SODF_PYRAE
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 03-AUG-2022, entry version 132.
DE RecName: Full=Superoxide dismutase [Fe];
DE EC=1.15.1.1;
GN Name=sod; OrderedLocusNames=PAE0274;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
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 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
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 presents a
RT challenging case in molecular replacement with multiple molecules, pseudo-
RT 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 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 family.
CC {ECO:0000305}.
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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 AlphaFoldDB; O93724; -.
DR SMR; O93724; -.
DR STRING; 178306.PAE0274; -.
DR EnsemblBacteria; AAL62675; AAL62675; PAE0274.
DR KEGG; pai:PAE0274; -.
DR PATRIC; fig|178306.9.peg.201; -.
DR eggNOG; arCOG04147; Archaea.
DR HOGENOM; CLU_031625_2_2_2; -.
DR InParanoid; O93724; -.
DR OMA; KWGSFDK; -.
DR BRENDA; 1.15.1.1; 5239.
DR EvolutionaryTrace; O93724; -.
DR Proteomes; UP000002439; Chromosome.
DR GO; GO:0030145; F:manganese 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; 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; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..211
FT /note="Superoxide dismutase [Fe]"
FT /id="PRO_0000160008"
FT BINDING 31
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT TURN 16..22
FT /evidence="ECO:0007829|PDB:1P7G"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:1P7G"
FT HELIX 35..54
FT /evidence="ECO:0007829|PDB:1P7G"
FT HELIX 62..82
FT /evidence="ECO:0007829|PDB:1P7G"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1P7G"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1P7G"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:1P7G"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:1P7G"
FT STRAND 126..136
FT /evidence="ECO:0007829|PDB:1P7G"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:1P7G"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:1P7G"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:1P7G"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:1P7G"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1P7G"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:1P7G"
FT HELIX 179..186
FT /evidence="ECO:0007829|PDB:1P7G"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1P7G"
FT HELIX 192..203
FT /evidence="ECO:0007829|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
