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Database: UniProt
Entry: P00449
LinkDB: P00449
Original site: P00449 
ID   SODM_GEOSE              Reviewed;         204 AA.
AC   P00449;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JAN-2019, entry version 103.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2407726; DOI=10.1128/jb.172.3.1539-1546.1990;
RA   Bowler C., van Kaer L., van Camp W., van Montagu M., Inze D.,
RA   Dhaese P.;
RT   "Characterization of the Bacillus stearothermophilus manganese
RT   superoxide dismutase gene and its ability to complement copper/zinc
RT   superoxide dismutase deficiency in Saccharomyces cerevisiae.";
RL   J. Bacteriol. 172:1539-1546(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Brehm J.K., Chambers S.P., Bown K.J., Atkinson T., Minton N.P.;
RL   Submitted (DEC-1991) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 2-204.
RX   PubMed=7397109; DOI=10.1021/bi00554a009;
RA   Brock C.J., Walker J.E.;
RT   "Superoxide dismutase from Bacillus stearothermophilus. Complete amino
RT   acid sequence of a manganese enzyme.";
RL   Biochemistry 19:2873-2882(1980).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-204.
RX   PubMed=7202415; DOI=10.1111/j.1432-1033.1981.tb05071.x;
RA   Auffret A.D., Blake T.J., Williams D.H.;
RT   "Mass spectrometric sequence studies of a superoxide dismutase from
RT   Bacillus stearothermophilus.";
RL   Eur. J. Biochem. 113:333-338(1981).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-61.
RX   PubMed=1089067; DOI=10.1016/0014-5793(75)80793-9;
RA   Bridgen J., Harris J.I., Northrop F.;
RT   "Evolutionary relationships in superoxide dismutase.";
RL   FEBS Lett. 49:392-395(1975).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX   PubMed=3351946; DOI=10.1016/0022-2836(88)90308-7;
RA   Parker M.W., Blake C.C.F.;
RT   "Crystal structure of manganese superoxide dismutase from Bacillus
RT   stearothermophilus at 2.4-A resolution.";
RL   J. Mol. Biol. 199:649-661(1988).
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;
CC       Note=Binds 1 Mn(2+) ion per subunit.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; M26646; AAA22600.1; -; Genomic_DNA.
DR   EMBL; M81914; AAA22767.1; -; Genomic_DNA.
DR   EMBL; M81188; AAA22765.1; -; Genomic_DNA.
DR   PIR; A35134; DSBSNF.
DR   RefSeq; WP_033010224.1; NZ_RCTK01000030.1.
DR   ProteinModelPortal; P00449; -.
DR   SMR; P00449; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Manganese; Metal-binding; Oxidoreductase;
KW   Phosphoprotein.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:1089067,
FT                                ECO:0000269|PubMed:7202415,
FT                                ECO:0000269|PubMed:7397109}.
FT   CHAIN         2    204       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160018.
FT   METAL        27     27       Manganese.
FT   METAL        82     82       Manganese.
FT   METAL       164    164       Manganese.
FT   METAL       168    168       Manganese.
FT   MOD_RES      34     34       Phosphothreonine. {ECO:0000250}.
FT   MOD_RES      70     70       Phosphothreonine. {ECO:0000250}.
FT   CONFLICT     58     58       L -> P (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    122    122       A -> G (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
SQ   SEQUENCE   204 AA;  22862 MW;  7DC976C3AD2C86F7 CRC64;
     MPFELPALPY PYDALEPHID KETMNIHHTK HHNTYVTNLN AALEGHPDLQ NKSLEELLSN
     LEALPESIRT AVRNNGGGHA NHSLFWTILS PNGGGEPTGE LADAINKKFG SFTAFKDEFS
     KAAAGRFGSG WAWLVVNNGE LEITSTPNQD SPIMEGKTPI LGLDVWEHAY YLKYQNRRPE
     YIAAFWNVVN WDEVAKRYSE AKAK
//
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