ID   SODC_PBCV1              Reviewed;         187 AA.
AC   Q90023;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   OrderedLocusNames=A245R;
OS   Paramecium bursaria Chlorella virus 1 (PBCV-1).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Algavirales; Phycodnaviridae; Chlorovirus.
OX   NCBI_TaxID=10506;
OH   NCBI_TaxID=114055; Chlorella.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7831789; DOI=10.1016/s0042-6822(95)80049-2;
RA   Lu Z., Li Y., Zhang Y., Kutish G.F., Rock D.L., van Etten J.L.;
RT   "Analysis of 45 kb of DNA located at the left end of the chlorella virus
RT   PBCV-1 genome.";
RL   Virology 206:339-352(1995).
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; JF411744; AAC96613.1; -; Genomic_DNA.
DR   PIR; T17736; T17736.
DR   RefSeq; NP_048593.1; NC_000852.5.
DR   SMR; Q90023; -.
DR   GeneID; 918416; -.
DR   KEGG; vg:918416; -.
DR   Proteomes; UP000000862; 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; Metal-binding; Oxidoreductase;
KW   Reference proteome; Signal; Zinc.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..187
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /id="PRO_0000032843"
FT   BINDING         76
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   DISULFID        87..176
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   187 AA;  19748 MW;  E12366A9274674DD CRC64;
     MSLLPTGTLI LLVLFILVLI TMTKNTSSLN VTKPVSAIAV LEGPVKGTVR FVEESSKVKI
     SVDISGLKPN RKHGFHVHEA GDLTDGCTSA CAHFNPFGTA HGGPDSKIRH VGDLGNILAD
     KNGKAKYSFY DSMIKLRGKC NIIGRAIVVH ADTDDLGLGG NAESLKTGNA GKRIGCAVIG
     YAKENFC