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Database: UniProt
Entry: A0A0L7TCT1_9GAMM
LinkDB: A0A0L7TCT1_9GAMM
Original site: A0A0L7TCT1_9GAMM 
ID   A0A0L7TCT1_9GAMM        Unreviewed;       205 AA.
AC   A0A0L7TCT1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   28-MAR-2018, entry version 12.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=NG42_04380 {ECO:0000313|EMBL:KOC91494.1}, NG43_11255
GN   {ECO:0000313|EMBL:KOC93172.1};
OS   Erwinia iniecta.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=1560201 {ECO:0000313|EMBL:KOC93172.1, ECO:0000313|Proteomes:UP000036851};
RN   [1] {ECO:0000313|EMBL:KOC93172.1, ECO:0000313|Proteomes:UP000036851, ECO:0000313|Proteomes:UP000037088}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B120 {ECO:0000313|EMBL:KOC91494.1,
RC   ECO:0000313|Proteomes:UP000037088}, and B149
RC   {ECO:0000313|EMBL:KOC93172.1, ECO:0000313|Proteomes:UP000036851};
RX   PubMed=26198254;
RA   Campillo T., Luna E., Portier P., Fischer-Le Saux M., Lapitan N.,
RA   Tisserat N.A., Leach J.E.;
RT   "Erwinia iniecta sp. nov., isolated from Russian wheat aphids
RT   (Diuraphis noxia).";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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:KOC93172.1}.
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DR   EMBL; JRXE01000005; KOC91494.1; -; Genomic_DNA.
DR   EMBL; JRXF01000016; KOC93172.1; -; Genomic_DNA.
DR   RefSeq; WP_052898057.1; NZ_JRXF01000016.1.
DR   EnsemblBacteria; KOC91494; KOC91494; NG42_04380.
DR   EnsemblBacteria; KOC93172; KOC93172; NG43_11255.
DR   PATRIC; fig|1560201.3.peg.945; -.
DR   Proteomes; UP000036851; Unassembled WGS sequence.
DR   Proteomes; UP000037088; 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:UP000036851,
KW   ECO:0000313|Proteomes:UP000037088};
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:UP000037088}.
FT   DOMAIN        2     88       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       95    200       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        81     81       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       167    167       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       171    171       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   205 AA;  22798 MW;  DE82C4311DDADC58 CRC64;
     MSYSLPSLPY AYDALEPHFD KQTMEIHHTK HHQTYVNNAN AALEGTEFAD LPVDELITKL
     DQVPADKKTV LRNNAGGHSN HSFFWKGLKT GTTLQGDLKA AIEKDFGSVD AFKAEFEKAA
     ATRFGSGWAW LVKKGDKLAV VSTANQDSPL MGEAISGVSG FPIVGLDVWE HAYYLKYQNK
     RPDYIKAFWE VVNWDEAAAR FASAK
//
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