SODC_NPVOP
ID SODC_NPVOP Reviewed; 152 AA.
AC O12933;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Putative superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
GN Name=SOD; ORFNames=ORF29;
OS Orgyia pseudotsugata multicapsid polyhedrosis virus (OpMNPV).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX NCBI_TaxID=262177;
OH NCBI_TaxID=33414; Orgyia pseudotsugata (Douglas-fir tussock moth).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9126251; DOI=10.1006/viro.1997.8448;
RA Ahrens C.H., Russell R.R., Funk C.J., Evans J., Harwood S., Rohrmann G.F.;
RT "The sequence of the Orgyia pseudotsugata multinucleocapsid nuclear
RT polyhedrosis virus genome.";
RL Virology 229:381-399(1997).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
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 -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; U75930; AAC59028.1; -; Genomic_DNA.
DR RefSeq; NP_046185.1; NC_001875.2.
DR SMR; O12933; -.
DR GeneID; 912048; -.
DR KEGG; vg:912048; -.
DR Proteomes; UP000009248; Genome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; -; 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; PTHR10003; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR PRINTS; PR00068; CUZNDISMTASE.
DR SUPFAM; SSF49329; SSF49329; 1.
DR PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant; Copper; Disulfide bond; Late protein; Metal-binding;
KW Oxidoreductase; Zinc.
FT CHAIN 1..152
FT /note="Putative superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000164163"
FT BINDING 43
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 54..144
FT /evidence="ECO:0000250"
SQ SEQUENCE 152 AA; 15855 MW; 2B778743FFB47BB0 CRC64;
MKAICIVAGE ASGRIYFKQG APDEPVSITG YLLNLPRGLH GFHVHEFGDT SNGCTSAGEH
FNPTRQRHGA PDAAERHVGD LGNVRSAGCT ALTAIHMSDN VITLFGPLSI LGRSLVVHTD
RDDLGLGEHP LSKTTGNSGG RLGCGIIGVC AN
