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Database: UniProt
Entry: A0A1E3C4D7_9CLOT
LinkDB: A0A1E3C4D7_9CLOT
Original site: A0A1E3C4D7_9CLOT 
ID   A0A1E3C4D7_9CLOT        Unreviewed;       223 AA.
AC   A0A1E3C4D7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   05-DEC-2018, entry version 10.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=A7W90_17090 {ECO:0000313|EMBL:ODM27791.1};
OS   Clostridium sp. Bc-iso-3.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1848158 {ECO:0000313|EMBL:ODM27791.1, ECO:0000313|Proteomes:UP000094992};
RN   [1] {ECO:0000313|EMBL:ODM27791.1, ECO:0000313|Proteomes:UP000094992}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bc-iso-3 {ECO:0000313|EMBL:ODM27791.1,
RC   ECO:0000313|Proteomes:UP000094992};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-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}.
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:ODM27791.1}.
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DR   EMBL; LXSB01000001; ODM27791.1; -; Genomic_DNA.
DR   RefSeq; WP_069196009.1; NZ_LXSB01000001.1.
DR   EnsemblBacteria; ODM27791; ODM27791; A7W90_17090.
DR   Proteomes; UP000094992; 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:UP000094992};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN       12     93       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      106    203       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        37     37       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        85     85       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       170    170       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       174    174       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   223 AA;  26124 MW;  1634B6A32666D8FD CRC64;
     MQYAMMPVAA GQHRLPPLPY SYNALEPIIG EETLRIHHDI LHKAYVDGLN QAEISLVEAR
     RSNDYKYIKF WENKLAYNGS GHILHSVFWT IMAPLGKGGQ PGIHTVNQIN SYFGSFNAFK
     EQFKSATENV EASGWGILTW QPTWRRLEIL QAEKHQNLTQ WSGIPILVCD VWEHAYYLDY
     QNRRKEYINR WWDLINWNEV ERRLLLAMNG QVPLTLMSNF RFA
//
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