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Database: UniProt/TrEMBL
Entry: A0A0U4I0F5_9ENTR
LinkDB: A0A0U4I0F5_9ENTR
Original site: A0A0U4I0F5_9ENTR 
ID   A0A0U4I0F5_9ENTR        Unreviewed;       206 AA.
AC   A0A0U4I0F5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   25-OCT-2017, entry version 10.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=AFK66_019175 {ECO:0000313|EMBL:ALX80630.1};
OS   Cronobacter malonaticus LMG 23826.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=1159491 {ECO:0000313|EMBL:ALX80630.1};
RN   [1] {ECO:0000313|Proteomes:UP000065564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 23826 {ECO:0000313|Proteomes:UP000065564};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000065564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 23826 {ECO:0000313|Proteomes:UP000065564};
RA   Descombes P., Baert L., Ngom-Bru C., Barretto C.;
RT   "Cronobacter genome sequencing and assembly.";
RL   Submitted (JAN-2016) 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: 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}.
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DR   EMBL; CP013940; ALX80630.1; -; Genomic_DNA.
DR   RefSeq; WP_015387089.1; NZ_CP013940.1.
DR   EnsemblBacteria; ALX80630; ALX80630; AFK66_019175.
DR   GeneID; 29457752; -.
DR   KEGG; cmj:AFK66_019175; -.
DR   PATRIC; fig|290339.8.peg.3415; -.
DR   KO; K04564; -.
DR   Proteomes; UP000065564; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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:UP000065564};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        2     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    201       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        82     82       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       172    172       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   206 AA;  23163 MW;  42689D1108A43522 CRC64;
     MSYTLPSLPY AYDALEPHFD KQTMEIHHTK HHQTYVNNAN AALESLPELA NLPVEELITK
     LDQVPADKKT VLRNNAGGHA NHSLFWKGLK KGTTLQGDLK AAIERDFGSV EKFKEEFEKA
     AATRFGSGWA WLVLKGDKLA VVSTANQDSP LMGEAISGAS GYPILGLDVW EHAYYLKFQN
     RRPDYIKEFW NVVNWDEAAA RFASQK
//
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