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Database: UniProt/SWISS-PROT
Entry: SODF_METTH
LinkDB: SODF_METTH
Original site: SODF_METTH 
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   25-OCT-2017, entry version 127.
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 /
OS   JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   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
RT   archaebacterium 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.,
RA   Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D.,
RA   Spadafora R., Vicare R., Wang Y., Wierzbowski J., Gibson R.,
RA   Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S.,
RA   McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M.,
RA   Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum
RT   deltaH: functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=1907270;
RA   Takao M., Yasui A., Oikawa A.;
RT   "Unique characteristics of superoxide dismutase of a strictly
RT   anaerobic 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
CC       systems.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
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
CC       family. {ECO:0000305}.
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   ProteinModelPortal; P18868; -.
DR   SMR; P18868; -.
DR   STRING; 187420.MTH160; -.
DR   EnsemblBacteria; AAB84666; AAB84666; MTH_160.
DR   KEGG; mth:MTH_160; -.
DR   PATRIC; fig|187420.15.peg.132; -.
DR   eggNOG; arCOG04147; Archaea.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; POG093Z0AKF; -.
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   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; Complete proteome; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    205       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000160006.
FT   METAL        33     33       Iron.
FT   METAL        81     81       Iron.
FT   METAL       167    167       Iron.
FT   METAL       171    171       Iron.
FT   TURN         18     24       {ECO:0000244|PDB:1MA1}.
FT   HELIX        27     35       {ECO:0000244|PDB:1MA1}.
FT   HELIX        37     57       {ECO:0000244|PDB:1MA1}.
FT   HELIX        64     86       {ECO:0000244|PDB:1MA1}.
FT   TURN         91     93       {ECO:0000244|PDB:1MA1}.
FT   HELIX       100    110       {ECO:0000244|PDB:1MA1}.
FT   HELIX       113    125       {ECO:0000244|PDB:1MA1}.
FT   STRAND      128    138       {ECO:0000244|PDB:1MA1}.
FT   TURN        139    142       {ECO:0000244|PDB:1MA1}.
FT   STRAND      143    150       {ECO:0000244|PDB:1MA1}.
FT   TURN        151    153       {ECO:0000244|PDB:1MA1}.
FT   STRAND      163    167       {ECO:0000244|PDB:1MA1}.
FT   HELIX       170    172       {ECO:0000244|PDB:1MA1}.
FT   HELIX       174    177       {ECO:0000244|PDB:1MA1}.
FT   HELIX       181    188       {ECO:0000244|PDB:1MA1}.
FT   TURN        189    191       {ECO:0000244|PDB:1MA1}.
FT   HELIX       194    202       {ECO:0000244|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
//
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