ID   SODF_ACIAM              Reviewed;         211 AA.
AC   Q9P9L3;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sod;
OS   Acidianus ambivalens (Desulfurolobus ambivalens).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Acidianus.
OX   NCBI_TaxID=2283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11154067; DOI=10.1515/bc.2000.134;
RA   Kardinahl S., Anemuller S., Schaefer G.;
RT   "The hyper-thermostable Fe-superoxide dismutase from the Archaeon Acidianus
RT   ambivalens: characterization, recombinant expression, crystallization and
RT   effects of metal exchange.";
RL   Biol. Chem. 381:1089-1101(2000).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological systems.
CC       {ECO:0000250}.
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; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; AF236110; AAF36989.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9P9L3; -.
DR   SMR; Q9P9L3; -.
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   3: Inferred from homology;
KW   Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..211
FT                   /note="Superoxide dismutase [Fe]"
FT                   /id="PRO_0000160004"
FT   BINDING         34
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   211 AA;  24342 MW;  5A88FFE400F77065 CRC64;
     MSSLTYLKKY ELPPLPYNLD ALEPYISKEI IDVHYNGHHR GYVNGANSFV DRVNKILKGE
     ISSGQYDIQG LLRGLVFNIN GHKLHSLYWQ NMAPAGKGGG KPGGVIGDLI EKQYGSFEKF
     KALFTEAANS LPGTGWTVLY YEVENGNLQI MTFENHFQNH IAELPILLIL DEFEHAYYLQ
     YKNKRADYVN NWWNLVNWDF ADKKLQQYMK K