ID   E0TI36_PARBH            Unreviewed;       202 AA.
AC   E0TI36;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
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=PB2503_06547 {ECO:0000313|EMBL:ADM09375.1};
OS   Parvularcula bermudensis (strain ATCC BAA-594 / HTCC2503 / KCTC 12087).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Parvularculales;
OC   Parvularculaceae; Parvularcula.
OX   NCBI_TaxID=314260 {ECO:0000313|EMBL:ADM09375.1, ECO:0000313|Proteomes:UP000001302};
RN   [1] {ECO:0000313|Proteomes:UP000001302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC   {ECO:0000313|Proteomes:UP000001302};
RA   Kang D.-M., Oh H.-M., Cho J.-C.;
RT   "Genome sequence of Parvularcula bermudensis HTCC2503.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADM09375.1, ECO:0000313|Proteomes:UP000001302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC   {ECO:0000313|Proteomes:UP000001302};
RX   PubMed=21037002; DOI=10.1128/JB.01205-10;
RA   Oh H.M., Kang I., Vergin K.L., Kang D., Rhee K.H., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2503T of Parvularcula bermudensis,
RT   the type species of the order "Parvularculales" in the class
RT   Alphaproteobacteria.";
RL   J. Bacteriol. 193:305-306(2011).
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; CP002156; ADM09375.1; -; Genomic_DNA.
DR   RefSeq; WP_013300349.1; NC_014414.1.
DR   AlphaFoldDB; E0TI36; -.
DR   STRING; 314260.PB2503_06547; -.
DR   KEGG; pbr:PB2503_06547; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_0_5; -.
DR   OrthoDB; 9803125at2; -.
DR   Proteomes; UP000001302; 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; 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   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:UP000001302}.
FT   DOMAIN          4..86
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          97..198
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         78
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         164
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         168
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   202 AA;  22449 MW;  82D494EB917C0A90 CRC64;
     MAISLMDLPY EKTALAPHIS EDTLNYHHGK HHQAYVTKTN DAIKGTALDD ADLEAIVKEA
     KKTANQGLFN NSAQVWNHNI YWQSMSPNGG GAPKAGSKIA EAIDKSFGSY DEFKAKFKDA
     GGTQFGSGWA WLVAKKDGSL EILKTLNADC PLTDESVTTL LTMDVWEHAY YLDYQNARPD
     YMTHFLDNLV NWDFAEERLA AA
//