位置:首页 > 蛋白库 > SODM_STRMU
SODM_STRMU
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   03-AUG-2022, entry version 142.
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; Firmicutes; 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   PRIDE; P09738; -.
DR   EnsemblBacteria; AAN58363; AAN58363; 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   OMA; KWGSFDK; -.
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; -; 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; 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024