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Database: UniProt
Entry: D3I9J9_9BACT
LinkDB: D3I9J9_9BACT
Original site: D3I9J9_9BACT 
ID   D3I9J9_9BACT            Unreviewed;       203 AA.
AC   D3I9J9;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   13-FEB-2019, entry version 38.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=HMPREF0669_00103 {ECO:0000313|EMBL:EFC71431.1};
OS   Prevotella sp. oral taxon 299 str. F0039.
OG   Plasmid unnamed {ECO:0000313|EMBL:EFC71431.1}.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=575614 {ECO:0000313|EMBL:EFC71431.1, ECO:0000313|Proteomes:UP000015929};
RN   [1] {ECO:0000313|EMBL:EFC71431.1, ECO:0000313|Proteomes:UP000015929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0039 {ECO:0000313|EMBL:EFC71431.1,
RC   ECO:0000313|Proteomes:UP000015929};
RC   PLASMID=unnamed {ECO:0000313|EMBL:EFC71431.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T.,
RA   Walk T., White J., Yandava C., Izard J., Baranova O.V., Blanton J.M.,
RA   Tanner A.C., Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EFC71431.1, ECO:0000313|Proteomes:UP000015929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0039 {ECO:0000313|EMBL:EFC71431.1,
RC   ECO:0000313|Proteomes:UP000015929};
RC   PLASMID=Plasmid {ECO:0000313|Proteomes:UP000015929};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA   Blanton J.M., Tanner A.C., Dewhirst F.E., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J.,
RA   McCowan C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella sp. Oral Taxon 299 strain F0039.";
RL   Submitted (JUN-2012) 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:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC         Evidence={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; CP003667; EFC71431.1; -; Genomic_DNA.
DR   RefSeq; WP_009227279.1; NC_022111.1.
DR   ProteinModelPortal; D3I9J9; -.
DR   STRING; 575614.HMPREF0669_00103; -.
DR   EnsemblBacteria; EFC71431; EFC71431; HMPREF0669_00103.
DR   KEGG; pro:HMPREF0669_00103; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; GCF_000163055-HMP:HMPREF0669_RS04220-MONOMER; -.
DR   Proteomes; UP000015929; Plasmid.
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:UP000015929};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Plasmid {ECO:0000313|EMBL:EFC71431.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015929}.
FT   DOMAIN       13     91       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      100    201       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        36     36       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        84     84       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   203 AA;  22780 MW;  092197B34FEEE520 CRC64;
     MLLTKIVFMM TISMPQLPYS PNALEPVISE QTINYHYGKH LQAYVNTLGT LVQGTEFEGK
     SVDEIVMTAP DGPIFNNAGQ TLNHALYFGQ FKSPVKDNVP TGKLADEINT TFGSFDEFKK
     QFSQAGATLF GSGWVWLAQD KDGKLIITKE ANAGNPLRHG QNPLMGIDVW EHAYYLDYQN
     RRVDHLAAVW EIINWDVVAS RLK
//
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