SODM_GEOSE
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 03-AUG-2022, entry version 113.
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., Dhaese P.;
RT "Characterization of the Bacillus stearothermophilus manganese superoxide
RT dismutase gene and its ability to complement copper/zinc superoxide
RT 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 acid
RT 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 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 family.
CC {ECO:0000305}.
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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 PDB; 6PRO; X-ray; 2.26 A; A/B=2-203.
DR PDBsum; 6PRO; -.
DR AlphaFoldDB; P00449; -.
DR SMR; P00449; -.
DR GeneID; 58573934; -.
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; Direct protein sequencing; Manganese; Metal-binding;
KW Oxidoreductase; Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1089067,
FT ECO:0000269|PubMed:7202415, ECO:0000269|PubMed:7397109"
FT CHAIN 2..204
FT /note="Superoxide dismutase [Mn]"
FT /id="PRO_0000160018"
FT BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 164
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 168
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT CONFLICT 58
FT /note="L -> P (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="A -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 12..18
FT /evidence="ECO:0007829|PDB:6PRO"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:6PRO"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:6PRO"
FT TURN 47..51
FT /evidence="ECO:0007829|PDB:6PRO"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:6PRO"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:6PRO"
FT HELIX 66..87
FT /evidence="ECO:0007829|PDB:6PRO"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:6PRO"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:6PRO"
FT STRAND 128..137
FT /evidence="ECO:0007829|PDB:6PRO"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:6PRO"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:6PRO"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:6PRO"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:6PRO"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:6PRO"
FT HELIX 178..185
FT /evidence="ECO:0007829|PDB:6PRO"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:6PRO"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:6PRO"
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
