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Database: UniProt
Entry: A0A0K8NTL2_IDESA
LinkDB: A0A0K8NTL2_IDESA
Original site: A0A0K8NTL2_IDESA 
ID   A0A0K8NTL2_IDESA        Unreviewed;       193 AA.
AC   A0A0K8NTL2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   16-JAN-2019, entry version 15.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=ISF6_0134 {ECO:0000313|EMBL:GAP33688.1};
OS   Ideonella sakaiensis (strain 201-F6).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Ideonella.
OX   NCBI_TaxID=1547922 {ECO:0000313|EMBL:GAP33688.1, ECO:0000313|Proteomes:UP000037660};
RN   [1] {ECO:0000313|Proteomes:UP000037660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=201-F6 {ECO:0000313|Proteomes:UP000037660};
RA   Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA   Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT   "Discovery of a poly(ethylene terephthalate assimilation.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAP33688.1, ECO:0000313|Proteomes:UP000037660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=201-F6 {ECO:0000313|EMBL:GAP33688.1,
RC   ECO:0000313|Proteomes:UP000037660};
RX   PubMed=26965627; DOI=10.1126/science.aad6359;
RA   Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA   Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT   "A bacterium that degrades and assimilates poly(ethylene
RT   terephthalate).";
RL   Science 351:1196-1199(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:GAP33688.1}.
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DR   EMBL; BBYR01000001; GAP33688.1; -; Genomic_DNA.
DR   RefSeq; WP_054017849.1; NZ_BBYR01000001.1.
DR   EnsemblBacteria; GAP33688; GAP33688; ISF6_0134.
DR   OrthoDB; 1440645at2; -.
DR   Proteomes; UP000037660; Unassembled WGS sequence.
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   Complete proteome {ECO:0000313|Proteomes:UP000037660};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:GAP33688.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037660}.
FT   DOMAIN        2     82       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       89    190       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        74     74       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       157    157       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   193 AA;  21353 MW;  BFCD83BF57B4A4D5 CRC64;
     MEHTLPPLPY AHDALAPHLS KETLEFHHDK HHNAYVVNLN NLQKGTEFEA MDLETIVKKS
     SGGIYNNAAQ IWNHTFFWHC MAPNGGGAPK GALAAAIDAK WGSYAAFKEA FSKSAVGNFG
     SGWTWLVKKA DGSVDIVNMG AAGTPLTTGD TPLLTIDVWE HAYYIDYRNL RPKFVETFLN
     ALVNWDFAEK NFG
//
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