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Database: UniProt
Entry: A0A0L9VCX3_PHAAN
LinkDB: A0A0L9VCX3_PHAAN
Original site: A0A0L9VCX3_PHAAN 
ID   A0A0L9VCX3_PHAAN        Unreviewed;       152 AA.
AC   A0A0L9VCX3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   16-JAN-2019, entry version 17.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=LR48_Vigan09g157400 {ECO:0000313|EMBL:KOM52915.1};
OS   Phaseolus angularis (Azuki bean) (Vigna angularis).
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=3914 {ECO:0000313|EMBL:KOM52915.1, ECO:0000313|Proteomes:UP000053144};
RN   [1] {ECO:0000313|Proteomes:UP000053144}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX   PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA   Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y.,
RA   Sun Y., Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C.,
RA   Ma Y., Wu B., Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W.,
RA   Li Y., Wang J., Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT   "Genome sequencing of adzuki bean (Vigna angularis) provides insight
RT   into high starch and low fat accumulation and domestication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
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; CM003379; KOM52915.1; -; Genomic_DNA.
DR   RefSeq; XP_017436006.1; XM_017580517.1.
DR   EnsemblPlants; KOM52915; KOM52915; LR48_Vigan09g157400.
DR   GeneID; 108342725; -.
DR   Gramene; KOM52915; KOM52915; LR48_Vigan09g157400.
DR   KEGG; var:108342725; -.
DR   KO; K04565; -.
DR   OrthoDB; 1574423at2759; -.
DR   Proteomes; UP000053144; Chromosome 9.
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:UP000053144};
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:UP000053144};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       12    148       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   152 AA;  15201 MW;  1FF3E95D11175308 CRC64;
     MVKAVAVLGS SEGVTGTVYF SQDGNGPTTV TGTLAGLKPG HHGFHVHALG DTTNGCLSTG
     PHFNPNSKEH GAPEDENRHA GDLGNVNVGD DGTATFSITD SQIPLTGPNS IIGRAVVVHA
     DPDDLGKGGH ELSKSTGNAG GRVACGIIGL QG
//
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