SODF_AERPE
ID SODF_AERPE Reviewed; 214 AA.
AC Q9Y8H8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Superoxide dismutase [Mn/Fe];
DE EC=1.15.1.1 {ECO:0000250|UniProtKB:P80293};
GN Name=sod; OrderedLocusNames=APE_0741;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10393342; DOI=10.1093/oxfordjournals.jbchem.a022426;
RA Yamano S., Sako Y., Nomura N., Maruyama T.;
RT "A cambialistic SOD in a strictly aerobic hyperthermophilic archaeon,
RT Aeropyrum pernix.";
RL J. Biochem. 126:218-225(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2
CC by successive reduction and oxidation of the transition metal ion at
CC the active site. {ECO:0000250|UniProtKB:P80293}.
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:0000250|UniProtKB:P80293};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697;
CC Evidence={ECO:0000250|UniProtKB:P80293};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P80293};
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000250|UniProtKB:P80293};
CC Note=Binds 1 Mn(2+) or Fe(3+) ion per subunit.
CC {ECO:0000250|UniProtKB:P80293};
CC -!- INTERACTION:
CC Q9Y8H8; Q9Y8H8: sod; NbExp=3; IntAct=EBI-8549588, EBI-8549588;
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AB012621; BAA76442.1; -; Genomic_DNA.
DR EMBL; BA000002; BAA79718.1; -; Genomic_DNA.
DR PIR; F72664; F72664.
DR PDB; 3AK1; X-ray; 1.57 A; A/B/C/D=1-214.
DR PDB; 3AK2; X-ray; 1.35 A; A/B/C/D=1-214.
DR PDB; 3AK3; X-ray; 1.48 A; A/B/C/D=1-214.
DR PDBsum; 3AK1; -.
DR PDBsum; 3AK2; -.
DR PDBsum; 3AK3; -.
DR AlphaFoldDB; Q9Y8H8; -.
DR SMR; Q9Y8H8; -.
DR MINT; Q9Y8H8; -.
DR STRING; 272557.APE_0741; -.
DR EnsemblBacteria; BAA79718; BAA79718; APE_0741.
DR KEGG; ape:APE_0741; -.
DR PATRIC; fig|272557.25.peg.534; -.
DR eggNOG; arCOG04147; Archaea.
DR OMA; KWGSFDK; -.
DR BRENDA; 1.15.1.1; 171.
DR EvolutionaryTrace; Q9Y8H8; -.
DR Proteomes; UP000002518; Chromosome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; Iron; Manganese; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..214
FT /note="Superoxide dismutase [Mn/Fe]"
FT /id="PRO_0000160005"
FT BINDING 31
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 31
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 79
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 79
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 165
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 165
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 169
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 169
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT TURN 16..22
FT /evidence="ECO:0007829|PDB:3AK2"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:3AK2"
FT HELIX 35..54
FT /evidence="ECO:0007829|PDB:3AK2"
FT HELIX 62..82
FT /evidence="ECO:0007829|PDB:3AK2"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:3AK2"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:3AK2"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:3AK2"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:3AK2"
FT STRAND 126..136
FT /evidence="ECO:0007829|PDB:3AK2"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:3AK2"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:3AK2"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:3AK2"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:3AK2"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:3AK2"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:3AK2"
FT HELIX 179..186
FT /evidence="ECO:0007829|PDB:3AK2"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:3AK2"
FT HELIX 192..205
FT /evidence="ECO:0007829|PDB:3AK2"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3AK2"
SQ SEQUENCE 214 AA; 24577 MW; 641122779485DF0A CRC64;
MVSFKRYELP PLPYNYNALE PYIIEEIMKL HHQKHHNTYV KGANAALEKI EKHLKGEIQI
DVRAVMRDFS FNYAGHIMHT IFWPNMAPPG KGGGTPGGRV ADLIEKQFGG FEKFKALFSA
AAKTVEGVGW GVLAFDPLTE ELRILQVEKH NVLMTAGLVP ILVIDVWEHA YYLQYKNDRG
SYVENWWNVV NWDDVEKRLE QALNNAKPLY LLPQ
