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Database: UniProt/TrEMBL
Entry: C6C6H2_DICP7
LinkDB: C6C6H2_DICP7
Original site: C6C6H2_DICP7 
ID   C6C6H2_DICP7            Unreviewed;       208 AA.
AC   C6C6H2;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 45.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Dd703_0072 {ECO:0000313|EMBL:ACS83891.1};
OS   Dickeya paradisiaca (strain Ech703) (Dickeya dadantii (strain
OS   Ech703)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=579405 {ECO:0000313|EMBL:ACS83891.1, ECO:0000313|Proteomes:UP000002734};
RN   [1] {ECO:0000313|EMBL:ACS83891.1, ECO:0000313|Proteomes:UP000002734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ech703 {ECO:0000313|EMBL:ACS83891.1,
RC   ECO:0000313|Proteomes:UP000002734};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Dickeya dadantii Ech703.";
RL   Submitted (JUN-2009) 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; CP001654; ACS83891.1; -; Genomic_DNA.
DR   STRING; 579405.Dd703_0072; -.
DR   EnsemblBacteria; ACS83891; ACS83891; Dd703_0072.
DR   KEGG; dda:Dd703_0072; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; DSPLMHG; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; DDAD579405:GHJU-72-MONOMER; -.
DR   Proteomes; UP000002734; 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   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:UP000002734};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:ACS83891.1}.
FT   DOMAIN        2     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    202       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       169    169       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       173    173       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   208 AA;  23129 MW;  BDC2FA0768B6C08C CRC64;
     MSYSLPSLPY AYDALEPHFD KQTMEIHHTK HHQAYVNNAN AALESLPEFA SLSAEELITK
     LDQLPADKKG PLRNNAGGHA NHSLFWKGLK LGTTLEGELK AAIERDFGSV DAFKEKFEQA
     AATRFGSGWA WLVLKADGKL AVVSTANQDS PLMGEAISGA SGYPLVALDV WEHAYYLKYQ
     NRRPDYIKAF WSVVNWDEAA KRFAEATK
//
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