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Database: UniProt/TrEMBL
Entry: A0A0F7K213_9GAMM
LinkDB: A0A0F7K213_9GAMM
Original site: A0A0F7K213_9GAMM 
ID   A0A0F7K213_9GAMM        Unreviewed;       192 AA.
AC   A0A0F7K213;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   28-MAR-2018, entry version 14.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=AAY24_15760 {ECO:0000313|EMBL:AKH21569.1};
OS   Sedimenticola thiotaurini.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Sedimenticola.
OX   NCBI_TaxID=1543721 {ECO:0000313|EMBL:AKH21569.1, ECO:0000313|Proteomes:UP000034410};
RN   [1] {ECO:0000313|EMBL:AKH21569.1, ECO:0000313|Proteomes:UP000034410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIP-G1 {ECO:0000313|EMBL:AKH21569.1,
RC   ECO:0000313|Proteomes:UP000034410};
RX   PubMed=26089430;
RA   Flood B.E., Jones D.S., Bailey J.V.;
RT   "Complete Genome Sequence of Sedimenticola thiotaurini Strain SIP-G1,
RT   a Polyphosphate- and Polyhydroxyalkanoate-Accumulating Sulfur-
RT   Oxidizing Gammaproteobacterium Isolated from Salt Marsh Sediments.";
RL   Genome Announc. 3:e00671-15(2015).
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; CP011412; AKH21569.1; -; Genomic_DNA.
DR   RefSeq; WP_046860494.1; NZ_CP011412.1.
DR   EnsemblBacteria; AKH21569; AKH21569; AAY24_15760.
DR   KEGG; seds:AAY24_15760; -.
DR   PATRIC; fig|1543721.4.peg.3247; -.
DR   KO; K04564; -.
DR   Proteomes; UP000034410; 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:UP000034410};
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:UP000034410}.
FT   DOMAIN        3     81       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       88    188       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        74     74       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       156    156       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       160    160       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   192 AA;  21302 MW;  9114D1F203B5F9A8 CRC64;
     MAHELPPLPY AQDALEPVIS KETLEYHYGK HHQTYVTNLN NLVKGTDLEN ASLEEIIMKA
     SGGQFNNAAQ VWNHTFYWNC LCPGGSAPSS QLSDAINSAF GSMDEFKKQF SASAAGNFGS
     GWTWLVKNSD GGLEIVNTSN AANPMTDGKT PLLTIDVWEH AYYIDYRNAR PKYLEAVWNI
     VNWEYVSANF AG
//
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