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Database: UniProt/TrEMBL
Entry: A0A0H3F3H9_RAHSY
LinkDB: A0A0H3F3H9_RAHSY
Original site: A0A0H3F3H9_RAHSY 
ID   A0A0H3F3H9_RAHSY        Unreviewed;       206 AA.
AC   A0A0H3F3H9;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   25-OCT-2017, entry version 12.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Rahaq_0042 {ECO:0000313|EMBL:ADW71675.1};
OS   Rahnella sp. (strain Y9602).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Rahnella.
OX   NCBI_TaxID=741091 {ECO:0000313|EMBL:ADW71675.1, ECO:0000313|Proteomes:UP000007257};
RN   [1] {ECO:0000313|Proteomes:UP000007257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y9602 {ECO:0000313|Proteomes:UP000007257};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Sobecky P.A.,
RA   Martinez R.J., Woyke T.;
RT   "Complete sequence of chromosome of Rahnella sp. Y9602.";
RL   Submitted (JAN-2011) 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; CP002505; ADW71675.1; -; Genomic_DNA.
DR   ProteinModelPortal; A0A0H3F3H9; -.
DR   STRING; 741091.Rahaq_0042; -.
DR   EnsemblBacteria; ADW71675; ADW71675; Rahaq_0042.
DR   KEGG; rah:Rahaq_0042; -.
DR   KO; K04564; -.
DR   OMA; DSPLMHG; -.
DR   Proteomes; UP000007257; 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:UP000007257};
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;  22876 MW;  4706DAFECB88B7AB CRC64;
     MSYSLPSLPY AYDALEPHFD KETMEIHHTK HHQAYVNNAN AALESLPELA ALPVEELITK
     LDQVPADKKV ALRNNAGGHA NHSLFWKGLK TGTTLQGELK SAIERDFGSV DAFKETFEKA
     ATTRFGSGWA WLVLKDGKLA VVSTANQDSP LMGEAISGAS GYPLLGLDVW EHAYYLKYQN
     KRPDYIKAFW AVVNWDEAAK RLAEAK
//
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