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Database: UniProt
Entry: K9XKI9_9CHRO
LinkDB: K9XKI9_9CHRO
Original site: K9XKI9_9CHRO 
ID   K9XKI9_9CHRO            Unreviewed;       248 AA.
AC   K9XKI9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   16-JAN-2019, entry version 30.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=Glo7428_4713 {ECO:0000313|EMBL:AFZ33145.1};
OS   Gloeocapsa sp. PCC 7428.
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Chroococcaceae; Gloeocapsa.
OX   NCBI_TaxID=1173026 {ECO:0000313|EMBL:AFZ33145.1, ECO:0000313|Proteomes:UP000010476};
RN   [1] {ECO:0000313|EMBL:AFZ33145.1, ECO:0000313|Proteomes:UP000010476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7428 {ECO:0000313|EMBL:AFZ33145.1,
RC   ECO:0000313|Proteomes:UP000010476};
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., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y.,
RA   Chain P., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA   Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A.,
RA   Goodwin L., Peters L., Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Gloeocapsa sp. PCC 7428.";
RL   Submitted (JUN-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:
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
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CP003646; AFZ33145.1; -; Genomic_DNA.
DR   RefSeq; WP_015191012.1; NC_019745.1.
DR   EnsemblBacteria; AFZ33145; AFZ33145; Glo7428_4713.
DR   KEGG; glp:Glo7428_4713; -.
DR   PATRIC; fig|1173026.3.peg.4957; -.
DR   KO; K04564; -.
DR   BioCyc; GSP1173026:G1HCT-4687-MONOMER; -.
DR   Proteomes; UP000010476; 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   InterPro; IPR006311; TAT_signal.
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.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000010476};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AFZ33145.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010476};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    248       Superoxide dismutase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003938016.
FT   DOMAIN       44    132       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      139    240       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        69     69       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       124    124       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       207    207       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       211    211       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   248 AA;  27712 MW;  EF765B3EDADA3410 CRC64;
     MTLNRRNLLF LLGASAGAVA IDTLRPHGLL QTALAAESPS GSGSFELPPL PYAYNALEPH
     IDAATMRFHH DRHHATYVKN LNAALEKHPQ LKGRSAEQLL SNLNSVPEDI RTSVRNNGGG
     HVNHSMFWRI MSPDGGGEPT GQIATVINQN FGSFAEFKKQ FNSAGEGRFG SGWAWLVRTR
     DGNYQITSTA NQDSPFMEGN YPIMGNDVWE HAYYLKYQNR RAEYLNAWWN VVNWNEINQR
     LAQATKTA
//
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