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Database: UniProt
Entry: A0A1S3VJI2_VIGRR
LinkDB: A0A1S3VJI2_VIGRR
Original site: A0A1S3VJI2_VIGRR 
ID   A0A1S3VJI2_VIGRR        Unreviewed;       152 AA.
AC   A0A1S3VJI2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   10-APR-2019, entry version 11.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=LOC106775777 {ECO:0000313|RefSeq:XP_014518445.1};
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
OC   50 kb inversion clade; NPAAA clade; indigoferoid/millettioid clade;
OC   Phaseoleae; Vigna.
OX   NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014518445.1};
RN   [1] {ECO:0000313|Proteomes:UP000087766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. VC1973A {ECO:0000313|Proteomes:UP000087766};
RX   PubMed=25384727; DOI=10.1038/ncomms6443;
RA   Kang Y.J., Kim S.K., Kim M.Y., Lestari P., Kim K.H., Ha B.K.,
RA   Jun T.H., Hwang W.J., Lee T., Lee J., Shim S., Yoon M.Y., Jang Y.E.,
RA   Han K.S., Taeprayoon P., Yoon N., Somta P., Tanya P., Kim K.S.,
RA   Gwag J.G., Moon J.K., Lee Y.H., Park B.S., Bombarely A., Doyle J.J.,
RA   Jackson S.A., Schafleitner R., Srinives P., Varshney R.K., Lee S.H.;
RT   "Genome sequence of mungbean and insights into evolution within Vigna
RT   species.";
RL   Nat. Commun. 5:5443-5443(2014).
RN   [2] {ECO:0000313|RefSeq:XP_014518445.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014518445.1};
RG   RefSeq;
RL   Submitted (DEC-2018) to UniProtKB.
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   RefSeq; XP_014518445.1; XM_014662959.1.
DR   SMR; A0A1S3VJI2; -.
DR   GeneID; 106775777; -.
DR   KEGG; vra:106775777; -.
DR   KO; K04565; -.
DR   Proteomes; UP000087766; Genome assembly.
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:UP000087766};
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:UP000087766};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       12    148       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   152 AA;  15256 MW;  2E3EE28711158BE2 CRC64;
     MVKAVAVLGS SEGVTGTVYF SQDGNGPTTV TGTLAGLKPG HHGFHVHALG DTTNGCLSTG
     PHFNPNNKEH GAPEDENRHA GDLGNVNVGD DGTVTFSITD SQIPLTGPNS IIGRAVVVHA
     DPDDLGKGGH ELSKSTGNAG GRVACGIIGL QG
//
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