ID A0A2G5EW51_AQUCA Unreviewed; 171 AA.
AC A0A2G5EW51;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
GN ORFNames=AQUCO_00400672v1 {ECO:0000313|EMBL:PIA59954.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA59954.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA59954.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000256|ARBA:ARBA00010457}.
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DR EMBL; KZ305021; PIA59954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5EW51; -.
DR STRING; 218851.A0A2G5EW51; -.
DR InParanoid; A0A2G5EW51; -.
DR OrthoDB; 3470597at2759; -.
DR Proteomes; UP000230069; Unassembled WGS sequence.
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:SF31; SUPEROXIDE DISMUTASE [CU-ZN] 3; 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.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000230069};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 25..157
FT /note="Superoxide dismutase copper/zinc binding"
FT /evidence="ECO:0000259|Pfam:PF00080"
SQ SEQUENCE 171 AA; 17608 MW; 44238A67168954FD CRC64;
MATASSTTST TTIKAVAVIN GANDVKGSLQ FLQLPNGFTQ VKGKITGLSP GLHGFHIHAL
GDTTNGCNST GPHFNPLKKN HGDPLSQERH AGDLGNIIAG PNGIAEVSVM DTQIPLSGQH
SILGRAVVVH ADPDDLGRGG HELSKTTGNA GARIGCGRES LGFSHLSSCE W
//
