
AC   O49066;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   05-DEC-2018, entry version 84.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=SODA;
OS   Capsicum annuum (Bell pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae;
OC   Capsiceae; Capsicum.
OX   NCBI_TaxID=4072;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Il K.S., Sun A.C.;
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AF036936; AAB88870.1; -; mRNA.
DR   PIR; T08045; T08045.
DR   RefSeq; NP_001311927.1; NM_001324998.1.
DR   UniGene; Can.6482; -.
DR   ProteinModelPortal; O49066; -.
DR   SMR; O49066; -.
DR   GeneID; 107871142; -.
DR   KEGG; cann:107871142; -.
DR   KO; K04564; -.
DR   Proteomes; UP000189700; Genome assembly.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Complete proteome; Manganese; Metal-binding; Mitochondrion;
KW   Oxidoreductase; Transit peptide.
FT   TRANSIT       1     24       Mitochondrion. {ECO:0000250}.
FT   CHAIN        25    228       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000032892.
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;  25512 MW;  4835341291182261 CRC64;
     MALRNLMTKK PFAGILTFRQ QLRCVQTFSL PDLSYDYGAL EPAISGEIMQ LHHQKHHQTY
     ITNYNNALQQ LHDAINKGDS PTVAKLQGAI KFNGGGHINH SVFWKNLAPT REGGGEPPKG
     SLGSAIDTNF GSLEAVIQKM NAEGAALQGS GWVWLGLDKE LKRLVIETTA NQDPLVIKGP
     NLVPLLGIDV WEHAYYLQYK NVKPDYLKNI WKVINWKYAA EVYEKECP
//
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