ID   SODM3_LEPBY             Reviewed;         239 AA.
AC   P50060;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Superoxide dismutase [Mn] 3;
DE            EC=1.15.1.1;
DE   Flags: Precursor; Fragment;
GN   Name=sodA3;
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   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U17611; AAA69953.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50060; -.
DR   SMR; P50060; -.
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   3: Inferred from homology;
KW   Manganese; Metal-binding; Oxidoreductase; Signal.
FT   SIGNAL          <1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..239
FT                   /note="Superoxide dismutase [Mn] 3"
FT                   /id="PRO_0000032905"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         57
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         199
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   239 AA;  26854 MW;  242CBD3C9C61D100 CRC64;
     ASTQQTPAQS PTASPTVSTP VAYVDRPLTA SPAQLPPLPY DAGALSKAID AETMRIHHDR
     HHQTYVDNLN TALKDQPNLQ NLSIEAMLRD LNAVPENIRN TIRNNAGGHL NHTIFWQIMS
     PDGGGQPTGA IAQAINQTFG NFESFRKQFN EAGGDRFGSG WVWLVRNAQG QLQIVSTANQ
     DNPIMEGNYP IMGNDVWEHA YYLRYQNRRA DYLNNWWNVV NWNEINRRFQ AASQQQARS