ID   SODF_SYNE7              Reviewed;         201 AA.
AC   P18655; Q31Q36;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodB; OrderedLocusNames=Synpcc7942_0801;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2501651; DOI=10.1007/bf00334390;
RA   Laudenbach D.E., Trick C.G., Straus N.A.;
RT   "Cloning and characterization of an Anacystis nidulans R2 superoxide
RT   dismutase gene.";
RL   Mol. Gen. Genet. 216:455-461(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological systems.
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   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABB56833.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X17431; CAB57855.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB56833.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_039755809.1; NC_007604.1.
DR   AlphaFoldDB; P18655; -.
DR   SMR; P18655; -.
DR   STRING; 1140.Synpcc7942_0801; -.
DR   PRIDE; P18655; -.
DR   EnsemblBacteria; ABB56833; ABB56833; Synpcc7942_0801.
DR   KEGG; syf:Synpcc7942_0801; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_0_3; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_0801-MON; -.
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; -; 1.
DR   Gene3D; 3.55.40.20; -; 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   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..201
FT                   /note="Superoxide dismutase [Fe]"
FT                   /id="PRO_0000160002"
FT   BINDING         27
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   201 AA;  22083 MW;  E08E14F00ACED949 CRC64;
     MSYELPALPF DYTALAPYIT KETLEFHHDK HHAAYVNNYN NAVKDTDLDG QPIEAVIKAI
     AGDASKAGLF NNAAQAWNHS FYWNSIKPNG GGAPTGALAD KIAADFGSFE NFVTEFKQAA
     ATQFGSGWAW LVLDNGTLKI TKTGNADTPI AHGQTPLLTI DVWEHAYYLD YQNRRPDYIS
     TFVEKLANWD FASANYAAAI A