SODM_CORDI
ID SODM_CORDI Reviewed; 199 AA.
AC P42821;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Superoxide dismutase [Mn];
DE EC=1.15.1.1;
GN Name=sodA; Synonyms=sod; OrderedLocusNames=DIP2261;
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=257309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA Parkhill J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-189.
RC STRAIN=ATCC 11913;
RX PubMed=7852575; DOI=10.1128/jcm.32.11.2801-2812.1994;
RA Zolg J.W., Philippi-Schulz S.;
RT "The superoxide dismutase gene, a target for detection and identification
RT of mycobacteria by PCR.";
RL J. Clin. Microbiol. 32:2801-2812(1994).
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 -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; BX248360; CAE50785.1; -; Genomic_DNA.
DR EMBL; X81382; CAA57145.1; -; Genomic_DNA.
DR PIR; I40677; I40677.
DR RefSeq; WP_004567418.1; NC_002935.2.
DR AlphaFoldDB; P42821; -.
DR SMR; P42821; -.
DR STRING; 257309.DIP2261; -.
DR EnsemblBacteria; CAE50785; CAE50785; DIP2261.
DR KEGG; cdi:DIP2261; -.
DR HOGENOM; CLU_031625_2_2_11; -.
DR OMA; KWGSFDK; -.
DR OrthoDB; 1440645at2; -.
DR Proteomes; UP000002198; 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; 3.55.40.20; -; 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 Manganese; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..199
FT /note="Superoxide dismutase [Mn]"
FT /id="PRO_0000160028"
FT BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CONFLICT 41
FT /note="A -> T (in Ref. 2; CAA57145)"
FT /evidence="ECO:0000305"
FT CONFLICT 123..124
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="F -> V (in Ref. 2; CAA57145)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 199 AA; 21887 MW; AAAB70FF509078D8 CRC64;
MTYALPELDY AYDALEPHIA AEIMELHHSK HHANYVNGAN AALEKLQKAR ENGEIGAVVT
ALSKDLAFNL GGHTNHSIFW KNLSPNGGGE PTGALAEAIA KEFGSFEKFK DHFSAAALGL
QGSGWAVLGY DHIGGRLVIE QLTDQQGNIS ANLTPLLMLD MWEHAFYLQY KNVKADYVKA
VWNVFNWDDV AARFEAATK
