ID Q66S06_OIKDI Unreviewed; 272 AA.
AC Q66S06;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 03-MAY-2023, entry version 65.
DE RecName: Full=Superoxide dismutase [Mn], mitochondrial {ECO:0000256|ARBA:ARBA00014518};
DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
GN ORFNames=008-48 {ECO:0000313|EMBL:AAT47885.1};
OS Oikopleura dioica (Tunicate).
OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC Oikopleuridae; Oikopleura.
OX NCBI_TaxID=34765 {ECO:0000313|EMBL:AAT47885.1};
RN [1] {ECO:0000313|EMBL:AAT47885.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15343333; DOI=10.1038/nature02709;
RA Seo H.C., Edvardsen R.B., Maeland A.D., Bjordal M., Jensen M.F., Hansen A.,
RA Flaat M., Weissenbach J., Lehrach H., Wincker P., Reinhardt R.,
RA Chourrout D.;
RT "Hox cluster disintegration with persistent anteroposterior order of
RT expression in Oikopleura dioica.";
RL Nature 431:67-71(2004).
RN [2] {ECO:0000313|EMBL:AAT47885.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15649342; DOI=10.1016/j.cub.2004.12.010;
RA Edvardsen R.B., Seo H.C., Jensen M.F., Mialon A., Mikhaleva J., Bjordal M.,
RA Cartry J., Reinhardt R., Weissenbach J., Wincker P., Chourrout D.;
RT "Remodelling of the homeobox gene complement in the tunicate Oikopleura
RT dioica.";
RL Curr. Biol. 15:R12-R13(2005).
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 -!- 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}.
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DR EMBL; AY613856; AAT47885.1; -; Genomic_DNA.
DR AlphaFoldDB; Q66S06; -.
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 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 Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 75..156
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 163..266
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
SQ SEQUENCE 272 AA; 29896 MW; B8F1EBE65817072E CRC64;
MDSYVAALEA KLAEATGIKI NQMANAASEG AAISEQTDFI KNIVISDGKA QSGVRNPLIA
KVLNNIKTET SQDLKYELPK LGYEYGQLEP TICEEIMRIH HSKHHNGYVT NLNAAVEKLA
AAERAGDVNA MNQLSEAINF NGGGHINHTI FWTNMAPNGG GQPTGELADQ INNDFGSFDA
FKKEMCAKSA AVKGSGWGWL GWNKEASKLQ VATCQNQDPL EATTGLIPLL GIDVWEHAYY
IQYKNLRAQY VEKIFDVFNW TNVAERFAKA KK
//
