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Database: UniProt/TrEMBL
Entry: Q8DIR2_THEEB
LinkDB: Q8DIR2_THEEB
Original site: Q8DIR2_THEEB 
ID   Q8DIR2_THEEB            Unreviewed;       200 AA.
AC   Q8DIR2;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   25-OCT-2017, entry version 95.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodB {ECO:0000313|EMBL:BAC09071.1};
OS   Thermosynechococcus elongatus (strain BP-1).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221 {ECO:0000313|EMBL:BAC09071.1, ECO:0000313|Proteomes:UP000000440};
RN   [1] {ECO:0000313|EMBL:BAC09071.1, ECO:0000313|Proteomes:UP000000440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BP-1 {ECO:0000313|EMBL:BAC09071.1,
RC   ECO:0000313|Proteomes:UP000000440};
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N.,
RA   Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
RN   [2] {ECO:0000213|PDB:1MY6}
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-200 IN COMPLEX WITH IRON.
RX   PubMed=12827458; DOI=10.1007/s00775-003-0469-0;
RA   Kerfeld C.A., Yoshida S., Tran K.T., Yeates T.O., Cascio D.,
RA   Bottin H., Berthomieu C., Sugiura M., Boussac A.;
RT   "The 1.6 A resolution structure of Fe-superoxide dismutase from the
RT   thermophilic cyanobacterium Thermosynechococcus elongatus.";
RL   J. Biol. Inorg. Chem. 8:707-714(2003).
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; BA000039; BAC09071.1; -; Genomic_DNA.
DR   RefSeq; NP_682309.1; NC_004113.1.
DR   RefSeq; WP_011057359.1; NC_004113.1.
DR   PDB; 1MY6; X-ray; 1.60 A; A/B=2-200.
DR   PDBsum; 1MY6; -.
DR   ProteinModelPortal; Q8DIR2; -.
DR   SMR; Q8DIR2; -.
DR   STRING; 197221.tll1519; -.
DR   EnsemblBacteria; BAC09071; BAC09071; BAC09071.
DR   GeneID; 1011132; -.
DR   KEGG; tel:tll1519; -.
DR   PATRIC; fig|197221.4.peg.1596; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; POG091H03Q7; -.
DR   EvolutionaryTrace; Q8DIR2; -.
DR   Proteomes; UP000000440; 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; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0000213|PDB:1MY6};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000440};
KW   Iron {ECO:0000213|PDB:1MY6};
KW   Metal-binding {ECO:0000213|PDB:1MY6, ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000440}.
FT   DOMAIN        6     88       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        28     28       Iron; via tele nitrogen.
FT                                {ECO:0000213|PDB:1MY6}.
FT   METAL        80     80       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        80     80       Iron; via tele nitrogen.
FT                                {ECO:0000213|PDB:1MY6}.
FT   METAL       162    162       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       162    162       Iron. {ECO:0000213|PDB:1MY6}.
FT   METAL       166    166       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       166    166       Iron; via tele nitrogen.
FT                                {ECO:0000213|PDB:1MY6}.
SQ   SEQUENCE   200 AA;  22216 MW;  666877141AEE800B CRC64;
     MAFVQEPLPF DPGALEPYGM SAKTLEFHYG KHHKGYVDNL NKLTQDTELA DKSLEDVIRT
     TYGDAAKVGI FNNAAQVWNH TFFWNSLKPG GGGVPTGDVA ARINSAFGSY DEFKAQFKNA
     AATQFGSGWA WLVLEAGTLK VTKTANAENP LVHGQVPLLT IDVWEHAYYL DYQNRRPDFI
     DNFLNQLVNW DFVAKNLAAA
//
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