ID A0A0Q5PW03_9BURK Unreviewed; 193 AA.
AC A0A0Q5PW03;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 16-JAN-2019, entry version 13.
DE RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN ORFNames=ASG35_27015 {ECO:0000313|EMBL:KQR85443.1};
OS Burkholderia sp. Leaf177.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1736287 {ECO:0000313|EMBL:KQR85443.1, ECO:0000313|Proteomes:UP000051826};
RN [1] {ECO:0000313|EMBL:KQR85443.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR85443.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR85443.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR85443.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:
CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:18421; EC=1.15.1.1;
CC Evidence={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:KQR85443.1}.
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DR EMBL; LMPF01000004; KQR85443.1; -; Genomic_DNA.
DR RefSeq; WP_056355096.1; NZ_LMPF01000004.1.
DR EnsemblBacteria; KQR85443; KQR85443; ASG35_27015.
DR Proteomes; UP000051826; 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:UP000051826};
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:UP000051826}.
FT DOMAIN 2 82 Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT DOMAIN 89 189 Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT METAL 27 27 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 74 74 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 157 157 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 161 161 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ SEQUENCE 193 AA; 21456 MW; C2D35E1117BF791B CRC64;
MEHTLPPLPF EKNALAPNMS EETLEYHYGK HHQTYVTNLN KLIPGTEFEN LSLEEIVKKA
SGGVFNNAAQ VWNHTFFWNS LSPKGGGAPA GALADAINAK YGSFDKFKEE FAKVATGTFG
SGWTWLVKKT DGSLDIVSTS NAATPLTTDA KALLTIDVWE HAYYIDYRNA RPKFIEAFWN
IANWEFASKN FGA
//
