ID SODM2_STAAM Reviewed; 199 AA.
AC P66830; Q99X82;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Superoxide dismutase [Mn/Fe] 2;
DE EC=1.15.1.1 {ECO:0000250|UniProtKB:P80293};
GN Name=sodM; OrderedLocusNames=SAV0133;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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 -!- SUBUNIT: Homodimer. Can also form a heterodimer with SodA (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; BA000017; BAB56295.1; -; Genomic_DNA.
DR RefSeq; WP_000874681.1; NC_002758.2.
DR AlphaFoldDB; P66830; -.
DR SMR; P66830; -.
DR World-2DPAGE; 0002:P66830; -.
DR KEGG; sav:SAV0133; -.
DR HOGENOM; CLU_031625_0_0_9; -.
DR PhylomeDB; P66830; -.
DR Proteomes; UP000002481; 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; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 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 PANTHER; PTHR43595; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43595:SF2; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
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; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 3: Inferred from homology;
KW Iron; Manganese; Metal-binding; Oxidoreductase; Stress response.
FT CHAIN 1..199
FT /note="Superoxide dismutase [Mn/Fe] 2"
FT /id="PRO_0000160080"
FT BINDING 27
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 81
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 81
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 161
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 161
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"
SQ SEQUENCE 199 AA; 23041 MW; 388566FB9943C635 CRC64;
MAFKLPNLPY AYDALEPYID QRTMEFHHDK HHNTYVTKLN ATVEGTELEH QSLADMIANL
DKVPEAMRMS VRNNGGGHFN HSLFWEILSP NSEEKGGVID DIKAQWGTLD EFKNEFANKA
TTLFGSGWTW LVVNDGKLEI VTTPNQDNPL TEGKTPILLF DVWEHAYYLK YQNKRPDYMT
AFWNIVNWKK VDELYQAAK
//
