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   24-JAN-2024, entry version 115.
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; Chlamydiota; Chlamydiia; 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., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   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 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 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF39404.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE002160; AAF39404.1; ALT_INIT; Genomic_DNA.
DR   PIR; A81688; A81688.
DR   RefSeq; WP_010230850.1; NZ_CP063055.1.
DR   AlphaFoldDB; Q9PKA0; -.
DR   SMR; Q9PKA0; -.
DR   GeneID; 1245926; -.
DR   KEGG; cmu:TC_0567; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_2_1_0; -.
DR   OrthoDB; 9803125at2; -.
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; 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; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR   PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], 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   3: Inferred from homology;
KW   Manganese; Metal-binding; Oxidoreductase.
FT   CHAIN           1..205
FT                   /note="Superoxide dismutase [Mn]"
FT                   /id="PRO_0000160025"
FT   BINDING         30
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="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
//