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Database: UniProt/SWISS-PROT
Entry: SODM_CHLTR
LinkDB: SODM_CHLTR
Original site: SODM_CHLTR 
ID   SODM_CHLTR              Reviewed;         206 AA.
AC   O84296;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   05-DEC-2018, entry version 107.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; Synonyms=sodM; OrderedLocusNames=CT_294;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V.,
RA   Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans:
RT   Chlamydia trachomatis.";
RL   Science 282:754-759(1998).
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       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AE001273; AAC67887.1; -; Genomic_DNA.
DR   PIR; H71531; H71531.
DR   RefSeq; NP_219799.1; NC_000117.1.
DR   RefSeq; WP_009871642.1; NC_000117.1.
DR   ProteinModelPortal; O84296; -.
DR   SMR; O84296; -.
DR   EnsemblBacteria; AAC67887; AAC67887; CT_294.
DR   GeneID; 35556504; -.
DR   GeneID; 884829; -.
DR   KEGG; ctr:CT_294; -.
DR   PATRIC; fig|272561.5.peg.315; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   InParanoid; O84296; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   BioCyc; CTRA272561:G1G18-308-MONOMER; -.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
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   3: Inferred from homology;
KW   Complete proteome; Manganese; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    206       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160027.
FT   METAL        30     30       Manganese. {ECO:0000250}.
FT   METAL        78     78       Manganese. {ECO:0000250}.
FT   METAL       166    166       Manganese. {ECO:0000250}.
FT   METAL       170    170       Manganese. {ECO:0000250}.
SQ   SEQUENCE   206 AA;  23475 MW;  96C8C45B8C355C21 CRC64;
     MVFSSYMLPA LPYDYDALEP VISAEIMQLH HQKHHQGYIN NLNEALKSLD VANATQDLAR
     LIAINPALRF NGGSHINHSL FWEMLAPQGK GGGVPPRHEL LKLIEKFWGS FDNFLKNFIT
     SSAAVQGSGW GWLAFCPQKQ ELMVQTTANQ DPLEATTGMI PLLGVDVWEH AYYLQYKNAR
     MDYLKSFPSI INWDYIENRF VEMSKQ
//
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