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Database: UniProt
Entry: Q9X6W9
LinkDB: Q9X6W9
Original site: Q9X6W9 
ID   SODF_AQUPY              Reviewed;         213 AA.
AC   Q9X6W9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   05-DEC-2018, entry version 86.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodB; Synonyms=sod;
OS   Aquifex pyrophilus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=2714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9109405; DOI=10.1016/S0014-5793(97)00262-7;
RA   Lim J.-H., Yu Y.G., Choi I.-G., Ryu J.-R., Ahn B.-Y., Kim S.-H.,
RA   Han Y.S.;
RT   "Cloning and expression of superoxide dismutase from Aquifex
RT   pyrophilus, a hyperthermophilic bacterium.";
RL   FEBS Lett. 406:142-146(1997).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX   PubMed=9236127; DOI=10.1006/jmbi.1997.1105;
RA   Lim J.-H., Yu Y.G., Han Y.S., Cho S., Ahn B.-Y., Kim S.-H., Cho Y.;
RT   "The crystal structure of an Fe-superoxide dismutase from the
RT   hyperthermophile Aquifex pyrophilus at 1.9-A resolution: structural
RT   basis for thermostability.";
RL   J. Mol. Biol. 270:259-274(1997).
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:
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   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC       Note=Binds 1 Fe cation per subunit.;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Highly thermostable. Retains about 70% of its activity after
CC         heating for 60 minutes at 100 degrees Celsius.;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AF152997; AAD34161.1; -; Genomic_DNA.
DR   PDB; 1COJ; X-ray; 1.90 A; A=2-213.
DR   PDBsum; 1COJ; -.
DR   ProteinModelPortal; Q9X6W9; -.
DR   SMR; Q9X6W9; -.
DR   EvolutionaryTrace; Q9X6W9; -.
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; 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   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Iron; Metal-binding; Oxidoreductase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    213       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000159972.
FT   METAL        28     28       Iron.
FT   METAL        82     82       Iron.
FT   METAL       164    164       Iron.
FT   METAL       168    168       Iron.
FT   HELIX        10     12       {ECO:0000244|PDB:1COJ}.
FT   STRAND       18     20       {ECO:0000244|PDB:1COJ}.
FT   HELIX        22     30       {ECO:0000244|PDB:1COJ}.
FT   HELIX        32     48       {ECO:0000244|PDB:1COJ}.
FT   TURN         50     53       {ECO:0000244|PDB:1COJ}.
FT   HELIX        55     57       {ECO:0000244|PDB:1COJ}.
FT   STRAND       60     62       {ECO:0000244|PDB:1COJ}.
FT   HELIX        64     87       {ECO:0000244|PDB:1COJ}.
FT   HELIX        99    108       {ECO:0000244|PDB:1COJ}.
FT   HELIX       112    125       {ECO:0000244|PDB:1COJ}.
FT   STRAND      127    134       {ECO:0000244|PDB:1COJ}.
FT   TURN        136    138       {ECO:0000244|PDB:1COJ}.
FT   STRAND      141    148       {ECO:0000244|PDB:1COJ}.
FT   STRAND      158    164       {ECO:0000244|PDB:1COJ}.
FT   HELIX       167    169       {ECO:0000244|PDB:1COJ}.
FT   HELIX       171    174       {ECO:0000244|PDB:1COJ}.
FT   HELIX       178    187       {ECO:0000244|PDB:1COJ}.
FT   HELIX       191    208       {ECO:0000244|PDB:1COJ}.
SQ   SEQUENCE   213 AA;  24475 MW;  58F392348671855D CRC64;
     MGVHKLEPKD HLKPQNLEGI SNEQIEPHFE AHYKGYVAKY NEIQEKLADQ NFADRSKANQ
     NYSEYRELKV EETFNYMGVV LHELYFGMLT PGGKGEPSEA LKKKIEEDIG GLDACTNELK
     AAAMAFRGWA ILGLDIFSGR LVVNGLDAHN VYNLTGLIPL IVIDTYEHAY YVDYKNKRPP
     YIDAFFKNIN WDVVNERFEK AMKAYEALKD FIK
//
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