ID   H6SLW7_PARPM            Unreviewed;       235 AA.
AC   H6SLW7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   28-JAN-2026, entry version 51.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=RSPPHO_02356 {ECO:0000313|EMBL:CCG08982.1};
OS   Pararhodospirillum photometricum DSM 122.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rhodospirillales; Rhodospirillaceae; Pararhodospirillum.
OX   NCBI_TaxID=1150469 {ECO:0000313|EMBL:CCG08982.1, ECO:0000313|Proteomes:UP000033220};
RN   [1] {ECO:0000313|EMBL:CCG08982.1, ECO:0000313|Proteomes:UP000033220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM122 {ECO:0000313|Proteomes:UP000033220};
RA   Duquesne K., Sturgis J.;
RT   "Shotgun genome sequence of Phaeospirillum photometricum DSM 122.";
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   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological systems.
CC       Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2
CC       by successive reduction and oxidation of the transition metal ion at
CC       the active site. {ECO:0000256|ARBA:ARBA00024318}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 superoxide + 2 H(+) = 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|ARBA:ARBA00047393};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697;
CC         Evidence={ECO:0000256|ARBA:ARBA00047393};
CC   -!- COFACTOR:
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC         Evidence={ECO:0000256|ARBA:ARBA00001965};
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; HE663493; CCG08982.1; -; Genomic_DNA.
DR   AlphaFoldDB; H6SLW7; -.
DR   STRING; 1150469.RSPPHO_02356; -.
DR   KEGG; rpm:RSPPHO_02356; -.
DR   PATRIC; fig|1150469.3.peg.2663; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_0_5; -.
DR   Proteomes; UP000033220; Chromosome DSM 122.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-ARBA.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:UniProtKB-ARBA.
DR   FunFam; 1.10.287.990:FF:000002; Superoxide dismutase; 1.
DR   FunFam; 3.55.40.20:FF:000001; Superoxide dismutase; 1.
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; PTHR42769; SUPEROXIDE DISMUTASE; 1.
DR   PANTHER; PTHR42769:SF3; SUPEROXIDE DISMUTASE [FE] 2, CHLOROPLASTIC; 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   Iron {ECO:0000256|ARBA:ARBA00023004};
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:UP000033220}.
FT   DOMAIN          38..121
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          129..229
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         62
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         114
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         196
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         200
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   235 AA;  26004 MW;  B064A3F2A571501E CRC64;
     MVAYPSQREV PAINLEHPGA PQKAARPFFR WRVSAMAFVL PPLPFAQDAL EPHMSAQTLS
     FHHGKHHNAY VTNLNALIAD TPLATQSLEE IIRETHGDPS RVGVFNNAAQ VWNHTFFWSG
     LKPGGGGTPS GALLDALTAA FGSFDAFKDQ FKQTAVSQFG SGWAWLVLDK GTLRLTKTGN
     ADVPLTSGQV PLLTCDVWEH AYYLDFQNRR PDFVQTFLDH LINWDFVASN FQAAQ
//