SODM_THET8
ID SODM_THET8 Reviewed; 204 AA.
AC P61503; P09214; Q5SKT6;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Superoxide dismutase [Mn];
DE EC=1.15.1.1;
GN Name=sodA; OrderedLocusNames=TTHA0557;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-204.
RX PubMed=3828357; DOI=10.1016/0167-4838(87)90086-0;
RA Sato S., Nakada Y., Nakazawa-Tomizawa K.;
RT "Amino-acid sequence of a tetrameric, manganese superoxide dismutase from
RT Thermus thermophilus HB8.";
RL Biochim. Biophys. Acta 912:178-184(1987).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=4066716; DOI=10.1016/s0021-9258(17)36254-3;
RA Stallings W.C., Pattridge K.A., Strong R.K., Ludwig M.L.;
RT "The structure of manganese superoxide dismutase from Thermus thermophilus
RT HB8 at 2.4-A resolution.";
RL J. Biol. Chem. 260:16424-16432(1985).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=2038060; DOI=10.1016/0022-2836(91)90569-r;
RA Ludwig M.L., Metzger A.L., Pattridge K.A., Stallings W.C.;
RT "Manganese superoxide dismutase from Thermus thermophilus. A structural
RT model refined at 1.8-A resolution.";
RL J. Mol. Biol. 219:335-358(1991).
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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Binds 1 Mn(2+) ion per subunit.;
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AP008226; BAD70380.1; -; Genomic_DNA.
DR RefSeq; WP_011172643.1; NC_006461.1.
DR RefSeq; YP_143823.1; NC_006461.1.
DR PDB; 1MNG; X-ray; 1.80 A; A/B=2-204.
DR PDB; 3MDS; X-ray; 1.80 A; A/B=2-204.
DR PDBsum; 1MNG; -.
DR PDBsum; 3MDS; -.
DR AlphaFoldDB; P61503; -.
DR SMR; P61503; -.
DR STRING; 300852.55771939; -.
DR EnsemblBacteria; BAD70380; BAD70380; BAD70380.
DR GeneID; 3169327; -.
DR KEGG; ttj:TTHA0557; -.
DR PATRIC; fig|300852.9.peg.556; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_0_1_0; -.
DR OMA; KWGSFDK; -.
DR PhylomeDB; P61503; -.
DR EvolutionaryTrace; P61503; -.
DR Proteomes; UP000000532; Chromosome.
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; Direct protein sequencing; Manganese; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3828357"
FT CHAIN 2..204
FT /note="Superoxide dismutase [Mn]"
FT /id="PRO_0000160108"
FT BINDING 29
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 84
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 171
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:1MNG"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:1MNG"
FT HELIX 23..31
FT /evidence="ECO:0007829|PDB:1MNG"
FT HELIX 33..46
FT /evidence="ECO:0007829|PDB:1MNG"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1MNG"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:1MNG"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1MNG"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1MNG"
FT HELIX 71..90
FT /evidence="ECO:0007829|PDB:1MNG"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:1MNG"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:1MNG"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:1MNG"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:1MNG"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1MNG"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:1MNG"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:1MNG"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:1MNG"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:1MNG"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:1MNG"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:1MNG"
SQ SEQUENCE 204 AA; 23230 MW; 37B9C1956FD8D46B CRC64;
MPYPFKLPDL GYPYEALEPH IDAKTMEIHH QKHHGAYVTN LNAALEKYPY LHGVEVEVLL
RHLAALPQDI QTAVRNNGGG HLNHSLFWRL LTPGGAKEPV GELKKAIDEQ FGGFQALKEK
LTQAAMGRFG SGWAWLVKDP FGKLHVLSTP NQDNPVMEGF TPIVGIDVWE HAYYLKYQNR
RADYLQAIWN VLNWDVAEEF FKKA
