ID   F7XLC9_METZD            Unreviewed;       202 AA.
AC   F7XLC9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   04-NOV-2026, entry version 61.
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   OrderedLocusNames=Mzhil_0926 {ECO:0000313|EMBL:AEH60788.1};
OS   Methanosalsum zhilinae (strain DSM 4017 / NBRC 107636 / OCM 62 / WeN5)
OS   (Methanohalophilus zhilinae).
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanosalsum.
OX   NCBI_TaxID=679901 {ECO:0000313|EMBL:AEH60788.1, ECO:0000313|Proteomes:UP000006622};
RN   [1] {ECO:0000313|EMBL:AEH60788.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 4017 {ECO:0000313|EMBL:AEH60788.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ovchinnikova G., Daligault H., Detter J.C., Han C., Tapia R., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA   Wu D., Spring S., Schueler E., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanosalsum zhilinae DSM 4017.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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 superoxide + 2 H(+) = 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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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; CP002101; AEH60788.1; -; Genomic_DNA.
DR   RefSeq; WP_013898227.1; NC_015676.1.
DR   AlphaFoldDB; F7XLC9; -.
DR   STRING; 679901.Mzhil_0926; -.
DR   GeneID; 10822548; -.
DR   KEGG; mzh:Mzhil_0926; -.
DR   HOGENOM; CLU_031625_2_2_2; -.
DR   OMA; AACTGRF; -.
DR   OrthoDB; 32917at2157; -.
DR   Proteomes; UP000006622; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   FunFam; 3.55.40.20:FF:000004; Superoxide dismutase [Fe]; 1.
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; IPR050265; Fe/Mn_Superoxide_Dismutase.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006622}.
FT   DOMAIN          6..85
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          96..196
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         30
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         78
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         164
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         168
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   202 AA;  23921 MW;  DEB59B7E921BBF6A CRC64;
     MAKEYYKLPP LAYGYDELEP YISEEQLRLH HDKHHQSYVD NLNSIIKMVE KAREEGKDYD
     YKAATKAASF NAGGNVLHDY FWWEMMPAEK AGEEPVGELL EQIKKDFGSF ERFKKEFSQV
     ALTVEGSGWA ALTYCGDTHR LSPIQIEKHN VNVYPDYPII MVLDMWEHAY YIDYRNEKAK
     FVDGFWNIIN WEELDKHFKK YL
//