ID A0A0C2BYK6_9BURK Unreviewed; 243 AA.
AC A0A0C2BYK6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 05-DEC-2018, entry version 18.
DE RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN ORFNames=BurMR1_1351 {ECO:0000313|EMBL:KIG01766.1};
OS Burkholderia sp. MR1.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=870478 {ECO:0000313|EMBL:KIG01766.1, ECO:0000313|Proteomes:UP000031560};
RN [1] {ECO:0000313|EMBL:KIG01766.1, ECO:0000313|Proteomes:UP000031560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR1 {ECO:0000313|EMBL:KIG01766.1,
RC ECO:0000313|Proteomes:UP000031560};
RA Pawitwar S., Utturkar S.M., Brown S.D., Yoshinaga M., Rosen B.P.;
RT "Draft Genome Sequence of Burkholderia sp. MR1.";
RL Submitted (DEC-2014) 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:KIG01766.1}.
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DR EMBL; JWHM01000057; KIG01766.1; -; Genomic_DNA.
DR RefSeq; WP_052450160.1; NZ_JWHM01000057.1.
DR EnsemblBacteria; KIG01766; KIG01766; BurMR1_1351.
DR GeneID; 34433002; -.
DR PATRIC; fig|870478.3.peg.5534; -.
DR Proteomes; UP000031560; 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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Complete proteome {ECO:0000313|Proteomes:UP000031560};
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:UP000031560};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}.
FT CHAIN 29 243 Superoxide dismutase. {ECO:0000256|SAM:
FT SignalP}.
FT /FTId=PRO_5002146321.
FT DOMAIN 45 124 Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT DOMAIN 131 232 Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT COILED 81 101 {ECO:0000256|SAM:Coils}.
FT METAL 69 69 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 117 117 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 200 200 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 204 204 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ SEQUENCE 243 AA; 26826 MW; AA70C164FEAE051E CRC64;
MATRRTFLHD TAALGAGLLM TNAQSADAAE NAGYVDKLTD ADGKYAAAPL PYAYDALEPV
IDARTVELHY DFHHKPAVAA ANKAEEALAK ARDTNDFALV KHHEKELAFQ LSSHLLHTVY
WTSISGKGGE PKNELAKAID KSFGSYAKFK AQLVAATVAT EASGWGVVGY HPAMDKVMIL
QCENHQKLTA WGVQPILVLD VFEHAYYLKY QNRRNEYVNQ LFNIVNWDNA SMRLRAAMSA
RSA
//
