ID A0A1G8KGJ7_9LACT Unreviewed; 200 AA.
AC A0A1G8KGJ7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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 ORFNames=CJ205_05460 {ECO:0000313|EMBL:PMC58239.1}, SAMN04487994_10119
GN {ECO:0000313|EMBL:SDI42534.1};
OS Dolosicoccus paucivorans.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae;
OC Dolosicoccus.
OX NCBI_TaxID=84521 {ECO:0000313|EMBL:PMC58239.1, ECO:0000313|Proteomes:UP000235682};
RN [1] {ECO:0000313|EMBL:SDI42534.1, ECO:0000313|Proteomes:UP000198903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15742 {ECO:0000313|EMBL:SDI42534.1,
RC ECO:0000313|Proteomes:UP000198903};
RA Cai Z.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PMC58239.1, ECO:0000313|Proteomes:UP000235682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0852 {ECO:0000313|EMBL:PMC58239.1,
RC ECO:0000313|Proteomes:UP000235682};
RA Thomas-White K., Kumar N., Forster S., Putonti C., Lawley T.,
RA Wolfe A.J.;
RT "Bacterial strain isolated from the female urinary microbiota.";
RL Submitted (SEP-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; PNHE01000020; PMC58239.1; -; Genomic_DNA.
DR EMBL; FNEL01000011; SDI42534.1; -; Genomic_DNA.
DR Proteomes; UP000198903; Unassembled WGS sequence.
DR Proteomes; UP000235682; 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:UP000198903,
KW ECO:0000313|Proteomes:UP000235682};
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:UP000198903}.
FT DOMAIN 2 88 Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT DOMAIN 97 197 Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT METAL 27 27 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 81 81 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 200 AA; 22834 MW; 89D5198000944325 CRC64;
MTFKLPELTY AYDALEPVID KETMEIHHSK HHQAYVNNLN AAVEGTEFAE LDLDELMKRI
NEVPADIQTA VRNNGGGHYN HSLFWTLLRA PQEDNRPEGA LLDKIEADFG SFDAFKEAFA
KAAATRFGSG WAWLVDNNGK LEVVSTPNQD NPAMDGLNPL LGLDVWEHTY YLKYQNRRPE
YIDAFFKVVN WDEVAKRFNA
//
