ID   SODM2_LEPBY             Reviewed;         206 AA.
AC   P50059;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Superoxide dismutase [Mn] 2;
DE            EC=1.15.1.1;
GN   Name=sodA2;
OS   Leptolyngbya boryana (Plectonema boryanum).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Leptolyngbyaceae; 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 filamentous
RT   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 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=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- INDUCTION: By methyl viologen, and under conditions of iron or nitrogen
CC       stress.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; U17610; AAA69952.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50059; -.
DR   SMR; P50059; -.
DR   PRIDE; P50059; -.
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; 3.55.40.20; -; 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   Manganese; Metal-binding; Oxidoreductase.
FT   CHAIN           1..206
FT                   /note="Superoxide dismutase [Mn] 2"
FT                   /id="PRO_0000160064"
FT   BINDING         27
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   206 AA;  23456 MW;  B149F228DB49091E CRC64;
     MAFELKPLPY AYDALEPYID ATTMQLHHDK HHAAYVNNLN AAIEKYSDLQ SMSVEDLVTH
     LDRVPEDVRT TVRNNAGGHV NHTMFWEIMG ANGSGAPTGA ISEAINNSFG SFDAFKQQFN
     DAGTKRFGSG WVWLVRSQQG DLQILSTPNQ DSPLIEGHTP IMGNDVWEHA YYLKYQNRRP
     EYLNAWWNVL NWEEINRRFD AAMSGH