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Database: UniProt
Entry: V7AZE6_PHAVU
LinkDB: V7AZE6_PHAVU
Original site: V7AZE6_PHAVU 
ID   V7AZE6_PHAVU            Unreviewed;       239 AA.
AC   V7AZE6;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   16-JAN-2019, entry version 27.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=PHAVU_009G141600g {ECO:0000313|EMBL:ESW09611.1};
OS   Phaseolus vulgaris (Kidney bean) (French bean).
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; Phaseolus.
OX   NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW09611.1, ECO:0000313|Proteomes:UP000000226};
RN   [1] {ECO:0000313|EMBL:ESW09611.1, ECO:0000313|Proteomes:UP000000226}
RP   NUCLEOTIDE SEQUENCE.
RA   Schmutz J., McClean P., Shu S., Cregan P., Rokhsar D., Jackson S.;
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
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:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CM002296; ESW09611.1; -; Genomic_DNA.
DR   RefSeq; XP_007137617.1; XM_007137555.1.
DR   EnsemblPlants; ESW09611; ESW09611; PHAVU_009G141600g.
DR   GeneID; 18620128; -.
DR   Gramene; ESW09611; ESW09611; PHAVU_009G141600g.
DR   KEGG; pvu:PHAVU_009G141600g; -.
DR   KO; K04564; -.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000000226; 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   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000226};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000226}.
FT   DOMAIN       39    119       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      129    231       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   COILED       72     92       {ECO:0000256|SAM:Coils}.
FT   METAL        63     63       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       111    111       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       200    200       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       204    204       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   239 AA;  26575 MW;  59D6964D50C5750B CRC64;
     MAARALLTRK TLASLLRNDA NPLRVGSAVA THSRGLHVYT LPDLDYDYGA LEPAISGEIM
     QLHHQKHHQT YITNYNKALE QLQDAVAKAD SAAVVKLQAA IKFNGGGHIN HSIFWKNLAP
     VREGGGEPPK GSLGWAIDTH FGSFEALIQK VNAEGAALQG SGWVWLGLDK ELKRLVVETT
     ANQDPLVTKA PNLVPLLGID VWEHAYYLQY KNVRPDYLKN IWKVINWKYA NDVYEKETS
//
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