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Database: UniProt
Entry: Q9PKA0
LinkDB: Q9PKA0
Original site: Q9PKA0 
ID   SODM_CHLMU              Reviewed;         205 AA.
AC   Q9PKA0;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   16-JAN-2019, entry version 102.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; OrderedLocusNames=TC_0567;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F.,
RA   White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J.,
RA   Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C.,
RA   Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F.,
RA   McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia
RT   pneumoniae AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF39404.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE002160; AAF39404.1; ALT_INIT; Genomic_DNA.
DR   PIR; A81688; A81688.
DR   RefSeq; WP_010230850.1; NZ_CP027217.1.
DR   ProteinModelPortal; Q9PKA0; -.
DR   SMR; Q9PKA0; -.
DR   STRING; 243161.CmurN_010100002883; -.
DR   EnsemblBacteria; AAF39404; AAF39404; TC_0567.
DR   GeneID; 1245926; -.
DR   KEGG; cmu:TC_0567; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OrthoDB; 1440645at2; -.
DR   Proteomes; UP000000800; 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; 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.
FT   CHAIN         1    205       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160025.
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   205 AA;  23312 MW;  BE755952B580FBBC CRC64;
     MVFSSYKLPD LPYDYDALEP VISAEIMHLH HQKHHQGYIN NLNEALKSLD VASATQDLTG
     LIAINPALRF NGGGHINHSL FWEMLAPQNK GGGTPPRHEL LKLIEKFWGS FDNFLKNFIS
     SSAAVQGSGW GWLAFCPKKQ ELMIQTTANQ DPLEATTGMI PLLGVDVWEH AYYLQYKNAR
     LDYLKNFPSI INWDYIESRF VEMSK
//
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