ID SODM_STRMU Reviewed; 203 AA.
AC P09738; Q59791;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 147.
DE RecName: Full=Superoxide dismutase [Mn/Fe];
DE EC=1.15.1.1 {ECO:0000250|UniProtKB:P80293};
GN Name=sodA; Synonyms=sod; OrderedLocusNames=SMU_629;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GS-5;
RX PubMed=1321118; DOI=10.1128/jb.174.15.4928-4934.1992;
RA Nakayama K.;
RT "Nucleotide sequence of Streptococcus mutans superoxide dismutase gene and
RT isolation of insertion mutants.";
RL J. Bacteriol. 174:4928-4934(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [3]
RP PROTEIN SEQUENCE OF 2-23.
RX PubMed=3722201; DOI=10.1016/s0021-9258(18)67663-x;
RA Martin M.E., Byers B.R., Olson M.O.J., Salin M.L., Arceneaux J.E.L.,
RA Tolbert C.;
RT "A Streptococcus mutans superoxide dismutase that is active with either
RT manganese or iron as a cofactor.";
RL J. Biol. Chem. 261:9361-9367(1986).
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 -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; D01037; BAB86870.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58363.1; -; Genomic_DNA.
DR PIR; A42710; A42710.
DR RefSeq; NP_721057.1; NC_004350.2.
DR RefSeq; WP_002261912.1; NC_004350.2.
DR PDB; 4YIP; X-ray; 2.15 A; A/B/C/D=1-202.
DR PDBsum; 4YIP; -.
DR AlphaFoldDB; P09738; -.
DR SMR; P09738; -.
DR STRING; 210007.SMU_629; -.
DR GeneID; 66817909; -.
DR KEGG; smu:SMU_629; -.
DR PATRIC; fig|210007.7.peg.555; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_0_1_9; -.
DR OrthoDB; 9803125at2; -.
DR PhylomeDB; P09738; -.
DR Proteomes; UP000002512; 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Iron; Manganese; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3722201"
FT CHAIN 2..203
FT /note="Superoxide dismutase [Mn/Fe]"
FT /id="PRO_0000160094"
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 163
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 167
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT CONFLICT 4
FT /note="L -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 12..18
FT /evidence="ECO:0007829|PDB:4YIP"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:4YIP"
FT HELIX 31..45
FT /evidence="ECO:0007829|PDB:4YIP"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4YIP"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:4YIP"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:4YIP"
FT HELIX 65..87
FT /evidence="ECO:0007829|PDB:4YIP"
FT HELIX 97..107
FT /evidence="ECO:0007829|PDB:4YIP"
FT HELIX 110..123
FT /evidence="ECO:0007829|PDB:4YIP"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:4YIP"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:4YIP"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:4YIP"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:4YIP"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4YIP"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:4YIP"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:4YIP"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:4YIP"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:4YIP"
SQ SEQUENCE 203 AA; 22626 MW; CC86C35928C415A6 CRC64;
MAILLPDLPY AYDALEPYID AETMTLHHDK HHATYVANAN AALEKHPEIG ENLEVLLADV
EQIPADIRQS LINNGGGHLN HALFWELLSP EKTKVTAEVA AAINEAFGSF DDFKAAFTAA
ATTRFGSGWA WLVVDKEGKL EVTSTANQDT PISQGLKPIL ALDVWEHAYY LNYRNVRPNY
IKAFFEVINW NTVARLYAEA LTK
//
