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Entry: SODC_SOYBN C6SZ56_SOYBN
LinkDB: SODC_SOYBN C6SZ56_SOYBN
Original site: SODC_SOYBN C6SZ56_SOYBN 
ID   SODC_SOYBN              Reviewed;         152 AA.
AC   Q7M1R5;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-OCT-2017, entry version 83.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
GN   Name=SOD1;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
OC   Phaseoleae; Glycine; Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=9648237; DOI=10.1271/bbb.62.1018;
RA   Arahira M., Nong V.H., Kadokura K., Kimura K., Udaka K., Fukazawa C.;
RT   "Molecular cloning and expression patterns of Cu/Zn-superoxide
RT   dismutases in developing soybean seeds.";
RL   Biosci. Biotechnol. Biochem. 62:1018-1021(1998).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
DR   PIR; JW0084; JW0084.
DR   RefSeq; NP_001235298.1; NM_001248369.1.
DR   UniGene; Gma.54770; -.
DR   ProteinModelPortal; Q7M1R5; -.
DR   SMR; Q7M1R5; -.
DR   STRING; 3847.GLYMA19G42890.1; -.
DR   EnsemblPlants; GLYMA19G42890.1; GLYMA19G42890.1; GLYMA19G42890.
DR   EnsemblPlants; GLYMA19G42890.2; GLYMA19G42890.2; GLYMA19G42890.
DR   GeneID; 100499991; -.
DR   Gramene; GLYMA19G42890.1; GLYMA19G42890.1; GLYMA19G42890.
DR   Gramene; GLYMA19G42890.2; GLYMA19G42890.2; GLYMA19G42890.
DR   KEGG; gmx:100499991; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   InParanoid; Q7M1R5; -.
DR   KO; K04565; -.
DR   OMA; HIHEATE; -.
DR   OrthoDB; EOG09360P4O; -.
DR   Proteomes; UP000008827; Chromosome 19.
DR   Genevisible; Q7M1R5; GM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
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   Antioxidant; Complete proteome; Copper; Cytoplasm; Disulfide bond;
KW   Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN         1    152       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164156.
FT   METAL        45     45       Copper; catalytic. {ECO:0000250}.
FT   METAL        47     47       Copper; catalytic. {ECO:0000250}.
FT   METAL        62     62       Copper; catalytic. {ECO:0000250}.
FT   METAL        62     62       Zinc; structural. {ECO:0000250}.
FT   METAL        70     70       Zinc; structural. {ECO:0000250}.
FT   METAL        79     79       Zinc; structural. {ECO:0000250}.
FT   METAL        82     82       Zinc; structural. {ECO:0000250}.
FT   METAL       119    119       Copper; catalytic. {ECO:0000250}.
FT   DISULFID     56    145       {ECO:0000250}.
SQ   SEQUENCE   152 AA;  15194 MW;  DD3CF5B167C4C782 CRC64;
     MVKAVAVLGS SEGVTGTIFF TQEGNGPTTV TGSLAGLKPG LHGFHVHALG DTTNGCLSTG
     AHFNPNNNEH GAPEDENRHA GDLGNVNVGD DGTVSFSITD SQIPLTGPNS IIGRAVVVHA
     DSDDLGKGGH ELSKTTGNAG GRVACGIIGL QG
//
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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (4)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (7)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (19)   

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ID   C6SZ56_SOYBN            Unreviewed;       152 AA.
AC   C6SZ56;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   25-OCT-2017, entry version 57.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=GLYMA_19G240400 {ECO:0000313|EMBL:KRG96907.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
OC   Phaseoleae; Glycine; Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:ACU14529.1};
RN   [1] {ECO:0000313|EMBL:ACU14529.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Cheung F., Xiao Y., Chan A., Moskal W., Town C.D.;
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRG96907.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRG96907.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U.,
RA   May G.D., Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K.,
RA   Sandhu D., Valliyodan B., Lindquist E., Peto M., Grant D., Shu S.,
RA   Goodstein D., Barry K., Futrell-Griggs M., Abernathy B., Du J.,
RA   Tian Z., Zhu L., Gill N., Joshi T., Libault M., Sethuraman A.,
RA   Zhang X.-C., Shinozaki K., Nguyen H.T., Wing R.A., Cregan P.,
RA   Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.C.,
RA   Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [3] {ECO:0000313|EMBL:KRG96907.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRG96907.1};
RA   Hoefler B.C., Straight P.D.;
RL   Submitted (JUN-2015) 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:RU000393}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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; BT090454; ACU14529.1; -; mRNA.
DR   EMBL; CM000852; KRG96907.1; -; Genomic_DNA.
DR   EMBL; CM000852; KRG96908.1; -; Genomic_DNA.
DR   RefSeq; NP_001235298.1; NM_001248369.1.
DR   UniGene; Gma.54770; -.
DR   GeneID; 100499991; -.
DR   KEGG; gmx:100499991; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   KO; K04565; -.
DR   OMA; HIHEATE; -.
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   2: Evidence at transcript level;
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       12    148       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   152 AA;  15194 MW;  DD3CF5B167C4C782 CRC64;
     MVKAVAVLGS SEGVTGTIFF TQEGNGPTTV TGSLAGLKPG LHGFHVHALG DTTNGCLSTG
     AHFNPNNNEH GAPEDENRHA GDLGNVNVGD DGTVSFSITD SQIPLTGPNS IIGRAVVVHA
     DSDDLGKGGH ELSKTTGNAG GRVACGIIGL QG
//
  All links  
Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (4)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (7)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (18)   

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