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Database: UniProt
Entry: P53641
LinkDB: P53641
Original site: P53641 
ID   SODF_PSEAE              Reviewed;         193 AA.
AC   P53641;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   29-OCT-2014, entry version 100.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodB; OrderedLocusNames=PA4366;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG
OS   12228).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8244935;
RA   Hassett D.J., Woodruff W.A., Wozniak D.J., Vasil M.L., Cohen M.S.,
RA   Ohman D.E.;
RT   "Cloning and characterization of the Pseudomonas aeruginosa sodA and
RT   sodB genes encoding manganese- and iron-cofactored superoxide
RT   dismutase: demonstration of increased manganese superoxide dismutase
RT   activity in alginate-producing bacteria.";
RL   J. Bacteriol. 175:7658-7665(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
RA   Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT   opportunistic pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR: Binds 1 iron ion per subunit. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
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DR   EMBL; L25675; AAA16786.1; -; Unassigned_DNA.
DR   EMBL; AE004091; AAG07754.1; -; Genomic_DNA.
DR   PIR; B53294; B53294.
DR   PIR; E83100; E83100.
DR   RefSeq; NP_253056.1; NC_002516.2.
DR   ProteinModelPortal; P53641; -.
DR   SMR; P53641; 2-191.
DR   STRING; 208964.PA4366; -.
DR   EnsemblBacteria; AAG07754; AAG07754; PA4366.
DR   GeneID; 881397; -.
DR   KEGG; pae:PA4366; -.
DR   PATRIC; 19843453; VBIPseAer58763_4573.
DR   PseudoCAP; PA4366; -.
DR   eggNOG; COG0605; -.
DR   HOGENOM; HOG000013584; -.
DR   InParanoid; P53641; -.
DR   KO; K04564; -.
DR   OMA; EGTEHAG; -.
DR   OrthoDB; EOG63NMNT; -.
DR   PhylomeDB; P53641; -.
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   PANTHER; PTHR11404; PTHR11404; 1.
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; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    193       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000159994.
FT   METAL        27     27       Iron. {ECO:0000250}.
FT   METAL        74     74       Iron. {ECO:0000250}.
FT   METAL       157    157       Iron. {ECO:0000250}.
FT   METAL       161    161       Iron. {ECO:0000250}.
FT   CONFLICT     30     31       KH -> NN (in Ref. 1; AAA16786).
FT                                {ECO:0000305}.
FT   CONFLICT     40     40       N -> T (in Ref. 1; AAA16786).
FT                                {ECO:0000305}.
FT   CONFLICT     92     92       A -> G (in Ref. 1; AAA16786).
FT                                {ECO:0000305}.
FT   CONFLICT    100    100       A -> G (in Ref. 1; AAA16786).
FT                                {ECO:0000305}.
FT   CONFLICT    118    123       TFGSGW -> HLRFRS (in Ref. 1; AAA16786).
FT                                {ECO:0000305}.
FT   CONFLICT    130    130       A -> P (in Ref. 1; AAA16786).
FT                                {ECO:0000305}.
FT   CONFLICT    169    176       NLRPKYVE -> TASEVRR (in Ref. 1;
FT                                AAA16786). {ECO:0000305}.
SQ   SEQUENCE   193 AA;  21351 MW;  81A0FB516972188C CRC64;
     MAFELPPLPY EKNALEPHIS AETLEYHHDK HHNTYVVNLN NLIPGTEFEG KSLEEIVKSS
     SGGIFNNAAQ VWNHTFYWNC LSPNGGGQPT GALADAINAA FGSFDKFKEE FTKTSVGTFG
     SGWGWLVKKA DGSLALASTI GAGNPLTSGD TPLLTCDVWE HAYYIDYRNL RPKYVEAFWN
     LVNWDFVAKN FAA
//
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