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Database: UniProt
Entry: U2A9R5_9FLAO
LinkDB: U2A9R5_9FLAO
Original site: U2A9R5_9FLAO 
ID   U2A9R5_9FLAO            Unreviewed;       260 AA.
AC   U2A9R5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   16-JAN-2019, entry version 19.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=HMPREF1551_01837 {ECO:0000313|EMBL:ERI62544.1};
OS   Capnocytophaga sp. oral taxon 863 str. F0517.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=1227266 {ECO:0000313|EMBL:ERI62544.1, ECO:0000313|Proteomes:UP000016494};
RN   [1] {ECO:0000313|EMBL:ERI62544.1, ECO:0000313|Proteomes:UP000016494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0517 {ECO:0000313|EMBL:ERI62544.1,
RC   ECO:0000313|Proteomes:UP000016494};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R.,
RA   Courtney L., Fronick C., O'Laughlin M., Godfrey J., Wilson R.M.,
RA   Miner T., Farmer C., Delehaunty K., Cordes M., Minx P., Tomlinson C.,
RA   Chen J., Wollam A., Pepin K.H., Bhonagiri V., Zhang X., Warren W.,
RA   Mitreva M., Mardis E.R., Wilson R.K.;
RL   Submitted (JUN-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ERI62544.1}.
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DR   EMBL; AWSR01000128; ERI62544.1; -; Genomic_DNA.
DR   EnsemblBacteria; ERI62544; ERI62544; HMPREF1551_01837.
DR   PATRIC; fig|1227266.3.peg.1632; -.
DR   Proteomes; UP000016494; Unassembled WGS sequence.
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:UP000016494};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN       61    143       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      150    254       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        86     86       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       136    136       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       222    222       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       226    226       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   260 AA;  29105 MW;  F10B4C5BABD96AAF CRC64;
     MLFPLSKFFY SMKKMILPGM LAVVASCHCP KTAQSTAQET VKQAVATENW GNPSDVKAQG
     KFQLSGLAYG YSDLEPYIDG RTMSIHYSKH YLAYTNNLNK AIAGTALESQ SIEQILSGLD
     LNNKAVRNNA GGYYNHTLFW EVMTPKKTAP QGKLLAQINA DFGSFENFKK QFADAAAKQF
     GSGWAWLVVG KDGKLHIGDT PNQDNPLMPN MPIQGTPILA LDVWEHAYYL KYQNLRPKYI
     EAFFNVINWD KVAEKFEASR
//
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