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Database: UniProt
Entry: A4WG88_ENT38
LinkDB: A4WG88_ENT38
Original site: A4WG88_ENT38 
ID   A4WG88_ENT38            Unreviewed;       206 AA.
AC   A4WG88;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   18-JUL-2018, entry version 67.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Ent638_4063 {ECO:0000313|EMBL:ABP62718.1};
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742 {ECO:0000313|EMBL:ABP62718.1, ECO:0000313|Proteomes:UP000000230};
RN   [1] {ECO:0000313|Proteomes:UP000000230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638 {ECO:0000313|Proteomes:UP000000230};
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP62718.1; -; Genomic_DNA.
DR   RefSeq; WP_015961022.1; NC_009436.1.
DR   STRING; 399742.Ent638_4063; -.
DR   EnsemblBacteria; ABP62718; ABP62718; Ent638_4063.
DR   GeneID; 32444070; -.
DR   KEGG; ent:Ent638_4063; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   BioCyc; ESP399742:GJ0E-4131-MONOMER; -.
DR   Proteomes; UP000000230; Chromosome.
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:UP000000230};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:ABP62718.1}.
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;  22941 MW;  5EBD921337E805F3 CRC64;
     MSYTLPSLPY AYDALEPHFD KQTMEIHHTK HHQAYVNNAN AALESLPEFA ELSVEELITK
     LDQLPADKKT VLRNNAGGHA NHSLFWKGLK TGTTLQGDLK AAIERDFGSV DAFKAEFEKA
     AATRFGSGWA WLVLKGDKLA VVSTANQDSP LMGEAVSGVS GFPIVGLDVW EHAYYLKFQN
     RRPDYIKAFW DVVNWDEAAA RFAAKK
//
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