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Database: UniProt
Entry: P61503
LinkDB: P61503
Original site: P61503 
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   05-DEC-2018, entry version 90.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; OrderedLocusNames=TTHA0557;
OS   Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HB8 / ATCC 27634 / DSM 579;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y.,
RA   Shibata T., 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
RT   from Thermus thermophilus HB8.";
RL   Biochim. Biophys. Acta 912:178-184(1987).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX   PubMed=4066716;
RA   Stallings W.C., Pattridge K.A., Strong R.K., Ludwig M.L.;
RT   "The structure of manganese superoxide dismutase from Thermus
RT   thermophilus 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
RT   structural 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
CC       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
CC       family. {ECO:0000305}.
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   ProteinModelPortal; P61503; -.
DR   SMR; P61503; -.
DR   STRING; 300852.TTHA0557; -.
DR   EnsemblBacteria; BAD70380; BAD70380; BAD70380.
DR   GeneID; 3169327; -.
DR   KEGG; ttj:TTHA0557; -.
DR   PATRIC; fig|300852.9.peg.556; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   PhylomeDB; P61503; -.
DR   BioCyc; TTHE300852:G1GKC-574-MONOMER; -.
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; 2.40.500.20; -; 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; Complete proteome; Direct protein sequencing; Manganese;
KW   Metal-binding; Oxidoreductase; Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:3828357}.
FT   CHAIN         2    204       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160108.
FT   METAL        29     29       Manganese.
FT   METAL        84     84       Manganese.
FT   METAL       167    167       Manganese.
FT   METAL       171    171       Manganese.
FT   HELIX        14     17       {ECO:0000244|PDB:1MNG}.
FT   TURN         18     20       {ECO:0000244|PDB:1MNG}.
FT   HELIX        23     31       {ECO:0000244|PDB:1MNG}.
FT   HELIX        33     46       {ECO:0000244|PDB:1MNG}.
FT   HELIX        49     51       {ECO:0000244|PDB:1MNG}.
FT   HELIX        56     61       {ECO:0000244|PDB:1MNG}.
FT   HELIX        63     65       {ECO:0000244|PDB:1MNG}.
FT   HELIX        68     70       {ECO:0000244|PDB:1MNG}.
FT   HELIX        71     90       {ECO:0000244|PDB:1MNG}.
FT   HELIX       101    111       {ECO:0000244|PDB:1MNG}.
FT   HELIX       114    126       {ECO:0000244|PDB:1MNG}.
FT   STRAND      130    138       {ECO:0000244|PDB:1MNG}.
FT   STRAND      144    150       {ECO:0000244|PDB:1MNG}.
FT   HELIX       155    158       {ECO:0000244|PDB:1MNG}.
FT   STRAND      161    167       {ECO:0000244|PDB:1MNG}.
FT   HELIX       170    172       {ECO:0000244|PDB:1MNG}.
FT   HELIX       174    177       {ECO:0000244|PDB:1MNG}.
FT   HELIX       181    188       {ECO:0000244|PDB:1MNG}.
FT   TURN        189    191       {ECO:0000244|PDB:1MNG}.
FT   HELIX       194    202       {ECO:0000244|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
//
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