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Database: UniProt/TrEMBL
Entry: A0A097BDD1_LISIV
LinkDB: A0A097BDD1_LISIV
Original site: A0A097BDD1_LISIV 
ID   A0A097BDD1_LISIV        Unreviewed;       202 AA.
AC   A0A097BDD1;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   28-MAR-2018, entry version 14.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=JL58_07560 {ECO:0000313|EMBL:AIS59845.1};
OS   Listeria ivanovii subsp. londoniensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=202752 {ECO:0000313|EMBL:AIS59845.1, ECO:0000313|Proteomes:UP000029667};
RN   [1] {ECO:0000313|EMBL:AIS59845.1, ECO:0000313|Proteomes:UP000029667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSLC 30167 {ECO:0000313|EMBL:AIS59845.1};
RX   PubMed=25614561;
RA   Hupfeld M., Fouts D.E., Loessner M.J., Klumpp J.;
RT   "Genome Sequences of the Listeria ivanovii subsp. ivanovii Type Strain
RT   and Two Listeria ivanovii subsp. londoniensis Strains.";
RL   Genome Announc. 3:0-0(2015).
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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; CP009575; AIS59845.1; -; Genomic_DNA.
DR   RefSeq; WP_003719733.1; NZ_CP009576.1.
DR   EnsemblBacteria; AIS59845; AIS59845; JL58_07560.
DR   KEGG; lia:JL58_07560; -.
DR   KEGG; lio:JL53_08030; -.
DR   KO; K04564; -.
DR   Proteomes; UP000029667; Chromosome.
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:UP000029667};
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;  22612 MW;  2B8C900598D6F7FD CRC64;
     MTYELPKLPY TYDALEPNFD KETMEIHYTK HHNTYVTKLN EAVAGHADLA SKPVEELVAN
     LDSVPEDIRG AVRNHGGGHA NHTLFWSILS PNGGGAPTGN LKAAIESEFG TFDEFKEKFN
     AAAAARFGSG WAWLVVNNGK LEIVSTANQD SPLSEGKTPV LGLDVWEHAY YLKFQNRRPE
     YIDTFWNVIN WEEANKRFDA AK
//
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