ID   I0IDH9_PHYMF            Unreviewed;       212 AA.
AC   I0IDH9;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
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   Name=sodA {ECO:0000313|EMBL:BAM03317.1};
GN   OrderedLocusNames=PSMK_11580 {ECO:0000313|EMBL:BAM03317.1};
OS   Phycisphaera mikurensis (strain NBRC 102666 / KCTC 22515 / FYK2301M01).
OC   Bacteria; Planctomycetota; Phycisphaerae; Phycisphaerales;
OC   Phycisphaeraceae; Phycisphaera.
OX   NCBI_TaxID=1142394 {ECO:0000313|EMBL:BAM03317.1, ECO:0000313|Proteomes:UP000007881};
RN   [1] {ECO:0000313|EMBL:BAM03317.1, ECO:0000313|Proteomes:UP000007881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102666 / KCTC 22515 / FYK2301M01
RC   {ECO:0000313|Proteomes:UP000007881};
RA   Ankai A., Hosoyama A., Terui Y., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA   Yamada-Narita S., Kawakoshi A., Fukunaga Y., Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Phycisphaera mikurensis NBRC 102666.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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; AP012338; BAM03317.1; -; Genomic_DNA.
DR   RefSeq; WP_014436536.1; NC_017080.1.
DR   AlphaFoldDB; I0IDH9; -.
DR   STRING; 1142394.PSMK_11580; -.
DR   GeneID; 80847606; -.
DR   KEGG; phm:PSMK_11580; -.
DR   PATRIC; fig|1142394.8.peg.1197; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_1_0; -.
DR   OrthoDB; 9803125at2; -.
DR   Proteomes; UP000007881; 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   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.
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:UP000007881}.
FT   DOMAIN          3..88
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          97..205
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         27
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         81
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         173
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         177
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   212 AA;  23337 MW;  66147593B98864FC CRC64;
     MAFSLPSLTY AYDALEPAID ARTMEVHYSK HFAGYASKLT AALEGTEWAD RSVEEILAKL
     DQLPEGKQTA VRNNGGGYFN HDLFFTTLKA PSENNAPSGE LAEAIERDFG GFADFKKSFS
     DAAASRFGSG WAWLCVQPGG KLHVTSTANQ DTTFMPPAFG GHGEGHHPVL GLDVWEHAYY
     LHYQNRRPDY IEAFFSVIDW DKVGEKHAAA KG
//