ID A0A3B3BV38_ORYME Unreviewed; 210 AA.
AC A0A3B3BV38;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN Name=SOD3 {ECO:0000313|Ensembl:ENSOMEP00000008908.1};
GN ORFNames=FQA47_020534 {ECO:0000313|EMBL:KAF6733489.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000008908.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000008908.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|EMBL:KAF6733489.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bigg-433 {ECO:0000313|EMBL:KAF6733489.1};
RX PubMed=32938378;
RA Liang P., Saqib H.S.A., Ni X., Shen Y.;
RT "Long-read sequencing and de novo genome assembly of marine medaka (Oryzias
RT melastigma).";
RL BMC Genomics 21:0-0(0).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
CC {ECO:0000256|RuleBase:RU000393}.
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:RU000393};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|RuleBase:RU000393};
CC Note=Binds 1 copper ion per subunit. {ECO:0000256|RuleBase:RU000393};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU000393};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU000393};
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000256|RuleBase:RU000393}.
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DR EMBL; WKFB01000157; KAF6733489.1; -; Genomic_DNA.
DR STRING; 30732.ENSOMEP00000008908; -.
DR PaxDb; 30732-ENSOMEP00000008908; -.
DR Ensembl; ENSOMET00000001669.1; ENSOMEP00000008908.1; ENSOMEG00000010084.1.
DR GeneTree; ENSGT00940000162224; -.
DR OMA; DGSLWKY; -.
DR OrthoDB; 3470597at2759; -.
DR Proteomes; UP000261560; Unplaced.
DR Proteomes; UP000646548; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR InterPro; IPR018152; SOD_Cu/Zn_BS.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003:SF77; EXTRACELLULAR SUPEROXIDE DISMUTASE [CU-ZN]; 1.
DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR PRINTS; PR00068; CUZNDISMTASE.
DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|RuleBase:RU000393};
KW Metal-binding {ECO:0000256|RuleBase:RU000393};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW Reference proteome {ECO:0000313|Proteomes:UP000646548};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|RuleBase:RU000393}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..210
FT /note="Superoxide dismutase [Cu-Zn]"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040589886"
FT DOMAIN 62..193
FT /note="Superoxide dismutase copper/zinc binding"
FT /evidence="ECO:0000259|Pfam:PF00080"
SQ SEQUENCE 210 AA; 22625 MW; FE9C6501A12F0364 CRC64;
MRAHRSVSVL KVALLVWLAC SQQCSSTYTD FLPPEFSQHN GTLYAACKVR PSAPLADDLP
NVSGQVLFKQ DQAEGKLQVL LQLSGFPTNE PSQPRAVHIH QYGDLSQGCT STGGHYNPYG
VHHPNHPGDF GNFVANAGRI SDRIESEATL FGGLSVLGRA VVVHETVDDL GQGGDAGSLM
HGNAGRRLAC CVIGMCSSNL WDEELNTRRK
//
