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Database: UniProt/TrEMBL
Entry: A0A1P8WK06_9PLAN
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ID   A0A1P8WK06_9PLAN        Unreviewed;       203 AA.
AC   A0A1P8WK06;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=sodB {ECO:0000313|EMBL:APZ94407.1};
GN   ORFNames=Fuma_04039 {ECO:0000313|EMBL:APZ94407.1};
OS   Fuerstiella marisgermanici.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Fuerstiella.
OX   NCBI_TaxID=1891926 {ECO:0000313|EMBL:APZ94407.1, ECO:0000313|Proteomes:UP000187735};
RN   [1] {ECO:0000313|EMBL:APZ94407.1, ECO:0000313|Proteomes:UP000187735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NH11 {ECO:0000313|EMBL:APZ94407.1,
RC   ECO:0000313|Proteomes:UP000187735};
RX   PubMed=28066393; DOI=10.3389/fmicb.2016.02079;
RA   Kohn T., Heuer A., Jogler M., Vollmers J., Boedeker C., Bunk B., Rast P.,
RA   Borchert D., Glockner I., Freese H.M., Klenk H.P., Overmann J.,
RA   Kaster A.K., Rohde M., Wiegand S., Jogler C.;
RT   "Fuerstia marisgermanicae gen. nov., sp. nov., an Unusual Member of the
RT   Phylum Planctomycetes from the German Wadden Sea.";
RL   Front. Microbiol. 7:2079-2079(2016).
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; CP017641; APZ94407.1; -; Genomic_DNA.
DR   RefSeq; WP_077025716.1; NZ_CP017641.1.
DR   AlphaFoldDB; A0A1P8WK06; -.
DR   STRING; 1891926.Fuma_04039; -.
DR   KEGG; fmr:Fuma_04039; -.
DR   OrthoDB; 9803125at2; -.
DR   Proteomes; UP000187735; 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:UP000187735}.
FT   DOMAIN          3..89
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          96..197
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         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   203 AA;  22348 MW;  0DD069306B3C67A4 CRC64;
     MAYTLPDLPY AKDALEPHID ARTMEIHHGK HHQAYINKVN AALEGTEYAD KCIIEVMKQL
     KSLPANLQGP VRNNGGGHAN HSLFWTVMSP EGGGAPSGEL ADAINAACGS FDKFKEDFSN
     AAATQFGSGW AWLSVKPDGT LTVESTPNQD TPLSEGRTPI LGLDVWEHAY YLNYQNRRPD
     YVSAFWNVVN WDEVAKRFAE AKG
//
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