ID   SODF_METTH              Reviewed;         205 AA.
AC   P18868;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sod; OrderedLocusNames=MTH_160;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2122808; DOI=10.1016/0003-9861(90)90633-a;
RA   Takao M., Oikawa A., Yasui A.;
RT   "Characterization of a superoxide dismutase gene from the archaebacterium
RT   Methanobacterium thermoautotrophicum.";
RL   Arch. Biochem. Biophys. 283:210-216(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=1907270; DOI=10.1016/s0021-9258(18)98656-4;
RA   Takao M., Yasui A., Oikawa A.;
RT   "Unique characteristics of superoxide dismutase of a strictly anaerobic
RT   archaebacterium Methanobacterium thermoautotrophicum.";
RL   J. Biol. Chem. 266:14151-14154(1991).
RN   [4]
RP   STRUCTURE BY NMR.
RX   PubMed=11670835; DOI=10.1021/ic981172o;
RA   Renault J.P., Morgenstern-Badarau I., Piccioli M.;
RT   "Thermochromic conformational change of Methanobacterium
RT   thermoautotrophicum iron superoxide dismutase.";
RL   Inorg. Chem. 38:614-615(1999).
RN   [5]
RP   EPR SPECTROSCOPY.
RX   PubMed=11197024; DOI=10.1021/ic0000451;
RA   Renault J.P., Verchere-Beaur C., Morgenstern-Badarau I., Yamakura F.,
RA   Gerloch M.;
RT   "EPR and ligand field studies of iron superoxide dismutases and iron-
RT   substituted manganese superoxide dismutases: relationships between
RT   electronic structure of the active site and activity.";
RL   Inorg. Chem. 39:2666-2675(2000).
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=Fe cation; Xref=ChEBI:CHEBI:24875;
CC       Note=Binds 1 Fe cation per subunit.;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; D00614; BAA00489.1; -; Genomic_DNA.
DR   EMBL; AE000666; AAB84666.1; -; Genomic_DNA.
DR   PIR; F69080; F69080.
DR   PDB; 1MA1; X-ray; 2.60 A; A/B/C/D/E/F=1-205.
DR   PDBsum; 1MA1; -.
DR   AlphaFoldDB; P18868; -.
DR   SMR; P18868; -.
DR   STRING; 187420.MTH_160; -.
DR   EnsemblBacteria; AAB84666; AAB84666; MTH_160.
DR   KEGG; mth:MTH_160; -.
DR   PATRIC; fig|187420.15.peg.132; -.
DR   HOGENOM; CLU_031625_2_2_2; -.
DR   OMA; KWGSFDK; -.
DR   EvolutionaryTrace; P18868; -.
DR   Proteomes; UP000005223; Chromosome.
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   1: Evidence at protein level;
KW   3D-structure; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..205
FT                   /note="Superoxide dismutase [Fe]"
FT                   /id="PRO_0000160006"
FT   BINDING         33
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         81
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         167
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         171
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   TURN            18..24
FT                   /evidence="ECO:0007829|PDB:1MA1"
FT   HELIX           27..35
FT                   /evidence="ECO:0007829|PDB:1MA1"
FT   HELIX           37..57
FT                   /evidence="ECO:0007829|PDB:1MA1"
FT   HELIX           64..86
FT                   /evidence="ECO:0007829|PDB:1MA1"
FT   TURN            91..93
FT                   /evidence="ECO:0007829|PDB:1MA1"
FT   HELIX           100..110
FT                   /evidence="ECO:0007829|PDB:1MA1"
FT   HELIX           113..125
FT                   /evidence="ECO:0007829|PDB:1MA1"
FT   STRAND          128..138
FT                   /evidence="ECO:0007829|PDB:1MA1"
FT   TURN            139..142
FT                   /evidence="ECO:0007829|PDB:1MA1"
FT   STRAND          143..150
FT                   /evidence="ECO:0007829|PDB:1MA1"
FT   TURN            151..153
FT                   /evidence="ECO:0007829|PDB:1MA1"
FT   STRAND          163..167
FT                   /evidence="ECO:0007829|PDB:1MA1"
FT   HELIX           170..172
FT                   /evidence="ECO:0007829|PDB:1MA1"
FT   HELIX           174..177
FT                   /evidence="ECO:0007829|PDB:1MA1"
FT   HELIX           181..188
FT                   /evidence="ECO:0007829|PDB:1MA1"
FT   TURN            189..191
FT                   /evidence="ECO:0007829|PDB:1MA1"
FT   HELIX           194..202
FT                   /evidence="ECO:0007829|PDB:1MA1"
SQ   SEQUENCE   205 AA;  24096 MW;  F38A93265FB34AD5 CRC64;
     MNDLEKKFYE LPELPYPYDA LEPHISREQL TIHHQKHHQA YVDGANALLR KLDEARESDT
     DVDIKAALKE LSFHVGGYVL HLFFWGNMGP ADECGGEPSG KLAEYIEKDF GSFERFRKEF
     SQAAISAEGS GWAVLTYCQR TDRLFIMQVE KHNVNVIPHF RILLVLDVWE HAYYIDYRNV
     RPDYVEAFWN IVNWKEVEKR FEDIL