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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