ID   D7E1G9_NOSA0            Unreviewed;       240 AA.
AC   D7E1G9;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Aazo_0749 {ECO:0000313|EMBL:ADI63196.1};
OS   Nostoc azollae (strain 0708) (Anabaena azollae (strain 0708)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Trichormus.
OX   NCBI_TaxID=551115 {ECO:0000313|EMBL:ADI63196.1, ECO:0000313|Proteomes:UP000001511};
RN   [1] {ECO:0000313|EMBL:ADI63196.1, ECO:0000313|Proteomes:UP000001511}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0708 {ECO:0000313|EMBL:ADI63196.1,
RC   ECO:0000313|Proteomes:UP000001511};
RX   PubMed=20628610; DOI=10.1371/journal.pone.0011486;
RA   Ran L., Larsson J., Vigil-Stenman T., Nylander J.A., Ininbergs K.,
RA   Zheng W.W., Lapidus A., Lowry S., Haselkorn R., Bergman B.;
RT   "Genome erosion in a nitrogen-fixing vertically transmitted endosymbiotic
RT   multicellular cyanobacterium.";
RL   PLoS ONE 5:E11486-E11486(2010).
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 family.
CC       {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CP002059; ADI63196.1; -; Genomic_DNA.
DR   RefSeq; WP_013190214.1; NC_014248.1.
DR   AlphaFoldDB; D7E1G9; -.
DR   STRING; 551115.Aazo_0749; -.
DR   KEGG; naz:Aazo_0749; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_1_3; -.
DR   OrthoDB; 9803125at2; -.
DR   Proteomes; UP000001511; Chromosome.
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; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 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   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43595; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43595:SF2; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
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; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000349-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001511};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..240
FT                   /note="Superoxide dismutase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003094950"
FT   DOMAIN          38..124
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          131..232
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         61
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         116
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         199
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         203
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   240 AA;  27307 MW;  378EE4E63EF8C3AF CRC64;
     MTLNRRHFLL LLGATASAFI LDSNATAETP SHTTPTIQLP PLPYAYEALE PHIDSRTMQF
     HHDKHHAAYV NNLNKVLDKY PKLKNKPVEA LLQNLDQVPS DIRTIVRNNA GGHVNHSMFW
     KIMKPNGGGE PSGEVATAIK DNFGSFIDFR RKFNEAGAGR FGSGWVWLVR TKNGKLEITT
     TGNQDSPIMK GKYPIFGNDV WEHAYYLKYQ NRRPDYLEAW WNVVNWDEIN QRFANGSELG
//