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Database: UniProt/TrEMBL
Entry: E5AMX3_PARRH
LinkDB: E5AMX3_PARRH
Original site: E5AMX3_PARRH 
ID   E5AMX3_PARRH            Unreviewed;       213 AA.
AC   E5AMX3;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   28-MAR-2018, entry version 38.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=RBRH_04037 {ECO:0000313|EMBL:CBW74054.1};
OS   Paraburkholderia rhizoxinica (strain DSM 19002 / CIP 109453 / HKI 454)
OS   (Burkholderia rhizoxinica).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=882378 {ECO:0000313|EMBL:CBW74054.1, ECO:0000313|Proteomes:UP000007437};
RN   [1] {ECO:0000313|EMBL:CBW74054.1, ECO:0000313|Proteomes:UP000007437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19002 / CIP 109453 / HKI 454
RC   {ECO:0000313|Proteomes:UP000007437};
RX   PubMed=21131495; DOI=10.1128/JB.01318-10;
RA   Lackner G., Moebius N., Partida-Martinez L., Hertweck C.;
RT   "Complete genome sequence of Burkholderia rhizoxinica, an endosymbiont
RT   of Rhizopus microsporus.";
RL   J. Bacteriol. 193:783-784(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; FR687359; CBW74054.1; -; Genomic_DNA.
DR   ProteinModelPortal; E5AMX3; -.
DR   STRING; 882378.RBRH_04037; -.
DR   EnsemblBacteria; CBW74054; CBW74054; RBRH_04037.
DR   KEGG; brh:RBRH_04037; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; BRHI882378:GJIB-537-MONOMER; -.
DR   Proteomes; UP000007437; 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:UP000007437};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:CBW74054.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007437}.
FT   DOMAIN       22    102       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      109    209       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        47     47       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        94     94       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       177    177       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       181    181       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   213 AA;  23488 MW;  E9BC2340FA92FD55 CRC64;
     MLGSMTYPGP QFVIKEACTM AQHTLPPLPF AKNALAPHIS EETLEFHYGK HHQAYVTNLN
     NLIPGTEFEN LSLEEIVKRS SGGIFNNAAQ VWNHTFFWNS LSPQGGGAPT GKLGDAINAK
     WGSYDAFKEA FTKVAIGTFG SGWAWLVKKA DGSLDIVSTS NAATPLTTDA TPLLTLDVWE
     HAYYIDYRNA RPKFVDAFWN VVNWDFAAKN FGV
//
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