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Database: UniProt
Entry: W7B519_9LIST
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ID   W7B519_9LIST            Unreviewed;       202 AA.
AC   W7B519;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   16-JAN-2019, entry version 20.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=MAQA_12601 {ECO:0000313|EMBL:EUJ17831.1};
OS   Listeria aquatica FSL S10-1188.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1265818 {ECO:0000313|EMBL:EUJ17831.1};
RN   [1] {ECO:0000313|EMBL:EUJ17831.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL S10-1188 {ECO:0000313|EMBL:EUJ17831.1};
RX   PubMed=24599893; DOI=10.1099/ijs.0.052720-0;
RA   den Bakker H.C., Warchocki S., Wright E.M., Allred A.F., Ahlstrom C.,
RA   Manuel C.S., Stasiewicz M.J., Burrell A., Roof S., Strawn L.,
RA   Fortes E.D., Nightingale K.K., Kephart D., Wiedmann M.;
RT   "Listeria floridensis sp. nov., Listeria aquatica sp. nov., Listeria
RT   cornellensis sp. nov., Listeria riparia sp. nov. and Listeria
RT   grandensis sp. nov., from agricultural and natural environments.";
RL   Int. J. Syst. Evol. Microbiol. 64:1882-1889(2014).
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:EUJ17831.1}.
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DR   EMBL; AOCG01000012; EUJ17831.1; -; Genomic_DNA.
DR   RefSeq; WP_036073760.1; NZ_AOCG01000012.1.
DR   EnsemblBacteria; EUJ17831; EUJ17831; MAQA_12601.
DR   PATRIC; fig|1265818.5.peg.2535; -.
DR   OrthoDB; 1440645at2; -.
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   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        2     90       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        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   202 AA;  22733 MW;  A0545EF3AEB86BF5 CRC64;
     MAYELPKLPY TYDALEPNFD KETMEIHYTK HHNTYVTKLN DAVKDYPELA SKSVEDLVAD
     LNSVPESIRT AVRNNGGGHA NHSLFWTILS PNGGGEPAGA LKEAIDSTFG SFDAFKEKFA
     AAAAARFGSG WAWLVLKDGK LEIISLPNQD SPLTEGYTPV LGLDVWEHAY YLKFQNRRPE
     YIDTFWNVVN WDEVARRFEA AK
//
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