SODF_AQUPY
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 03-AUG-2022, entry version 95.
DE RecName: Full=Superoxide dismutase [Fe] {ECO:0000305};
DE Short=Fe-SOD {ECO:0000303|PubMed:9109405};
DE EC=1.15.1.1 {ECO:0000269|PubMed:9109405};
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], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP AND SUBUNIT.
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., Han Y.S.;
RT "Cloning and expression of superoxide dismutase from Aquifex pyrophilus, a
RT hyperthermophilic bacterium.";
RL FEBS Lett. 406:142-146(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-213 IN COMPLEX WITH IRON,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
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 basis
RT 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 systems.
CC {ECO:0000305|PubMed:9109405}.
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 Evidence={ECO:0000269|PubMed:9109405};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:9109405, ECO:0000269|PubMed:9236127};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:9109405,
CC ECO:0000269|PubMed:9236127};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Highly thermostable. Retains about 70% of its activity after heating
CC for 60 minutes at 100 degrees Celsius. {ECO:0000269|PubMed:9236127};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9109405,
CC ECO:0000269|PubMed:9236127}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AF152997; AAD34161.1; -; Genomic_DNA.
DR PDB; 1COJ; X-ray; 1.90 A; A=2-213.
DR PDBsum; 1COJ; -.
DR AlphaFoldDB; 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; 3.55.40.20; -; 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
FT /note="Removed"
FT CHAIN 2..213
FT /note="Superoxide dismutase [Fe]"
FT /id="PRO_0000159972"
FT BINDING 28
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:9236127,
FT ECO:0007744|PDB:1COJ"
FT BINDING 82
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:9236127,
FT ECO:0007744|PDB:1COJ"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:9236127,
FT ECO:0007744|PDB:1COJ"
FT BINDING 168
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:9236127,
FT ECO:0007744|PDB:1COJ"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1COJ"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1COJ"
FT HELIX 22..30
FT /evidence="ECO:0007829|PDB:1COJ"
FT HELIX 32..48
FT /evidence="ECO:0007829|PDB:1COJ"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:1COJ"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:1COJ"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1COJ"
FT HELIX 64..87
FT /evidence="ECO:0007829|PDB:1COJ"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:1COJ"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:1COJ"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:1COJ"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:1COJ"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:1COJ"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:1COJ"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1COJ"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:1COJ"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:1COJ"
FT HELIX 191..208
FT /evidence="ECO:0007829|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
