ID A0A1E5UDY8_9FLAO Unreviewed; 252 AA.
AC A0A1E5UDY8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 05-DEC-2018, entry version 8.
DE RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN ORFNames=BHF72_2410 {ECO:0000313|EMBL:OEL11139.1};
OS Cloacibacterium normanense.
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=237258 {ECO:0000313|EMBL:OEL11139.1, ECO:0000313|Proteomes:UP000095601};
RN [1] {ECO:0000313|EMBL:OEL11139.1, ECO:0000313|Proteomes:UP000095601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRS-1 {ECO:0000313|EMBL:OEL11139.1,
RC ECO:0000313|Proteomes:UP000095601};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) 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:OEL11139.1}.
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DR EMBL; MKGI01000053; OEL11139.1; -; Genomic_DNA.
DR RefSeq; WP_069798735.1; NZ_MKGI01000053.1.
DR EnsemblBacteria; OEL11139; OEL11139; BHF72_2410.
DR PATRIC; fig|237258.4.peg.2570; -.
DR Proteomes; UP000095601; 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; 2.
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:UP000095601};
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:UP000095601};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}.
FT CHAIN 23 252 Superoxide dismutase. {ECO:0000256|SAM:
FT SignalP}.
FT /FTId=PRO_5009186865.
FT DOMAIN 52 133 Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT DOMAIN 141 244 Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT METAL 76 76 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 126 126 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 213 213 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 217 217 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ SEQUENCE 252 AA; 28003 MW; 6FE2E3A051A10070 CRC64;
MKKLVQWAFV AIAFSAVTSC VAVVGNTAQP VVNVESTDYG KPSDVTANAG AFKIKTLKHN
YDAFSKYVDA KTMYIHFSKH YVGYLNNLNK AVEGKPQVNM TIEEVLKTLD TSNAALRNNA
GGYYNHNLYF DLMTPNSTGK PTGKLADAIN RDFGSFENFK KQFSDAGAKQ FGSGWAWLVT
DASGKLKVGS TPNQDNPLMP GMSISGTPVL AMDVWEHAYY LKYQNKRADY IEAFFNVIDW
NVVSDYYEKA MK
//
