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Database: UniProt
Entry: Q08713
LinkDB: Q08713
Original site: Q08713 
ID   SODF_SULAC              Reviewed;         211 AA.
AC   Q08713; Q4JC65;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JAN-2019, entry version 120.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sod; Synonyms=sodF; OrderedLocusNames=Saci_0195;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 /
OS   NBRC 15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8334170; DOI=10.1016/0167-4781(93)90099-Y;
RA   Klenk H.-P., Schleper C., Schwass V., Brudler R.;
RT   "Nucleotide sequence, transcription and phylogeny of the gene encoding
RT   the superoxide dismutase of Sulfolobus acidocaldarius.";
RL   Biochim. Biophys. Acta 1174:95-98(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=9878438; DOI=10.1006/jmbi.1998.2344;
RA   Knapp S., Kardinahl S., Hellgren N., Tibbelin G., Schaefer G.,
RA   Ladenstein R.;
RT   "Refined crystal structure of a superoxide dismutase from the
RT   hyperthermophilic archaeon Sulfolobus acidocaldarius at 2.2-A
RT   resolution.";
RL   J. Mol. Biol. 285:689-702(1999).
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   -!- SUBUNIT: Homotetramer at high temperature; homodimer at room
CC       temperature.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; X63386; CAA44993.1; -; Genomic_DNA.
DR   EMBL; CP000077; AAY79614.1; -; Genomic_DNA.
DR   PIR; S34616; S34616.
DR   RefSeq; WP_011277115.1; NC_007181.1.
DR   PDB; 1B06; X-ray; 2.20 A; A/B/C/D/E/F=2-211.
DR   PDBsum; 1B06; -.
DR   ProteinModelPortal; Q08713; -.
DR   SMR; Q08713; -.
DR   STRING; 330779.Saci_0195; -.
DR   EnsemblBacteria; AAY79614; AAY79614; Saci_0195.
DR   GeneID; 3474008; -.
DR   KEGG; sai:Saci_0195; -.
DR   PATRIC; fig|330779.12.peg.187; -.
DR   eggNOG; arCOG04147; Archaea.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; 74803at2157; -.
DR   BioCyc; SACI330779:G1G4L-189-MONOMER; -.
DR   BRENDA; 1.15.1.1; 6160.
DR   EvolutionaryTrace; Q08713; -.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; 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   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; Cytoplasm; Iron; Metal-binding;
KW   Oxidoreductase; Reference proteome.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    211       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000160009.
FT   METAL        34     34       Iron.
FT   METAL        85     85       Iron.
FT   METAL       171    171       Iron.
FT   METAL       175    175       Iron.
FT   TURN         19     25       {ECO:0000244|PDB:1B06}.
FT   HELIX        28     36       {ECO:0000244|PDB:1B06}.
FT   HELIX        38     58       {ECO:0000244|PDB:1B06}.
FT   HELIX        68     90       {ECO:0000244|PDB:1B06}.
FT   TURN         95     97       {ECO:0000244|PDB:1B06}.
FT   HELIX       104    114       {ECO:0000244|PDB:1B06}.
FT   HELIX       117    130       {ECO:0000244|PDB:1B06}.
FT   STRAND      133    141       {ECO:0000244|PDB:1B06}.
FT   TURN        143    145       {ECO:0000244|PDB:1B06}.
FT   STRAND      148    154       {ECO:0000244|PDB:1B06}.
FT   TURN        155    157       {ECO:0000244|PDB:1B06}.
FT   STRAND      166    171       {ECO:0000244|PDB:1B06}.
FT   HELIX       174    176       {ECO:0000244|PDB:1B06}.
FT   HELIX       178    181       {ECO:0000244|PDB:1B06}.
FT   HELIX       185    192       {ECO:0000244|PDB:1B06}.
FT   HELIX       193    195       {ECO:0000244|PDB:1B06}.
FT   HELIX       198    206       {ECO:0000244|PDB:1B06}.
FT   TURN        207    210       {ECO:0000244|PDB:1B06}.
SQ   SEQUENCE   211 AA;  24266 MW;  184829345CC5D13D CRC64;
     MTQVIQLKRY EFPQLPYKVD ALEPYISKDI IDVHYNGHHK GYVNGANSLL DRLEKLIKGD
     LPQGQYDLQG ILRGLTFNIN GHKLHAIYWN NMAPAGKGGG KPGGALADLI NKQYGSFDRF
     KQVFSESANS LPGSGWTVLY YDNESGNLQI MTVENHFMNH IAELPVILIV DEFEHAYYLQ
     YKNKRGDYLN AWWNVVNWDD AEKRLQKYLN K
//
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