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Database: UniProt/SWISS-PROT
Entry: SODC_LEGPH
LinkDB: SODC_LEGPH
Original site: SODC_LEGPH 
ID   SODC_LEGPH              Reviewed;         162 AA.
AC   Q5ZT17; P53637;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-OCT-2017, entry version 86.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=sodC; OrderedLocusNames=lpg2348;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 /
OS   ATCC 33152 / DSM 7513).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9086394;
RA   Amemura-Maekawa J., Kura F., Watanabe H.;
RT   "Cloning and nucleotide sequences of iron and copper-zinc superoxide
RT   dismutase genes of Legionella pneumophila and their distribution among
RT   Legionella species.";
RL   Jpn. J. Med. Sci. Biol. 49:167-186(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M.,
RA   Asamani G., Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J.,
RA   Steshenko V., Park S.H., Zhao B., Teplitskaya E., Edwards J.R.,
RA   Pampou S., Georghiou A., Chou I.-C., Iannuccilli W., Ulz M.E.,
RA   Kim D.H., Geringer-Sameth A., Goldsberry C., Morozov P., Fischer S.G.,
RA   Segal G., Qu X., Rzhetsky A., Zhang P., Cayanis E., De Jong P.J.,
RA   Ju J., Kalachikov S., Shuman H.A., Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella
RT   pneumophila.";
RL   Science 305:1966-1968(2004).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
DR   EMBL; D29953; BAA06223.1; -; Genomic_DNA.
DR   EMBL; AE017354; AAU28410.1; -; Genomic_DNA.
DR   RefSeq; WP_010948054.1; NC_002942.5.
DR   RefSeq; YP_096357.1; NC_002942.5.
DR   ProteinModelPortal; Q5ZT17; -.
DR   SMR; Q5ZT17; -.
DR   STRING; 272624.lpg2348; -.
DR   PaxDb; Q5ZT17; -.
DR   EnsemblBacteria; AAU28410; AAU28410; lpg2348.
DR   GeneID; 19833913; -.
DR   KEGG; lpn:lpg2348; -.
DR   PATRIC; fig|272624.6.peg.2468; -.
DR   eggNOG; ENOG4108Z7T; Bacteria.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263449; -.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   Proteomes; UP000000609; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Antioxidant; Complete proteome; Copper; Disulfide bond; Metal-binding;
KW   Oxidoreductase; Periplasm; Reference proteome; Signal; Zinc.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21    162       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000032832.
FT   METAL        66     66       Copper; catalytic. {ECO:0000250}.
FT   METAL        68     68       Copper; catalytic. {ECO:0000250}.
FT   METAL        83     83       Copper; catalytic. {ECO:0000250}.
FT   METAL        83     83       Zinc; structural. {ECO:0000250}.
FT   METAL        92     92       Zinc; structural. {ECO:0000250}.
FT   METAL       100    100       Zinc; structural. {ECO:0000250}.
FT   METAL       103    103       Zinc; structural. {ECO:0000250}.
FT   METAL       137    137       Copper; catalytic. {ECO:0000250}.
FT   DISULFID     73    158       {ECO:0000250}.
SQ   SEQUENCE   162 AA;  17076 MW;  BC3F47DB67445312 CRC64;
     MNKSGIILIG TILFSSMAIA DDLTAPIYTT GPKPVAIGKV TFTQTPYGVL ITPDLTNLPE
     GPHGFHLHKT ADCGNHGMHA EGHYDPQNTN SHQGPYGNGH LGDLPVLYVT SNGKAMIPTL
     APRLKLSDMH NLAVMIHANG DTYSDNPPQG GGGDRIACGV IK
//
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