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Database: UniProt/TrEMBL
Entry: K9UQB8_9CYAN
LinkDB: K9UQB8_9CYAN
Original site: K9UQB8_9CYAN 
ID   K9UQB8_9CYAN            Unreviewed;       197 AA.
AC   K9UQB8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   07-JUN-2017, entry version 24.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=Cha6605_5537 {ECO:0000313|EMBL:AFY96414.1};
OS   Chamaesiphon minutus PCC 6605.
OC   Bacteria; Cyanobacteria; Synechococcales; Chamaesiphonaceae;
OC   Chamaesiphon.
OX   NCBI_TaxID=1173020 {ECO:0000313|EMBL:AFY96414.1, ECO:0000313|Proteomes:UP000010366};
RN   [1] {ECO:0000313|EMBL:AFY96414.1, ECO:0000313|Proteomes:UP000010366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6605 {ECO:0000313|EMBL:AFY96414.1,
RC   ECO:0000313|Proteomes:UP000010366};
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., Chen A.,
RA   Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Pagani I., Pati A., Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X.,
RA   Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Chamaesiphon sp. PCC 6605.";
RL   Submitted (MAY-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; CP003600; AFY96414.1; -; Genomic_DNA.
DR   RefSeq; WP_015162496.1; NC_019697.1.
DR   EnsemblBacteria; AFY96414; AFY96414; Cha6605_5537.
DR   KEGG; cmp:Cha6605_5537; -.
DR   PATRIC; fig|1173020.3.peg.6361; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000010366; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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   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:UP000010366};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010366}.
FT   DOMAIN        6     87       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       94    194       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        79     79       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   197 AA;  21841 MW;  207F390C97CF5104 CRC64;
     MAFVQEALPY DVSALEPHMS AKTFEFHYGK HHATYVTNLN NLTKDTPMAD MSIEDVVRGS
     FGDASKAGIF NNAAQVWNHA FFWKSMKPNG GGAPTGELAA KIDADFGSFD QFKTDFKAAA
     TTQFGSGWAW LVNDGGTLKI TKTGNAENPL VHGQTPLLTL DVWEHAYYLD FQNRRPDFIS
     TYLDSLVNWD FAAANFK
//
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