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Entry: C5WSP7_SORBI
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Original site: C5WSP7_SORBI 
ID   C5WSP7_SORBI            Unreviewed;       163 AA.
AC   C5WSP7;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 2.
DT   10-APR-2019, entry version 46.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=SORBI_3001G453800 {ECO:0000313|EMBL:EER95258.2};
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae;
OC   PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Sorghinae;
OC   Sorghum.
OX   NCBI_TaxID=4558 {ECO:0000313|EMBL:EER95258.2, ECO:0000313|Proteomes:UP000000768};
RN   [1] {ECO:0000313|EMBL:EER95258.2, ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=19189423; DOI=10.1038/nature07723;
RA   Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA   Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A.,
RA   Schmutz J., Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K.,
RA   Chapman J., Feltus F.A., Gowik U., Grigoriev I.V., Lyons E.,
RA   Maher C.A., Martis M., Narechania A., Otillar R.P., Penning B.W.,
RA   Salamov A.A., Wang Y., Zhang L., Carpita N.C., Freeling M.,
RA   Gingle A.R., Hash C.T., Keller B., Klein P., Kresovich S.,
RA   McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman, Ware D.,
RA   Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT   "The Sorghum bicolor genome and the diversification of grasses.";
RL   Nature 457:551-556(2009).
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|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.
CC       {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.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; CM000760; EER95258.2; -; Genomic_DNA.
DR   STRING; 4558.Sb01g042660.1; -.
DR   EnsemblPlants; EER95258; EER95258; SORBI_3001G453800.
DR   Gramene; EER95258; EER95258; SORBI_3001G453800.
DR   eggNOG; KOG1579; Eukaryota.
DR   eggNOG; COG0646; LUCA.
DR   Proteomes; UP000000768; Chromosome 1.
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   Complete proteome {ECO:0000313|Proteomes:UP000000768};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       17    157       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   163 AA;  16716 MW;  20F7AEEA73170474 CRC64;
     MAGKAGGLKG VALIGGGANS TVAGALHFFE DPSTRYTEVR GKVTGLTPGR HGFHIHVFGD
     TTNGCNSTGP HFNPHNKPHG APFDKERHAG DLGNIVANED GVAEVFIRDL QISLSGPHSI
     LGRAVVVHAD PDDLGRGGHE LSKSTGNAGA RIGCGIIGIQ SSV
//
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