UniProt/TrEMBL: Q0VH22

Database: UniProt/TrEMBL
Entry: Q0VH22_BRANA

LinkDB:  Q0VH22_BRANA 
Original site:  Q0VH22_BRANA

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (7)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (2)   
All databases (15)   

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ID   Q0VH22_BRANA            Unreviewed;       152 AA.
AC   Q0VH22;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708 {ECO:0000313|EMBL:AAY40317.1};
RN   [1] {ECO:0000313|EMBL:AAY40317.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Yang Y., Li G., Yong D.;
RT   "Cloning and characterization of the Cu/Zn superoxide dismutase gene in
RT   Brassica napus.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABE28385.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Yang Y., Gan L., Ding Y.;
RT   "Cloning and characterization of Cu/Zn superoxide dismutase gene in
RT   Brassica napus.";
RL   Submitted (MAR-2006) 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|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|ARBA:ARBA00001605,
CC         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; AY970822; AAY40317.1; -; mRNA.
DR   EMBL; DQ431853; ABE28385.1; -; Genomic_DNA.
DR   RefSeq; XP_013716465.1; XM_013861011.1.
DR   AlphaFoldDB; Q0VH22; -.
DR   SMR; Q0VH22; -.
DR   EnsemblPlants; CDY06331; CDY06331; GSBRNA2T00122261001.
DR   GeneID; 106420167; -.
DR   Gramene; CDY06331; CDY06331; GSBRNA2T00122261001.
DR   KEGG; bna:106420167; -.
DR   OMA; FEWDETE; -.
DR   OrthoDB; 3470597at2759; -.
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:SF71; SUPEROXIDE DISMUTASE; 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; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   2: Evidence at transcript level;
KW   Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000393};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN          14..148
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   152 AA;  15180 MW;  2E089025B60544CE CRC64;
     MAKGVAVLNS SEGVKGTIFF TQEGDGATTV TGTVSGLKPG PHGFHVHALG DTTNGCMSTG
     PHFNPDGKTH GAPEDANRHA GDLGNIIVGD DGTATFTITD SQIPLTGPNS IVGRAVVVHA
     ERDDLGKGGH ELSLSTGNAG GRVACGIIGL QG
//

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