SODM_CHLRE
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 03-AUG-2022, entry version 123.
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; core chlorophytes; Chlorophyceae;
OC CS clade; 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 Chlamydomonas
RT 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 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 family.
CC {ECO:0000305}.
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DR EMBL; U24500; AAA80639.1; -; mRNA.
DR PIR; T08047; T08047.
DR RefSeq; XP_001700058.1; XM_001700006.1.
DR AlphaFoldDB; Q42684; -.
DR SMR; Q42684; -.
DR STRING; 3055.EDP07754; -.
DR ProMEX; Q42684; -.
DR EnsemblPlants; PNW86799; PNW86799; CHLRE_02g096150v5.
DR GeneID; 5725400; -.
DR Gramene; PNW86799; PNW86799; CHLRE_02g096150v5.
DR KEGG; cre:CHLRE_02g096150v5; -.
DR eggNOG; KOG0876; Eukaryota.
DR HOGENOM; CLU_031625_0_1_1; -.
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; 3.55.40.20; -; 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; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..218
FT /note="Superoxide dismutase [Mn], mitochondrial"
FT /id="PRO_0000032893"
FT BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="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
