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Database: UniProt
Entry: T0P4Q6_PHOTE
LinkDB: T0P4Q6_PHOTE
Original site: T0P4Q6_PHOTE 
ID   T0P4Q6_PHOTE            Unreviewed;       208 AA.
AC   T0P4Q6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-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=B738_18474 {ECO:0000313|EMBL:EQB99331.1};
OS   Photorhabdus temperata subsp. temperata M1021.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=1221520 {ECO:0000313|EMBL:EQB99331.1, ECO:0000313|Proteomes:UP000015813};
RN   [1] {ECO:0000313|EMBL:EQB99331.1, ECO:0000313|Proteomes:UP000015813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1021 {ECO:0000313|EMBL:EQB99331.1,
RC   ECO:0000313|Proteomes:UP000015813};
RX   PubMed=24029767;
RA   Park G.S., Khan A.R., Hong S.J., Jang E.K., Ullah I., Jung B.K.,
RA   Choi J., Yoo N.K., Park K.J., Shin J.H.;
RT   "Draft Genome Sequence of Entomopathogenic Bacterium Photorhabdus
RT   temperata Strain M1021, Isolated from Nematodes.";
RL   Genome Announc. 1:e00747-13(2013).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EQB99331.1}.
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DR   EMBL; AUXQ01000050; EQB99331.1; -; Genomic_DNA.
DR   EnsemblBacteria; EQB99331; EQB99331; B738_18474.
DR   PATRIC; fig|1221520.3.peg.3847; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000015813; Unassembled WGS sequence.
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:UP000015813};
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:UP000015813}.
FT   DOMAIN        2     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    202       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        82     82       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       169    169       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       173    173       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   208 AA;  23561 MW;  FD599030F10D02D1 CRC64;
     MSYSLPSLPY SYDALEPHFD KQTMEIHHTK HHQTYINNAN GALEAFPELA KLDVDDLIQQ
     LDKIPADKRT FVRNNAGGHA NHSLFWKGLK LGTTLQGPLK EAIERDFGSV DSFKEKFEQA
     AATRFGSGWA WLVLKDDGKL AVVSTANQDS PLMGEAISGA SGYPIAGLDV WEHAYYLQYQ
     NRRPDYIKAF WNVVNWDEAA KRYQEKVK
//
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