ID Q5JCT2_EPIML Unreviewed; 154 AA.
AC Q5JCT2;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
OS Epinephelus malabaricus (Malabar grouper) (Holocentrus malabaricus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Serranoidei; Serranidae; Epinephelinae;
OC Epinephelini; Epinephelus.
OX NCBI_TaxID=162300 {ECO:0000313|EMBL:AAK62563.1};
RN [1] {ECO:0000313|EMBL:AAK62563.1}
RP NUCLEOTIDE SEQUENCE.
RA Lin C.-T., Ken C.-F., Qian Y.-F., Weng D.-F.;
RT "Cloning and expression of Cu/Zn superoxide dismutase from grouper
RT (Epinephelus epistictus).";
RL Submitted (DEC-2016) 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|ARBA:ARBA00003917, 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|ARBA:ARBA00010457, ECO:0000256|RuleBase:RU000393}.
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DR EMBL; AY035854; AAK62563.1; -; mRNA.
DR AlphaFoldDB; Q5JCT2; -.
DR SMR; Q5JCT2; -.
DR BRENDA; 1.15.1.1; 7765.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
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:SF103; 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 2: Evidence at transcript level;
KW Copper {ECO:0000256|RuleBase:RU000393};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023139};
KW Metal-binding {ECO:0000256|RuleBase:RU000393};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Zinc {ECO:0000256|RuleBase:RU000393}.
FT DOMAIN 16..150
FT /note="Superoxide dismutase copper/zinc binding"
FT /evidence="ECO:0000259|Pfam:PF00080"
SQ SEQUENCE 154 AA; 15886 MW; 1A8D219C1DA53BC6 CRC64;
MVLKAVCVLK GAGETSGTVY FEQETDSAPV KLTGEIKGLT PGEHGFQVHA FGDNTNGCIS
AGPHFNPHNK HHAGPTDAER HVGDLGNVTA GGDNVAKIDI TDKIITLNGP YSIIGRTMVI
HEKADDLGTG GNEESLKTGN AGGRLACGVI GISQ
//
