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Database: UniProt
Entry: P23744
LinkDB: P23744
Original site: P23744 
ID   SODF_METJ               Reviewed;         202 AA.
AC   P23744;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   05-DEC-2018, entry version 78.
DE   RecName: Full=Superoxide dismutase [Mn/Fe];
DE            EC=1.15.1.1;
GN   Name=sodB;
OS   Methylomonas sp. (strain J).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomonas.
OX   NCBI_TaxID=32038;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=1848999; DOI=10.1021/bi00227a008;
RA   Matsumoto T., Terauchi K., Isobe T., Matsuoka K., Yamakura F.;
RT   "Iron- and manganese-containing superoxide dismutases from
RT   Methylomonas J: identity of the protein moiety and amino acid
RT   sequence.";
RL   Biochemistry 30:3210-3216(1991).
RN   [2]
RP   CHARACTERIZATION, AND PROTEIN SEQUENCE OF 1-32.
RX   PubMed=1906419; DOI=10.3109/10715769109145802;
RA   Yamakura F., Matsumoto T., Terauchi K.;
RT   "Isolation of Mn-SOD and low active Fe-SOD from Methylomonas J;
RT   consisting of identical proteins.";
RL   Free Radic. Res. Commun. 12:329-334(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; Evidence={ECO:0000250};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) or Fe(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   ProteinModelPortal; P23744; -.
DR   SMR; P23744; -.
DR   PRIDE; P23744; -.
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   Direct protein sequencing; Iron; Manganese; Metal-binding;
KW   Oxidoreductase.
FT   CHAIN         1    202       Superoxide dismutase [Mn/Fe].
FT                                /FTId=PRO_0000159988.
FT   METAL        26     26       Manganese or iron. {ECO:0000250}.
FT   METAL        80     80       Manganese or iron. {ECO:0000250}.
FT   METAL       163    163       Manganese or iron. {ECO:0000250}.
FT   METAL       167    167       Manganese or iron. {ECO:0000250}.
SQ   SEQUENCE   202 AA;  22363 MW;  3213A8B4697A5B58 CRC64;
     AYTLPPLDYA YTALEPHIDA QTMEIHHTKH HQTYINNVNA ALEGTSFANE PVEALLQKLD
     SLPENLRGPV RNNGGGHANH SLFWKVLTPN GGGEPKGALA DAIKSDIGGL DTFKEAFTKA
     ALTRFGSGWA WLSVTPEKKL VVESTGNQDS PLSTGNTPIL GLDVWEHAYY LKYQNRRPEY
     IGAFFNVVNW DEVSRRYQEA LA
//
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