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Database: UniProt
Entry: Q42684
LinkDB: Q42684
Original site: Q42684 
ID   SODM_CHLRE              Reviewed;         218 AA.
AC   Q42684;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JAN-2019, entry version 111.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=SODA; Synonyms=SOD1;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae;
OC   Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=137c / CC-125;
RA   Kitayama K., Kitayama M., Togasaki R.K.;
RT   "A cDNA clone encoding a manganese-superoxide dismutase from
RT   Chlamydomonas reinhardtii.";
RL   (er) Plant Gene Register PGR95-034(1995).
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; U24500; AAA80639.1; -; mRNA.
DR   PIR; T08047; T08047.
DR   RefSeq; XP_001700058.1; XM_001700006.1.
DR   UniGene; Cre.13231; -.
DR   ProteinModelPortal; Q42684; -.
DR   SMR; Q42684; -.
DR   ProMEX; Q42684; -.
DR   EnsemblPlants; PNW86799; PNW86799; CHLRE_02g096150v5.
DR   GeneID; 5725400; -.
DR   Gramene; PNW86799; PNW86799; CHLRE_02g096150v5.
DR   KEGG; cre:CHLREDRAFT_53941; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; WKVMTNP; -.
DR   OrthoDB; 1353361at2759; -.
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   Manganese; Metal-binding; Mitochondrion; Oxidoreductase;
KW   Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion. {ECO:0000255}.
FT   CHAIN         ?    218       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000032893.
FT   METAL        27     27       Manganese. {ECO:0000250}.
FT   METAL        84     84       Manganese. {ECO:0000250}.
FT   METAL       174    174       Manganese. {ECO:0000250}.
FT   METAL       178    178       Manganese. {ECO:0000250}.
SQ   SEQUENCE   218 AA;  23900 MW;  728CF66B4130BF09 CRC64;
     MAQALPPLPY DYGSLEPHVD ATTMNIHHTK HHQTYVNNLN AALDKFPELK DLGLVDLNKA
     VGTDKLPKDV ATVIRNNGGG HYNHSFFWKV MTNPSNTNGP NGDVKAAIEA SFGSVDEMKA
     KFNAAAAGRF GSGWAWLSVK PDGSLSIDST PNQDNPLMTA LPDVAGGIPL LGLDVWEHAY
     YLKYQNRRPE YIAAWWNVVN WEQVAENYKA AQAGTVPL
//
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