ID SODM_CHLPN Reviewed; 207 AA.
AC Q9Z9C4;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 24-JAN-2024, entry version 138.
DE RecName: Full=Superoxide dismutase [Mn];
DE EC=1.15.1.1;
GN Name=sodA; Synonyms=sodM; OrderedLocusNames=CPn_0057, CP_0718, CpB0058;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
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; AE001363; AAD18210.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38524.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98268.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP97991.1; -; Genomic_DNA.
DR PIR; B72124; B72124.
DR PIR; B86498; B86498.
DR RefSeq; NP_224265.1; NC_000922.1.
DR RefSeq; WP_010882707.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z9C4; -.
DR SMR; Q9Z9C4; -.
DR STRING; 406984.CPK_ORF00561; -.
DR GeneID; 45050101; -.
DR KEGG; cpa:CP_0718; -.
DR KEGG; cpj:sodM; -.
DR KEGG; cpn:CPn_0057; -.
DR KEGG; cpt:CpB0058; -.
DR PATRIC; fig|115713.3.peg.65; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_2_1_0; -.
DR OrthoDB; 9803125at2; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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..207
FT /note="Superoxide dismutase [Mn]"
FT /id="PRO_0000160026"
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 207 AA; 23541 MW; 45A4A6FF096F8934 CRC64;
MSFVPYSLPE LPYDYDALEP VISSEIMILH HQKHHQIYIN NLNAALKRLD AAETQQNLNE
LIALEPALRF NGGGHINHSL FWETLAPIDQ GGGQPPKHEL LSLIERFWGT MDNFLKKLIE
VAAGVQGSGW AWLGFCPAKQ ELVLQATANQ DPLEPLTGKL PLLGVDVWEH AYYLQYKNVR
MDYLKAFPQI INWGHIENRF SEIISSK
//
