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Database: UniProt
Entry: J1KSF7_9FLAO
LinkDB: J1KSF7_9FLAO
Original site: J1KSF7_9FLAO 
ID   J1KSF7_9FLAO            Unreviewed;       203 AA.
AC   J1KSF7;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   10-OCT-2018, entry version 26.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=FF52_12586 {ECO:0000313|EMBL:EJG01098.1};
OS   Flavobacterium sp. F52.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1202532 {ECO:0000313|EMBL:EJG01098.1, ECO:0000313|Proteomes:UP000002690};
RN   [1] {ECO:0000313|EMBL:EJG01098.1, ECO:0000313|Proteomes:UP000002690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F52 {ECO:0000313|EMBL:EJG01098.1,
RC   ECO:0000313|Proteomes:UP000002690};
RX   PubMed=22965088; DOI=10.1128/JB.01249-12;
RA   Kolton M., Green S.J., Harel Y.M., Sela N., Elad Y., Cytryn E.;
RT   "Draft Genome Sequence of Flavobacterium sp. Strain F52, Isolated from
RT   the Rhizosphere of Bell Pepper (Capsicum annuum L. cv. Maccabi).";
RL   J. Bacteriol. 194:5462-5463(2012).
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}.
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:EJG01098.1}.
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DR   EMBL; AKZQ01000026; EJG01098.1; -; Genomic_DNA.
DR   RefSeq; WP_008465979.1; NZ_AKZQ01000026.1.
DR   ProteinModelPortal; J1KSF7; -.
DR   EnsemblBacteria; EJG01098; EJG01098; FF52_12586.
DR   GeneID; 32307356; -.
DR   PATRIC; fig|1202532.3.peg.2581; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; FSP1202532:G1181-662-MONOMER; -.
DR   Proteomes; UP000002690; 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:UP000002690};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        3     85       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       92    198       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        77     77       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       169    169       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   203 AA;  22486 MW;  9E3276903E242E08 CRC64;
     MAFELPQLPY AYDALEPHID ARTMEIHHTK HHNAYTTNLN AAIAGTDLEG KTIENILINL
     DKSNAAVRNN GGGFYNHNLF WTVMSPNGGG LPTGDLLAAI ESSFGSFEEF KAKFAKAGAT
     QFGSGWAWLT VQKGGKLEVV GTPNQDNPLM PEVAGHGGTP ILGMDVWEHA YYLNYQNRRP
     DYIEAFFNVI NWTEVARRFA LEK
//
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