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Database: UniProt
Entry: D4GGH3_PANAM
LinkDB: D4GGH3_PANAM
Original site: D4GGH3_PANAM 
ID   D4GGH3_PANAM            Unreviewed;       210 AA.
AC   D4GGH3;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   28-MAR-2018, entry version 43.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodA {ECO:0000313|EMBL:ADD75274.1};
GN   OrderedLocusNames=PANA_0107 {ECO:0000313|EMBL:ADD75274.1};
OS   Pantoea ananatis (strain LMG 20103).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD75274.1, ECO:0000313|Proteomes:UP000001702};
RN   [1] {ECO:0000313|EMBL:ADD75274.1, ECO:0000313|Proteomes:UP000001702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD75274.1,
RC   ECO:0000313|Proteomes:UP000001702};
RX   PubMed=20348253; DOI=10.1128/JB.00060-10;
RA   De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R.,
RA   Joubert F., Coutinho T.A.;
RT   "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT   Eucalyptus blight and dieback.";
RL   J. Bacteriol. 192:2936-2937(2010).
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; CP001875; ADD75274.1; -; Genomic_DNA.
DR   ProteinModelPortal; D4GGH3; -.
DR   STRING; 706191.PANA_0107; -.
DR   EnsemblBacteria; ADD75274; ADD75274; PANA_0107.
DR   KEGG; pam:PANA_0107; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000001702; 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   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:UP000001702};
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:UP000001702}.
FT   DOMAIN        7     93       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      100    205       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        32     32       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        86     86       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       172    172       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       176    176       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   210 AA;  23560 MW;  8BBC1E0A1D615A7E CRC64;
     MERKNMSYSL PSLPYAYDAL EPHFDKQTME IHHTKHHQTY VNNANAALEG TEFADLPVDE
     LITKLDQLPA DKKGPLRNNA GGHANHSLFW KGLKTGTTLQ GELKAAIEKD FGSVEKFQEE
     FEKAATTRFG SGWAWLVKKG DKLAVVSTAN QDNPLMGEAV AGVSGYPIIG LDVWEHAYYL
     KYQNKRPDYI KAFWNVVNWD EAAARFASAK
//
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