ID   Q6UTE6_XENLA            Unreviewed;       224 AA.
AC   Q6UTE6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sod2.L {ECO:0000313|Xenbase:XB-GENE-1000995};
GN   Synonyms=sod2 {ECO:0000313|Xenbase:XB-GENE-1000995};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAQ63483.1};
RN   [1] {ECO:0000313|EMBL:AAQ63483.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Di Pietro C., Di Pietro V., Emmanuele G., Ferro A., Maugeri T., Modica E.,
RA   Pigola G., Pulvirenti A., Purrello M., Ragusa M., Scalia M., Shasha D.,
RA   Travali S., Zimmitti V.;
RT   "ANTICLUSTAL: multiple sequence alignment by antipole clustering and linear
RT   approximate 1-median computation.";
RL   (In) Unknown A. (eds.);
RL   IEEE COMPUTER SOCIETY BIOINFORMATICS CONFERENCE, pp.0-0, Unknown Publisher
RL   (2003).
RN   [2] {ECO:0000313|EMBL:AAQ63483.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15699630; DOI=10.1089/dna.2005.24.111;
RA   Purrello M., Di Pietro C., Ragusa M., Pulvirenti A., Giugno R.,
RA   Pietro V.D., Emmanuele G., Travali S., Scalia M., Shasha D., Ferro A.;
RT   "In vitro and in silico cloning of Xenopus laevis SOD2 cDNA and its
RT   phylogenetic analysis.";
RL   DNA Cell Biol. 24:111-116(2005).
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   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological systems.
CC       {ECO:0000256|ARBA:ARBA00002170}.
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|ARBA:ARBA00001605,
CC         ECO:0000256|RuleBase:RU000414};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
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; AY362041; AAQ63483.1; -; mRNA.
DR   RefSeq; NP_001083968.1; NM_001090499.1.
DR   AlphaFoldDB; Q6UTE6; -.
DR   GeneID; 399216; -.
DR   Xenbase; XB-GENE-1000995; sod2.L.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000349-1};
KW   Nitration {ECO:0000256|ARBA:ARBA00023074};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000414};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          27..108
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          115..218
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         52
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         100
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         185
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         189
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   224 AA;  25166 MW;  BC89B2B91BA61323 CRC64;
     MLCRLSVCGR GRMRCVPALA YSFCKEKHTL PDLPYDYGAL QPHISAEIMQ LHHSKHHATY
     VNNLNITEEK YAEALAKGDV TTQVSLQAAL KFNGGGHINH TIFWTNLSPN GGGEPQGELL
     DAIKRDFGSF EKFKEKLNTV SVGVQGSGWG WLGYNKDSNR LQLAACANQD PLQGTTGLIP
     LLGIDVWEHA YYLQYKNVRP DYLKAIWNVI NWENVTERYQ ASKK
//