ID A0A0M6Z9S8_9RHOB Unreviewed; 200 AA.
AC A0A0M6Z9S8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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 Name=sodB {ECO:0000313|EMBL:CTQ64392.1};
GN ORFNames=LA5096_00367 {ECO:0000313|EMBL:CTQ64392.1};
OS Labrenzia alba.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Labrenzia.
OX NCBI_TaxID=311410 {ECO:0000313|EMBL:CTQ64392.1, ECO:0000313|Proteomes:UP000049983};
RN [1] {ECO:0000313|EMBL:CTQ64392.1, ECO:0000313|Proteomes:UP000049983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5096 {ECO:0000313|EMBL:CTQ64392.1,
RC ECO:0000313|Proteomes:UP000049983};
RA Noorani M.;
RL Submitted (JUL-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}.
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DR EMBL; CXWC01000001; CTQ64392.1; -; Genomic_DNA.
DR RefSeq; WP_055116253.1; NZ_CXWE01000004.1.
DR EnsemblBacteria; CTQ64392; CTQ64392; LA5096_00367.
DR OrthoDB; 1440645at2; -.
DR Proteomes; UP000049983; 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:UP000049983};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW ECO:0000256|RuleBase:RU000414};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW ECO:0000313|EMBL:CTQ64392.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000049983}.
FT DOMAIN 2 85 Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT DOMAIN 95 191 Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT METAL 27 27 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 77 77 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 160 160 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 164 164 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ SEQUENCE 200 AA; 22197 MW; 9EADF343BD5AD05B CRC64;
MSFELPDLPY AYDALAPYMS SETLEFHHDK HHQAYVTKGN ELLAGSGLEG KSLEEIVKAS
FGSNAPLFNN AGQHYNHIHF WKWMKKNGGG TSLPGAIASA IDSDLGGYDK FRADFIAAGM
GQFGSGWAWL AVKDGKLAIM KTPNGENPLV HGAVPVLGCD VWEHSYYIDY RNARPKYLEA
FVDNMVNWDY VLELYEAATK
//
