GenomeNet

Database: UniProt
Entry: Q9Y1B0
LinkDB: Q9Y1B0
Original site: Q9Y1B0 
ID   SODF_PLAMA              Reviewed;         198 AA.
AC   Q9Y1B0;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   26-NOV-2014, entry version 57.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
DE   AltName: Full=FeSOD;
GN   Name=SODB;
OS   Plasmodium malariae.
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=5858;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10599926; DOI=10.1007/s004360050675;
RA   Baert C.B., Deloron P., Viscogliosi E., Delgado-Viscogliosi P.,
RA   Camus D., Dive D.;
RT   "Cloning and characterization of iron-containing superoxide dismutase
RT   from the human malaria species Plasmodium ovale, P. malariae and P.
RT   vivax.";
RL   Parasitol. Res. 85:1018-1024(1999).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF139528; AAD43523.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q9Y1B0; -.
DR   SMR; Q9Y1B0; 2-198.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN         1    198       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000290113.
FT   METAL        27     27       Iron. {ECO:0000250}.
FT   METAL        74     74       Iron. {ECO:0000250}.
FT   METAL       158    158       Iron. {ECO:0000250}.
FT   METAL       162    162       Iron. {ECO:0000250}.
SQ   SEQUENCE   198 AA;  22602 MW;  E24F368D2EA6C713 CRC64;
     MVITLPKLKY ALNALSPHIS EETLNFHYNK HHAGYVNKLN TLIKDTPFAE KSLLDIVKES
     SGAIFNNAAQ IWNHTFYWDS MGPDCGGEPH GGIKEKIQED FGSFNNFKEQ FSNILCGHFG
     SGWGWLALNN NNKLVILQTH DAGNPIKDNT GIPILTCDIW EHAYCIDYRN DRASYVKAWW
     NLVNWNFANE NLKKAMQK
//
DBGET integrated database retrieval system