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Database: UniProt
Entry: P83157
LinkDB: P83157
Original site: P83157 
ID   SODF_ANASL              Reviewed;           9 AA.
AC   P83157;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   05-DEC-2018, entry version 27.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
DE   Flags: Fragment;
GN   Name=sodB {ECO:0000250|UniProtKB:P09213};
OS   Anabaena sp. (strain L31).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=29412;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RA   Apte S.K., Uhlemann E., Schmid R., Altendorf K.;
RL   Submitted (OCT-2001) to UniProtKB.
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems.
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; Evidence={ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000250|UniProtKB:P09213};
CC       Note=Binds 1 Fe cation per subunit.
CC       {ECO:0000250|UniProtKB:P09213};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P09213}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000255}.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN         1     >9       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000262944.
FT   NON_TER       9      9
SQ   SEQUENCE   9 AA;  1063 MW;  C54267376B06C2C9 CRC64;
     AFVQEPLPY
//
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