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Database: UniProt
Entry: A0A1D7XKL0_9CLOT
LinkDB: A0A1D7XKL0_9CLOT
Original site: A0A1D7XKL0_9CLOT 
ID   A0A1D7XKL0_9CLOT        Unreviewed;       204 AA.
AC   A0A1D7XKL0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   13-FEB-2019, entry version 17.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=BGI42_07790 {ECO:0000313|EMBL:AOR23639.1};
OS   Clostridium taeniosporum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=394958 {ECO:0000313|EMBL:AOR23639.1, ECO:0000313|Proteomes:UP000094652};
RN   [1] {ECO:0000313|Proteomes:UP000094652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1/k {ECO:0000313|Proteomes:UP000094652};
RA   Walker J.R.;
RT   "Genomics of Clostridium taeniosporum, an organism which forms
RT   endospores with ribbon-like appendages.";
RL   Submitted (SEP-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:
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}.
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DR   EMBL; CP017253; AOR23639.1; -; Genomic_DNA.
DR   RefSeq; WP_069679790.1; NZ_CP017253.2.
DR   EnsemblBacteria; AOR23639; AOR23639; BGI42_07790.
DR   KEGG; ctae:BGI42_07790; -.
DR   KO; K04564; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; GCF_001735765:G1F6T-1565-MONOMER; -.
DR   Proteomes; UP000094652; 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:UP000094652};
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:UP000094652}.
FT   DOMAIN        3     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    196       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        26     26       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        82     82       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   204 AA;  23643 MW;  638D5429B8AE13C2 CRC64;
     MFDKIELSYE YDDLEPYIDA ETVNIHYNKH LQGYVNNLNK ILKGYDNLTK GKTLEQILLN
     VGSFPQEIRQ NIINQGGGVI NHNLYFYILS PKPKLKPEGS LLYEINNTFG NIENLKIQLT
     NLTISQFGSG YGFLVKDMNG KLSIHKTLNQ NSPISDGLTP ILCIDVWEHA YYLKYKNLRA
     DYVKNIWNVI DWGKIENLYE NYII
//
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