ID A0A1X6Y9P5_9RHOB Unreviewed; 199 AA.
AC A0A1X6Y9P5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 16-JAN-2019, entry version 7.
DE RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN Name=sodB {ECO:0000313|EMBL:SLN14949.1};
GN ORFNames=RUM8411_00388 {ECO:0000313|EMBL:SLN14949.1};
OS Ruegeria meonggei.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Ruegeria.
OX NCBI_TaxID=1446476 {ECO:0000313|EMBL:SLN14949.1, ECO:0000313|Proteomes:UP000193778};
RN [1] {ECO:0000313|EMBL:SLN14949.1, ECO:0000313|Proteomes:UP000193778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8411 {ECO:0000313|EMBL:SLN14949.1,
RC ECO:0000313|Proteomes:UP000193778};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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}.
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DR EMBL; FWFP01000001; SLN14949.1; -; Genomic_DNA.
DR Proteomes; UP000193778; 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:UP000193778};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW ECO:0000256|RuleBase:RU000414};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW ECO:0000313|EMBL:SLN14949.1}.
FT DOMAIN 3 89 Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT DOMAIN 98 198 Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT METAL 28 28 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 82 82 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 164 164 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 168 168 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ SEQUENCE 199 AA; 21972 MW; DFC22A56F8DB2F4D CRC64;
MAFELPDLPY AHDALAAKGM SAETLEYHHD LHHKAYVDNG NKLIAGTEWD GKSLEEIITG
TYDANAVAQN GIFNNISQLW NHNQFWEMMG PGGAAMPGEL EKALTESFGS VDEFKSQFSA
AGAGQFGSGW AWLVKNTDGS LAVTKTENGV NPLCFGQTAL LGCDVWEHSY YIDFRNKRPA
YLSNFLDNLV NWENVASRM
//
