ID   SODF_SACS2              Reviewed;         211 AA.
AC   P80857;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sod; OrderedLocusNames=SSO0316;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9880816; DOI=10.1093/oxfordjournals.jbchem.a022258;
RA   Yamano S., Maruyama T.;
RT   "An azide-insensitive superoxide dismutase from a hyperthermophilic
RT   archaeon, Sulfolobus solfataricus.";
RL   J. Biochem. 125:186-193(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 5833 / MT-4;
RX   PubMed=11248699; DOI=10.1046/j.1432-1327.2001.02052.x;
RA   De Vendittis E., Ursby T., Rullo R., Gogliettino M.A., Masullo M.,
RA   Bocchini V.;
RT   "Phenylmethanesulfonyl fluoride inactivates an archaeal superoxide
RT   dismutase by chemical modification of a specific tyrosine residue: cloning,
RT   sequencing and expression of the gene coding for Sulfolobus solfataricus
RT   superoxide dismutase.";
RL   Eur. J. Biochem. 268:1794-1801(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-211.
RC   STRAIN=DSM 5833 / MT-4;
RX   PubMed=9428655; DOI=10.1016/s0167-4838(97)00105-2;
RA   Dello Russo A., Rullo R., Nitti G., Masullo M., Bocchini V.;
RT   "Iron superoxide dismutase from the archaeon Sulfolobus solfataricus:
RT   average hydrophobicity and amino acid weight are involved in the adaptation
RT   of proteins to extreme environments.";
RL   Biochim. Biophys. Acta 1343:23-30(1997).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH IRON IONS, AND
RP   SUBUNIT.
RX   PubMed=9931259; DOI=10.1006/jmbi.1998.2471;
RA   Ursby T., Adinolfi B.S., Al-Karadaghi S., de Vendittis E., Bocchini V.;
RT   "Iron superoxide dismutase from the archaeon Sulfolobus solfataricus:
RT   analysis of structure and thermostability.";
RL   J. Mol. Biol. 286:189-205(1999).
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=Fe cation; Xref=ChEBI:CHEBI:24875;
CC       Note=Binds 1 Fe cation per subunit.;
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9931259}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; AB012620; BAA75509.1; -; Genomic_DNA.
DR   EMBL; Y15326; CAA75583.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK40652.1; -; Genomic_DNA.
DR   PIR; E90174; E90174.
DR   RefSeq; WP_009990609.1; NC_002754.1.
DR   PDB; 1WB7; X-ray; 2.24 A; A/B=2-211.
DR   PDB; 1WB8; X-ray; 2.30 A; A/B=2-211.
DR   PDBsum; 1WB7; -.
DR   PDBsum; 1WB8; -.
DR   AlphaFoldDB; P80857; -.
DR   SMR; P80857; -.
DR   STRING; 273057.SSO0316; -.
DR   EnsemblBacteria; AAK40652; AAK40652; SSO0316.
DR   GeneID; 44129290; -.
DR   KEGG; sso:SSO0316; -.
DR   PATRIC; fig|273057.12.peg.310; -.
DR   eggNOG; arCOG04147; Archaea.
DR   HOGENOM; CLU_031625_2_2_2; -.
DR   InParanoid; P80857; -.
DR   OMA; KWGSFDK; -.
DR   PhylomeDB; P80857; -.
DR   BRENDA; 1.15.1.1; 6163.
DR   EvolutionaryTrace; P80857; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
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; Cytoplasm; Direct protein sequencing; Iron; Metal-binding;
KW   Oxidoreductase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9428655"
FT   CHAIN           2..211
FT                   /note="Superoxide dismutase [Fe]"
FT                   /id="PRO_0000160010"
FT   BINDING         34
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         85
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         171
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         175
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   TURN            19..25
FT                   /evidence="ECO:0007829|PDB:1WB7"
FT   HELIX           28..36
FT                   /evidence="ECO:0007829|PDB:1WB7"
FT   HELIX           38..57
FT                   /evidence="ECO:0007829|PDB:1WB7"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:1WB8"
FT   HELIX           68..90
FT                   /evidence="ECO:0007829|PDB:1WB7"
FT   STRAND          98..100
FT                   /evidence="ECO:0007829|PDB:1WB7"
FT   HELIX           104..114
FT                   /evidence="ECO:0007829|PDB:1WB7"
FT   HELIX           117..129
FT                   /evidence="ECO:0007829|PDB:1WB7"
FT   STRAND          133..141
FT                   /evidence="ECO:0007829|PDB:1WB7"
FT   TURN            143..145
FT                   /evidence="ECO:0007829|PDB:1WB7"
FT   STRAND          148..154
FT                   /evidence="ECO:0007829|PDB:1WB7"
FT   TURN            155..157
FT                   /evidence="ECO:0007829|PDB:1WB7"
FT   STRAND          166..171
FT                   /evidence="ECO:0007829|PDB:1WB7"
FT   HELIX           174..176
FT                   /evidence="ECO:0007829|PDB:1WB7"
FT   HELIX           178..181
FT                   /evidence="ECO:0007829|PDB:1WB7"
FT   HELIX           185..192
FT                   /evidence="ECO:0007829|PDB:1WB7"
FT   HELIX           193..195
FT                   /evidence="ECO:0007829|PDB:1WB7"
FT   HELIX           198..206
FT                   /evidence="ECO:0007829|PDB:1WB7"
SQ   SEQUENCE   211 AA;  24244 MW;  693C2C94B9A3D630 CRC64;
     MTLQIQFKKY ELPPLPYKID ALEPYISKDI IDVHYNGHHK GYVNGANSLL ERLEKVVKGD
     LQTGQYDIQG IIRGLTFNIN GHKLHALYWE NMAPSGKGGG KPGGALADLI NKQYGSFDRF
     KQVFTETANS LPGTGWAVLY YDTESGNLQI MTFENHFQNH IAEIPIILIL DEFEHAYYLQ
     YKNKRADYVN AWWNVVNWDA AEKKLQKYLT K