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Database: UniProt/TrEMBL
Entry: A0A0A8UXA1_LEGHA
LinkDB: A0A0A8UXA1_LEGHA
Original site: A0A0A8UXA1_LEGHA 
ID   A0A0A8UXA1_LEGHA        Unreviewed;       192 AA.
AC   A0A0A8UXA1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   07-JUN-2017, entry version 14.
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:CEK12121.1};
GN   ORFNames=LHA_3136 {ECO:0000313|EMBL:CEK12121.1};
OS   Legionella hackeliae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=449 {ECO:0000313|EMBL:CEK12121.1, ECO:0000313|Proteomes:UP000032803};
RN   [1] {ECO:0000313|EMBL:CEK12121.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC35250 {ECO:0000313|EMBL:CEK12121.1};
RA   GOMEZ-VALERO Laura;
RL   Submitted (SEP-2014) 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: 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; LN681225; CEK12121.1; -; Genomic_DNA.
DR   RefSeq; WP_045107195.1; NZ_LNYF01000012.1.
DR   EnsemblBacteria; CEK12121; CEK12121; LHA_3136.
DR   KEGG; lha:LHA_3136; -.
DR   PATRIC; fig|449.7.peg.1665; -.
DR   KO; K04564; -.
DR   Proteomes; UP000032803; 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   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   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:UP000032803};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:CEK12121.1}.
FT   DOMAIN        4     82       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       89    189       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       157    157       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   192 AA;  21666 MW;  B72012704D3F0855 CRC64;
     MAITLPQLPY AMDALEPHIS KETLEYHYGK HHSAYVTNLN KLIPGTEFEN LSLEDIIKKS
     SGGIFNNAAQ VWNHTFYWHC LSPNGGGEPT GKIGDAIGKH FGSFEKFKEE FSQVAATTFG
     SGWAWLVQDK NSSLKIINTS NAGTPMTEGL QALLTCDVWE HAYYIDYRNV RPDYIKAFWS
     LVNWEFVASN LR
//
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