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Database: UniProt
Entry: O93724
LinkDB: O93724
Original site: O93724 
ID   SODF_PYRAE              Reviewed;         211 AA.
AC   O93724;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   16-JAN-2019, entry version 121.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sod; OrderedLocusNames=PAE0274;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630
OS   / NBRC 100827).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
OC   Thermoproteaceae; Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827;
RA   Baikalov C.J., Slupska M.M., Miller J.H.;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-211, AND SUBUNIT.
RX   PubMed=14646077; DOI=10.1107/S0907444903019942;
RA   Lee S., Sawaya M.R., Eisenberg D.;
RT   "Structure of superoxide dismutase from Pyrobaculum aerophilum
RT   presents a challenging case in molecular replacement with multiple
RT   molecules, pseudo-symmetry and twinning.";
RL   Acta Crystallogr. D 59:2191-2199(2003).
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; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:14646077}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; U82371; AAD00533.2; -; Genomic_DNA.
DR   EMBL; AE009441; AAL62675.1; -; Genomic_DNA.
DR   PDB; 1P7G; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=2-211.
DR   PDB; 3EVK; X-ray; 1.85 A; A/B/C/D=2-211.
DR   PDBsum; 1P7G; -.
DR   PDBsum; 3EVK; -.
DR   ProteinModelPortal; O93724; -.
DR   SMR; O93724; -.
DR   STRING; 178306.PAE0274; -.
DR   PRIDE; O93724; -.
DR   EnsemblBacteria; AAL62675; AAL62675; PAE0274.
DR   KEGG; pai:PAE0274; -.
DR   PATRIC; fig|178306.9.peg.201; -.
DR   eggNOG; arCOG04147; Archaea.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   InParanoid; O93724; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   BRENDA; 1.15.1.1; 5239.
DR   EvolutionaryTrace; O93724; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
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   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   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    211       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000160008.
FT   METAL        31     31       Iron. {ECO:0000250}.
FT   METAL        79     79       Iron. {ECO:0000250}.
FT   METAL       165    165       Iron. {ECO:0000250}.
FT   METAL       169    169       Iron. {ECO:0000250}.
FT   TURN         16     22       {ECO:0000244|PDB:1P7G}.
FT   HELIX        25     33       {ECO:0000244|PDB:1P7G}.
FT   HELIX        35     54       {ECO:0000244|PDB:1P7G}.
FT   HELIX        62     82       {ECO:0000244|PDB:1P7G}.
FT   TURN         83     85       {ECO:0000244|PDB:1P7G}.
FT   STRAND       92     94       {ECO:0000244|PDB:1P7G}.
FT   HELIX        98    108       {ECO:0000244|PDB:1P7G}.
FT   HELIX       111    123       {ECO:0000244|PDB:1P7G}.
FT   STRAND      126    136       {ECO:0000244|PDB:1P7G}.
FT   TURN        137    140       {ECO:0000244|PDB:1P7G}.
FT   STRAND      141    148       {ECO:0000244|PDB:1P7G}.
FT   TURN        149    151       {ECO:0000244|PDB:1P7G}.
FT   STRAND      159    165       {ECO:0000244|PDB:1P7G}.
FT   HELIX       168    170       {ECO:0000244|PDB:1P7G}.
FT   HELIX       172    175       {ECO:0000244|PDB:1P7G}.
FT   HELIX       179    186       {ECO:0000244|PDB:1P7G}.
FT   HELIX       187    189       {ECO:0000244|PDB:1P7G}.
FT   HELIX       192    203       {ECO:0000244|PDB:1P7G}.
SQ   SEQUENCE   211 AA;  24204 MW;  F5943D397DD31561 CRC64;
     MVTTKRYTLP PLPYAYNALE PYISAEIMQL HHQKHHQGYV NGANAALEKL EKFRKGEAQI
     DIRAVLRDLS FHLNGHILHS IFWPNMAPPG KGGGKPGGKI ADLINKFFGS FEKFKEEFSQ
     AAKNVEGVGW AILVYEPLEE QLLILQIEKH NLMHAADAQV LLALDVWEHA YYLQYKNDRG
     SYVDNWWNVV NWDDVERRLQ KALNGQIALK L
//
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