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Database: UniProt
Entry: P50061
LinkDB: P50061
Original site: P50061 
ID   SODF_LEPBY              Reviewed;         199 AA.
AC   P50061;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   05-DEC-2018, entry version 78.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodB;
OS   Leptolyngbya boryana (Plectonema boryanum).
OC   Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae;
OC   Leptolyngbya.
OX   NCBI_TaxID=1184;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UTEX 485 / CCAP 1462/4;
RX   PubMed=7860607; DOI=10.1128/jb.177.4.964-972.1995;
RA   Campbell W.S., Laudenbach D.E.;
RT   "Characterization of four superoxide dismutase genes from a
RT   filamentous cyanobacterium.";
RL   J. Bacteriol. 177:964-972(1995).
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;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Expressed constitutively, although partially repressed
CC       under conditions of iron stress.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; U17612; AAA69954.1; -; Genomic_DNA.
DR   ProteinModelPortal; P50061; -.
DR   SMR; P50061; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Cytoplasm; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN         1    199       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000160065.
FT   METAL        28     28       Iron. {ECO:0000250}.
FT   METAL        80     80       Iron. {ECO:0000250}.
FT   METAL       162    162       Iron. {ECO:0000250}.
FT   METAL       166    166       Iron. {ECO:0000250}.
SQ   SEQUENCE   199 AA;  21934 MW;  F6F4B123DF5E49DF CRC64;
     MAFTQPPLPF PKDALEPYGM KAETFDYHYG KHHAAYVTNL NKLVEGTPME SLSLEDVIKQ
     SFGDSSKVGV FNNAAQVWNH TFFWNCLKAG GGGAPTGELA AKIDAAFGSL DKFKEEFSNA
     AATQFGSGWA WLVDDGGTLK VTKTPNAENP LVHGQKPLLT LDVWEHAYYL DFQNARPAFI
     KNFLDNLVNW DFVAQNLAA
//
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