ID Q6UTE6_XENLA Unreviewed; 224 AA.
AC Q6UTE6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 91.
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 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
//