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Database: UniProt/TrEMBL
Entry: B7KHG4_CYAP7
LinkDB: B7KHG4_CYAP7
Original site: B7KHG4_CYAP7 
ID   B7KHG4_CYAP7            Unreviewed;       241 AA.
AC   B7KHG4;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   07-JUN-2017, entry version 54.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=PCC7424_2237 {ECO:0000313|EMBL:ACK70659.1};
OS   Cyanothece sp. (strain PCC 7424) (Synechococcus sp. (strain ATCC
OS   29155)).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Cyanothecaceae; Cyanothece.
OX   NCBI_TaxID=65393 {ECO:0000313|EMBL:ACK70659.1, ECO:0000313|Proteomes:UP000002384};
RN   [1] {ECO:0000313|Proteomes:UP000002384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7424 {ECO:0000313|Proteomes:UP000002384};
RX   PubMed=21972240; DOI=10.1128/mBio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M.,
RA   Min H., Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a
RT   group of unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
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; CP001291; ACK70659.1; -; Genomic_DNA.
DR   RefSeq; WP_015954264.1; NC_011729.1.
DR   ProteinModelPortal; B7KHG4; -.
DR   STRING; 65393.PCC7424_2237; -.
DR   EnsemblBacteria; ACK70659; ACK70659; PCC7424_2237.
DR   KEGG; cyc:PCC7424_2237; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; DSPLMHG; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000002384; 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   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:UP000002384};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:ACK70659.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002384}.
FT   DOMAIN       40    127       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      134    235       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        64     64       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       119    119       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       202    202       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       206    206       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   241 AA;  27585 MW;  1024454F6E3624FA CRC64;
     MNINRRNFLF ILGAGIGTTA LGIYPRQGFA QTLEDNSEPF KLPPLPYSYN ALEPYIDEET
     MRFHHDKHHA GYTKKFNAAI SKYPDLKIQS AEELLSNIDK LPKNIQTTVR QNGGGYLNHA
     IFWEIMSPNG GGQPTGEIAE AINQEFGSFE AFKNAFNEAG NSRFGSGWAW LVLDKKGKLQ
     VVSTPNQDSP LMEGMYPIMG NDVWEHAYYL KYRNDRGQYL QQWWNVVNWN EVNKRFLLVK
     V
//
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