SODM_DEIRA
ID SODM_DEIRA Reviewed; 211 AA.
AC Q9RUV2;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Superoxide dismutase [Mn];
DE EC=1.15.1.1;
DE AltName: Full=MnSOD;
GN Name=sodA; OrderedLocusNames=DR_1279;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RA Joshi B.S., Apte S.K., Schmid R., Altendorf K.;
RL Submitted (APR-2003) to UniProtKB.
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC {ECO:0000250}.
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; Evidence={ECO:0000250};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AE000513; AAF10851.1; -; Genomic_DNA.
DR PIR; B75415; B75415.
DR RefSeq; NP_295003.1; NC_001263.1.
DR RefSeq; WP_010887922.1; NZ_CP015081.1.
DR PDB; 1Y67; X-ray; 1.85 A; A/B/C/D=2-211.
DR PDB; 2AW9; X-ray; 2.70 A; A/B=2-211.
DR PDB; 2CDY; X-ray; 2.00 A; A/B/C/D=2-211.
DR PDB; 2CE4; X-ray; 2.20 A; A/B=2-211.
DR PDB; 3KKY; X-ray; 1.80 A; A/B=1-211.
DR PDBsum; 1Y67; -.
DR PDBsum; 2AW9; -.
DR PDBsum; 2CDY; -.
DR PDBsum; 2CE4; -.
DR PDBsum; 3KKY; -.
DR AlphaFoldDB; Q9RUV2; -.
DR SMR; Q9RUV2; -.
DR STRING; 243230.DR_1279; -.
DR EnsemblBacteria; AAF10851; AAF10851; DR_1279.
DR KEGG; dra:DR_1279; -.
DR PATRIC; fig|243230.17.peg.1475; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_0_1_0; -.
DR InParanoid; Q9RUV2; -.
DR OMA; KWGSFDK; -.
DR OrthoDB; 1440645at2; -.
DR BRENDA; 1.15.1.1; 1856.
DR EvolutionaryTrace; Q9RUV2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:CACAO.
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|Ref.2"
FT CHAIN 2..211
FT /note="Superoxide dismutase [Mn]"
FT /id="PRO_0000160029"
FT BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT TURN 12..18
FT /evidence="ECO:0007829|PDB:3KKY"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:3KKY"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:3KKY"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:3KKY"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:3KKY"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:3KKY"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3KKY"
FT HELIX 68..86
FT /evidence="ECO:0007829|PDB:3KKY"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:3KKY"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:3KKY"
FT STRAND 131..140
FT /evidence="ECO:0007829|PDB:3KKY"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:3KKY"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:3KKY"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:3KKY"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:3KKY"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:3KKY"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:3KKY"
FT HELIX 187..194
FT /evidence="ECO:0007829|PDB:3KKY"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3KKY"
FT HELIX 200..210
FT /evidence="ECO:0007829|PDB:3KKY"
SQ SEQUENCE 211 AA; 23478 MW; A71F22F516A1897E CRC64;
MAYTLPQLPY AYDALEPHID ARTMEIHHTK HHQTYVDNAN KALEGTEFAD LPVEQLIQQL
DRVPADKKGA LRNNAGGHAN HSMFWQIMGQ GQGQNGANQP SGELLDAINS AFGSFDAFKQ
KFEDAAKTRF GSGWAWLVVK DGKLDVVSTA NQDNPLMGEA IAGVSGTPIL GVDVWEHAYY
LNYQNRRPDY LAAFWNVVNW DEVSKRYAAA K
