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Database: UniProt
Entry: T2KGA5_9FLAO
LinkDB: T2KGA5_9FLAO
Original site: T2KGA5_9FLAO 
ID   T2KGA5_9FLAO            Unreviewed;       202 AA.
AC   T2KGA5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   28-MAR-2018, entry version 19.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=BN863_280 {ECO:0000313|EMBL:CDF77740.1};
OS   Formosa agariphila KMM 3901.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Formosa.
OX   NCBI_TaxID=1347342 {ECO:0000313|EMBL:CDF77740.1, ECO:0000313|Proteomes:UP000016160};
RN   [1] {ECO:0000313|EMBL:CDF77740.1, ECO:0000313|Proteomes:UP000016160}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Type strain: KMM 3901 {ECO:0000313|EMBL:CDF77740.1};
RX   PubMed=23995932; DOI=10.1128/AEM.01937-13;
RA   Mann A.J., Hahnke R.L., Huang S., Werner J., Xing P., Barbeyron T.,
RA   Huettel B., Stueber K., Reinhardt R., Harder J., Gloeckner F.O.,
RA   Amann R.I., Teeling H.;
RT   "The genome of the alga-associated marine flavobacterium Formosa
RT   agariphila KMM 3901T reveals a broad potential for degradation of
RT   algal polysaccharides.";
RL   Appl. Environ. Microbiol. 79:6813-6822(2013).
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; HG315671; CDF77740.1; -; Genomic_DNA.
DR   RefSeq; WP_038532941.1; NZ_HG315671.1.
DR   EnsemblBacteria; CDF77740; CDF77740; BN863_280.
DR   PATRIC; fig|1347342.6.peg.29; -.
DR   Proteomes; UP000016160; Chromosome.
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:UP000016160};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:CDF77740.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016160}.
FT   DOMAIN        3     84       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       93    197       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       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   202 AA;  22626 MW;  9B89DFD17916A280 CRC64;
     MAFELPKLQY AYDALEPNID ARTMEIHHTK HHQGYTTKLN GAIEGTELEG KSIEDILTSL
     DMSNGAVRNN GGGFYNHSLF WEIMNPEGKG RLSGDLKAAI EEAFESVDAF KEAFSNAAAT
     QFGSGWAWLC VHKGGKVSVC STPNQDNPLM PGVNCDGTPI LGLDVWEHAY YLNYQNRRPD
     YINAFFDVIN WNEVERRYAE AK
//
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