SODM1_CAEEL
ID SODM1_CAEEL Reviewed; 221 AA.
AC P31161;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Superoxide dismutase [Mn] 1, mitochondrial;
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=sod-2; Synonyms=sdm-1; ORFNames=F10D11.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Suzuki N., Ishii N., Suzuki K.;
RT "Cloning and characterization of manganese superoxide dismutase gene in
RT C.elegans.";
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8905235; DOI=10.1093/dnares/3.3.171;
RA Suzuki N., Inokuma K., Yasuda K., Ishii N.;
RT "Cloning, sequencing and mapping of a manganese superoxide dismutase gene
RT of the nematode Caenorhabditis elegans.";
RL DNA Res. 3:171-174(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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; D12984; BAA02363.1; -; mRNA.
DR EMBL; D85499; BAA12821.1; -; Genomic_DNA.
DR EMBL; Z81057; CAB02913.1; -; Genomic_DNA.
DR PIR; JC5122; JC5122.
DR RefSeq; NP_492290.1; NM_059889.4.
DR PDB; 3DC6; X-ray; 1.80 A; A/C=25-221.
DR PDBsum; 3DC6; -.
DR AlphaFoldDB; P31161; -.
DR SMR; P31161; -.
DR BioGRID; 38065; 17.
DR STRING; 6239.F10D11.1.2; -.
DR iPTMnet; P31161; -.
DR EPD; P31161; -.
DR PaxDb; P31161; -.
DR PeptideAtlas; P31161; -.
DR EnsemblMetazoa; F10D11.1.1; F10D11.1.1; WBGene00004931.
DR GeneID; 172632; -.
DR KEGG; cel:CELE_F10D11.1; -.
DR UCSC; F10D11.1.1; c. elegans.
DR CTD; 172632; -.
DR WormBase; F10D11.1; CE09323; WBGene00004931; sod-2.
DR eggNOG; KOG0876; Eukaryota.
DR GeneTree; ENSGT00390000011877; -.
DR HOGENOM; CLU_031625_2_1_1; -.
DR InParanoid; P31161; -.
DR OMA; KWGSFDK; -.
DR OrthoDB; 1353361at2759; -.
DR PhylomeDB; P31161; -.
DR Reactome; R-CEL-3299685; Detoxification of Reactive Oxygen Species.
DR EvolutionaryTrace; P31161; -.
DR PRO; PR:P31161; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004931; Expressed in embryo and 4 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005746; C:mitochondrial respirasome; IDA:WormBase.
DR GO; GO:0005739; C:mitochondrion; HDA:WormBase.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:WormBase.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:WormBase.
DR GO; GO:0019430; P:removal of superoxide radicals; IMP:WormBase.
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 1: Evidence at protein level;
KW 3D-structure; Manganese; Metal-binding; Mitochondrion; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 25..221
FT /note="Superoxide dismutase [Mn] 1, mitochondrial"
FT /id="PRO_0000032876"
FT BINDING 50
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT TURN 35..41
FT /evidence="ECO:0007829|PDB:3DC6"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:3DC6"
FT HELIX 54..74
FT /evidence="ECO:0007829|PDB:3DC6"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:3DC6"
FT HELIX 85..103
FT /evidence="ECO:0007829|PDB:3DC6"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:3DC6"
FT HELIX 127..139
FT /evidence="ECO:0007829|PDB:3DC6"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:3DC6"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:3DC6"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:3DC6"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:3DC6"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:3DC6"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:3DC6"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:3DC6"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:3DC6"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:3DC6"
FT HELIX 209..219
FT /evidence="ECO:0007829|PDB:3DC6"
SQ SEQUENCE 221 AA; 24537 MW; EEA518B2800379F7 CRC64;
MLQNTVRCVS KLVQPITGVA AVRSKHSLPD LPYDYADLEP VISHEIMQLH HQKHHATYVN
NLNQIEEKLH EAVSKGNVKE AIALQPALKF NGGGHINHSI FWTNLAKDGG EPSAELLTAI
KSDFGSLDNL QKQLSASTVA VQGSGWGWLG YCPKGKILKV ATCANQDPLE ATTGLVPLFG
IDVWEHAYYL QYKNVRPDYV NAIWKIANWK NVSERFAKAQ Q
