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Database: UniProt
Entry: A0A1B9E9Q8_9FLAO
LinkDB: A0A1B9E9Q8_9FLAO
Original site: A0A1B9E9Q8_9FLAO 
ID   A0A1B9E9Q8_9FLAO        Unreviewed;       258 AA.
AC   A0A1B9E9Q8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   28-MAR-2018, entry version 9.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=LPBF_01410 {ECO:0000313|EMBL:OCB78679.1};
OS   Flavobacterium crassostreae.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1763534 {ECO:0000313|EMBL:OCB78679.1, ECO:0000313|Proteomes:UP000093510};
RN   [1] {ECO:0000313|EMBL:OCB78679.1, ECO:0000313|Proteomes:UP000093510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0076 {ECO:0000313|EMBL:OCB78679.1,
RC   ECO:0000313|Proteomes:UP000093510};
RA   Ploux O.;
RL   Submitted (MAR-2016) 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}.
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:OCB78679.1}.
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DR   EMBL; LVEP01000002; OCB78679.1; -; Genomic_DNA.
DR   RefSeq; WP_066331498.1; NZ_LVEP01000002.1.
DR   EnsemblBacteria; OCB78679; OCB78679; LPBF_01410.
DR   Proteomes; UP000093510; 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:UP000093510};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093510}.
FT   DOMAIN       54    137       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      146    248       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        79     79       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       129    129       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       216    216       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       220    220       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   258 AA;  29265 MW;  3100E69F0D04A357 CRC64;
     MKNTALLIVS WITTLFLFSC QDKKLTEVVE VPLPTAQEKV AIGHPEDVKA AQGSFQLEKL
     AYSYDALAPT VSALTLETHY SKHYLSYTNN LNKAISGTPY ENQSIENILA KLDLNNPELR
     NNAGGYYNHT LYWKSMAPDT PDVATDTLAA VINRDFGSFK NFEIAFKNEA TNQFGSAWTF
     LVVDKYGKLK LTSTQNQDNP LMRNAAVPGT PILALDLWEH AYYLGYQYRR KSYIDSFFTV
     INWAKINENY EAAIRKKY
//
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