ID   G0IUU5_CYCMS            Unreviewed;       201 AA.
AC   G0IUU5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
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=Cycma_1733 {ECO:0000313|EMBL:AEL25487.1};
OS   Cyclobacterium marinum (strain ATCC 25205 / DSM 745 / LMG 13164 / NCIMB
OS   1802) (Flectobacillus marinus).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Cyclobacterium.
OX   NCBI_TaxID=880070 {ECO:0000313|EMBL:AEL25487.1, ECO:0000313|Proteomes:UP000001635};
RN   [1] {ECO:0000313|Proteomes:UP000001635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25205 / DSM 745 / LMG 13164 / NCIMB 1802
RC   {ECO:0000313|Proteomes:UP000001635};
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Chertkov O.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Cyclobacterium marinum DSM 745.";
RL   Submitted (JUL-2011) 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; CP002955; AEL25487.1; -; Genomic_DNA.
DR   RefSeq; WP_014019782.1; NC_015914.1.
DR   AlphaFoldDB; G0IUU5; -.
DR   STRING; 880070.Cycma_1733; -.
DR   KEGG; cmr:Cycma_1733; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_1_10; -.
DR   OrthoDB; 9803125at2; -.
DR   Proteomes; UP000001635; 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:UP000001635}.
FT   DOMAIN          3..85
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          92..196
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         77
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         163
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         167
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   201 AA;  22062 MW;  388BF08770AD6761 CRC64;
     MAFELPSLPY ETNALEPNID AKTMEIHHGK HHNAYVTKLN DAIKGTDLES KSIEELMENV
     SSAPAGVRNN GGGHYNHSLF WTILSPNGGG APSGDLAAAI DAKFGSFDKF KEEFANAAAT
     RFGSGWAWLS VSNGELVVSS TPNQDNPVMD IAETKGTPIL GLDVWEHAYY LNYQNRRPDY
     ISAFWNVVNW DEVAKRYAAA K
//