ID   G7VBY8_9CREN            Unreviewed;       211 AA.
AC   G7VBY8;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
GN   ORFNames=P186_1051 {ECO:0000313|EMBL:AET32488.1};
OS   Pyrobaculum ferrireducens.
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=1104324 {ECO:0000313|EMBL:AET32488.1, ECO:0000313|Proteomes:UP000005867};
RN   [1] {ECO:0000313|EMBL:AET32488.1, ECO:0000313|Proteomes:UP000005867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1860 {ECO:0000313|EMBL:AET32488.1,
RC   ECO:0000313|Proteomes:UP000005867};
RX   PubMed=22247528; DOI=10.1128/JB.06465-11;
RA   Mardanov A.V., Gumerov V.M., Slobodkina G.B., Beletsky A.V.,
RA   Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT   "Complete genome sequence of strain 1860, a crenarchaeon of the genus
RT   pyrobaculum able to grow with various electron acceptors.";
RL   J. Bacteriol. 194:727-728(2012).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
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         Evidence={ECO:0000256|RuleBase:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CP003098; AET32488.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7VBY8; -.
DR   SMR; G7VBY8; -.
DR   STRING; 1104324.P186_1051; -.
DR   KEGG; pyr:P186_1051; -.
DR   eggNOG; arCOG04147; Archaea.
DR   HOGENOM; CLU_031625_2_2_2; -.
DR   OrthoDB; 32917at2157; -.
DR   BioCyc; PSP1104324:GJSN-1027-MONOMER; -.
DR   Proteomes; UP000005867; Chromosome.
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; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 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   PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR   PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1.
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; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000349-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN          6..87
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          97..198
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         31
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         79
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         165
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         169
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   211 AA;  24170 MW;  D4CF085820859A9D CRC64;
     MVTVKKYTLP ELPYAYNALE PYIAEEIMKL HHQKHHQGYV NGANAALEKL EKFRKGEAQI
     DIRAVLRDFS FHLNGHVLHS IFWPNMAPPG KGGGKPGGKT ADLINQFFGS FEKFKEEFSQ
     AAKNVEGVGW AILVYEPLAE QLVILQVEKH NLMHAADAQV LLALDVWEHA YYLQYKNDRG
     SYVDNWWNVV NWDDVERRLQ KALNGQIALK I
//