SODF_SULAC
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 03-AUG-2022, entry version 133.
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 / NBRC
OS 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 the
RT 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 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 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 family.
CC {ECO:0000305}.
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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 AlphaFoldDB; Q08713; -.
DR SMR; Q08713; -.
DR STRING; 330779.Saci_0195; -.
DR PRIDE; Q08713; -.
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 HOGENOM; CLU_031625_2_2_2; -.
DR OMA; KWGSFDK; -.
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; 3.55.40.20; -; 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; Cytoplasm; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..211
FT /note="Superoxide dismutase [Fe]"
FT /id="PRO_0000160009"
FT BINDING 34
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 85
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 171
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 175
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT TURN 19..25
FT /evidence="ECO:0007829|PDB:1B06"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:1B06"
FT HELIX 38..58
FT /evidence="ECO:0007829|PDB:1B06"
FT HELIX 68..90
FT /evidence="ECO:0007829|PDB:1B06"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1B06"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:1B06"
FT HELIX 117..130
FT /evidence="ECO:0007829|PDB:1B06"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:1B06"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1B06"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:1B06"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1B06"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:1B06"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:1B06"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:1B06"
FT HELIX 185..192
FT /evidence="ECO:0007829|PDB:1B06"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1B06"
FT HELIX 198..206
FT /evidence="ECO:0007829|PDB:1B06"
FT TURN 207..210
FT /evidence="ECO:0007829|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
