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Database: UniProt
Entry: K9PE47_9CYAN
LinkDB: K9PE47_9CYAN
Original site: K9PE47_9CYAN 
ID   K9PE47_9CYAN            Unreviewed;       200 AA.
AC   K9PE47;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   28-MAR-2018, entry version 25.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=Cal7507_0532 {ECO:0000313|EMBL:AFY31024.1};
OS   Calothrix sp. PCC 7507.
OC   Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Calothrix.
OX   NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY31024.1, ECO:0000313|Proteomes:UP000010390};
RN   [1] {ECO:0000313|EMBL:AFY31024.1, ECO:0000313|Proteomes:UP000010390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY31024.1,
RC   ECO:0000313|Proteomes:UP000010390};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A.,
RA   Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished genome of Calothrix sp. PCC 7507.";
RL   Submitted (APR-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   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CP003943; AFY31024.1; -; Genomic_DNA.
DR   RefSeq; WP_015126849.1; NC_019682.1.
DR   EnsemblBacteria; AFY31024; AFY31024; Cal7507_0532.
DR   KEGG; calo:Cal7507_0532; -.
DR   PATRIC; fig|99598.3.peg.592; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; CSP99598:G1HCH-523-MONOMER; -.
DR   Proteomes; UP000010390; 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; -; 1.
DR   Gene3D; 2.40.500.20; -; 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   Complete proteome {ECO:0000313|Proteomes:UP000010390};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AFY31024.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010390}.
FT   DOMAIN        6     87       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       95    195       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        80     80       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       162    162       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       166    166       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   200 AA;  22398 MW;  4A0A26FCFC741464 CRC64;
     MAFVQAPLPY DFNALEPYGM KAETFEYHYG KHHKAYVDNL NKLTDGTELA DKSLEEVIQI
     SYKDSSKVGI FNNAAQVWNH TFFWSSLAPA GGGTPTDELA AKIDKDFGSL DKLKEEFSNA
     AATQFGSGWA WLIDDGGTLK VIKTPNAENP LAYGQKALLT LDVWEHAYYI DYRNARPGYI
     KNFLDQLINW DFAAENLAKA
//
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