SODC_ASPNG
ID SODC_ASPNG Reviewed; 154 AA.
AC P85978;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000303|PubMed:18395490};
DE EC=1.15.1.1 {ECO:0000269|PubMed:18395490};
GN Name=sodC {ECO:0000250|UniProtKB:Q9Y8D9};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-154, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND MASS SPECTROMETRY.
RC STRAIN=26 {ECO:0000269|PubMed:18395490};
RX PubMed=18395490; DOI=10.1016/j.saa.2008.02.023;
RA Dolashki A., Abrashev R., Stevanovic S., Stefanova L., Ali S.A.,
RA Velkova L., Hristova R., Angelova M., Voelter W., Devreese B.,
RA Van Beeumen J., Dolashka-Angelova P.;
RT "Biochemical properties of Cu/Zn-superoxide dismutase from fungal strain
RT Aspergillus niger 26.";
RL Spectrochim. Acta A Mol. Biomol. Spectrosc. 71:975-983(2008).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
CC {ECO:0000250|UniProtKB:P00442}.
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:0000269|PubMed:18395490};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P00442};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P00442};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00442};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00442};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Retains over 90% of its activity between pH 5.6 and 7.0. Retains 85%
CC of its activity at pH 4.0 and 60% of its activity at pH 12.0.
CC {ECO:0000269|PubMed:18395490};
CC Temperature dependence:
CC Full activity is retained between 25 and 45 degrees Celsius.
CC {ECO:0000269|PubMed:18395490};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18395490}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00442}.
CC -!- MASS SPECTROMETRY: Mass=15821; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18395490};
CC -!- MASS SPECTROMETRY: Mass=15824; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18395490};
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000255}.
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DR AlphaFoldDB; P85978; -.
DR SMR; P85978; -.
DR STRING; 5061.CADANGAP00005537; -.
DR VEuPathDB; FungiDB:An07g03770; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1143951; -.
DR VEuPathDB; FungiDB:ATCC64974_45950; -.
DR VEuPathDB; FungiDB:M747DRAFT_138609; -.
DR eggNOG; KOG0441; Eukaryota.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW Antioxidant; Copper; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Metal-binding; Oxidoreductase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18395490"
FT CHAIN 2..154
FT /note="Superoxide dismutase [Cu-Zn]"
FT /evidence="ECO:0000269|PubMed:18395490"
FT /id="PRO_0000355101"
FT REGION 125..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT BINDING 49
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT BINDING 64
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT BINDING 121
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT DISULFID 58..147
FT /evidence="ECO:0000250|UniProtKB:P00442"
SQ SEQUENCE 154 AA; 15976 MW; 36967A7C19FB44D5 CRC64;
MVKAVAVIRG DSKVSGTVTF EQANENTPTT ISWNITGHDA NAERGFHVHQ FGDNTNGCTS
AGPHFNPYGK THGAPEDDER HVGDLGNFKT DAEGNAVGSK QDKLVKLIGA ESVLGRTLVV
HAGTDDLGRG GNEESKKTGN AGPRPACGVI GIAA
