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Database: UniProt
Entry: B0SK56_LEPBP
LinkDB: B0SK56_LEPBP
Original site: B0SK56_LEPBP 
ID   B0SK56_LEPBP            Unreviewed;       190 AA.
AC   B0SK56;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   16-JAN-2019, entry version 68.
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:ABZ96174.1};
GN   OrderedLocusNames=LEPBI_I0027 {ECO:0000313|EMBL:ABZ96174.1};
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 /
OS   Paris).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ96174.1, ECO:0000313|Proteomes:UP000001847};
RN   [1] {ECO:0000313|EMBL:ABZ96174.1, ECO:0000313|Proteomes:UP000001847}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / ATCC 23582 / Paris
RC   {ECO:0000313|Proteomes:UP000001847};
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C.,
RA   McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z.,
RA   Coppel R.L., Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides
RT   insights into the evolution of Leptospira and the pathogenesis of
RT   leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(2008).
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; CP000786; ABZ96174.1; -; Genomic_DNA.
DR   RefSeq; WP_012387065.1; NC_010602.1.
DR   ProteinModelPortal; B0SK56; -.
DR   STRING; 456481.LEPBI_I0027; -.
DR   EnsemblBacteria; ABZ96174; ABZ96174; LEPBI_I0027.
DR   GeneID; 35831543; -.
DR   KEGG; lbi:LEPBI_I0027; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; LBIF456481:LEPBI_RS00150-MONOMER; -.
DR   Proteomes; UP000001847; Chromosome I.
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:UP000001847};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:ABZ96174.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001847}.
FT   DOMAIN        2     82       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       89    188       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        74     74       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       156    156       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       160    160       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   190 AA;  21285 MW;  3A72B4CA06CC9EA0 CRC64;
     MEHKLPELPY AKDALAPHIS AETLEFHYGK HHQTYITNLN NLIKGTEFES ASLEDIVKKS
     SGGIFNNAAQ VWNHTFYWHS LSPNGGGAPK GAVADLITKS FGSFDAFKEK FTQSAVTNFG
     SGWTWLVKKG DGLEIVNTSN AGSPLKDGMQ ALLTIDVWEH AYYIDFRNAR PKYVEAFWNL
     VNWDFANKNL
//
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