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Database: UniProt
Entry: P80293
LinkDB: P80293
Original site: P80293 
ID   SODM_PROFR              Reviewed;         201 AA.
AC   P80293;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   05-DEC-2018, entry version 95.
DE   RecName: Full=Superoxide dismutase [Mn/Fe];
DE            EC=1.15.1.1;
GN   Name=sodA;
OS   Propionibacterium freudenreichii subsp. shermanii.
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Propionibacterium.
OX   NCBI_TaxID=1752;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=PZ3;
RX   PubMed=8307013; DOI=10.1111/j.1432-1033.1994.tb19960.x;
RA   Meier B., Sehn A.P., Schinina M.E., Barra D.;
RT   "In vivo incorporation of copper into the iron-exchangeable and
RT   manganese-exchangeable superoxide dismutase from Propionibacterium
RT   shermanii. Amino acid sequence and identity of the protein moieties.";
RL   Eur. J. Biochem. 219:463-468(1994).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RA   Schmidt M., Meier B., Parak F.;
RT   "X-ray structure of the cambialistic superoxide dismutase from
RT   Propionibacterium shermanii active with Fe or Mn.";
RL   J. Biol. Inorg. Chem. 1:532-541(1996).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
RA   Schmidt M., Scherk C., Iakovleva O., Nolting H.F., Meier B., Parak F.;
RL   Submitted (SEP-1997) to the PDB data bank.
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
RX   PubMed=10231372; DOI=10.1046/j.1432-1327.1999.00359.x;
RA   Schmidt M.;
RT   "Manipulating the coordination mumber of the ferric iron within the
RT   cambialistic superoxide dismutase of Propionibacterium shermanii by
RT   changing the pH-value. A crystallographic analysis.";
RL   Eur. J. Biochem. 262:117-127(1999).
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       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC       Note=Binds 1 Mn(2+) or Fe(2+) ion per subunit.;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   PIR; JC4396; JC4396.
DR   PDB; 1AR4; X-ray; 1.90 A; A/B=1-201.
DR   PDB; 1AR5; X-ray; 1.60 A; A/B=1-201.
DR   PDB; 1AVM; X-ray; 1.55 A; A/B=1-201.
DR   PDB; 1BS3; X-ray; 1.55 A; A/B=1-201.
DR   PDB; 1BSM; X-ray; 1.35 A; A/B=1-201.
DR   PDB; 1BT8; X-ray; 1.85 A; A/B=1-201.
DR   PDBsum; 1AR4; -.
DR   PDBsum; 1AR5; -.
DR   PDBsum; 1AVM; -.
DR   PDBsum; 1BS3; -.
DR   PDBsum; 1BSM; -.
DR   PDBsum; 1BT8; -.
DR   ProteinModelPortal; P80293; -.
DR   SMR; P80293; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   EvolutionaryTrace; P80293; -.
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   3D-structure; Direct protein sequencing; Iron; Manganese;
KW   Metal-binding; Oxidoreductase.
FT   CHAIN         1    201       Superoxide dismutase [Mn/Fe].
FT                                /FTId=PRO_0000160066.
FT   METAL        27     27       Manganese or iron.
FT   METAL        75     75       Manganese or iron.
FT   METAL       161    161       Manganese or iron.
FT   METAL       165    165       Manganese or iron.
FT   TURN         12     18       {ECO:0000244|PDB:1BSM}.
FT   HELIX        21     29       {ECO:0000244|PDB:1BSM}.
FT   HELIX        31     52       {ECO:0000244|PDB:1BSM}.
FT   HELIX        58     80       {ECO:0000244|PDB:1BSM}.
FT   HELIX        94    104       {ECO:0000244|PDB:1BSM}.
FT   HELIX       107    119       {ECO:0000244|PDB:1BSM}.
FT   STRAND      122    132       {ECO:0000244|PDB:1BSM}.
FT   TURN        133    136       {ECO:0000244|PDB:1BSM}.
FT   STRAND      137    144       {ECO:0000244|PDB:1BSM}.
FT   TURN        145    147       {ECO:0000244|PDB:1BSM}.
FT   STRAND      155    161       {ECO:0000244|PDB:1BSM}.
FT   HELIX       164    166       {ECO:0000244|PDB:1BSM}.
FT   HELIX       168    171       {ECO:0000244|PDB:1BSM}.
FT   HELIX       175    183       {ECO:0000244|PDB:1BSM}.
FT   HELIX       188    197       {ECO:0000244|PDB:1BSM}.
FT   TURN        198    200       {ECO:0000244|PDB:1BT8}.
SQ   SEQUENCE   201 AA;  22633 MW;  5BFEF424C7B32E00 CRC64;
     AVYTLPELPY DYSALEPYIS GEIMELHHDK HHKAYVDGAN TALDKLAEAR DKADFGAINK
     LEKDLAFNLA GHVNHSVFWK NMAPKGSAPE RPTDELGAAI DEFFGSFDNM KAQFTAAATG
     IQGSGWASLV WDPLGKRINT LQFYDHQNNL PAGSIPLLQL DMWEHAFYLQ YKNVKGDYVK
     SWWNVVNWDD VALRFSEARV A
//
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