ID SODM_MYCLE Reviewed; 207 AA.
AC P13367;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 140.
DE RecName: Full=Superoxide dismutase [Mn];
DE EC=1.15.1.1;
GN Name=sodA; OrderedLocusNames=ML0072;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2682526; DOI=10.1093/nar/17.20.8378;
RA Thangaraj H.S., Lamb F.I., Davis E.O., Colston M.J.;
RT "Nucleotide and deduced amino acid sequence of Mycobacterium leprae
RT manganese superoxide dismutase.";
RL Nucleic Acids Res. 17:8378-8378(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1692812; DOI=10.1128/iai.58.6.1937-1942.1990;
RA Thangaraj H.S., Lamb F.I., Davis E.O., Jenner P.J., Jeyakumar L.H.,
RA Colston M.J.;
RT "Identification, sequencing, and expression of Mycobacterium leprae
RT superoxide dismutase, a major antigen.";
RL Infect. Immun. 58:1937-1942(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; X16453; CAA34472.1; -; Genomic_DNA.
DR EMBL; AL583917; CAC29580.1; -; Genomic_DNA.
DR PIR; S06599; S06599.
DR RefSeq; NP_301180.1; NC_002677.1.
DR RefSeq; WP_010907505.1; NC_002677.1.
DR AlphaFoldDB; P13367; -.
DR SMR; P13367; -.
DR STRING; 272631.gene:17573884; -.
DR KEGG; mle:ML0072; -.
DR PATRIC; fig|272631.5.peg.111; -.
DR Leproma; ML0072; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_2_2_11; -.
DR OrthoDB; 9803125at2; -.
DR Proteomes; UP000000806; 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; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..207
FT /note="Superoxide dismutase [Mn]"
FT /id="PRO_0000160052"
FT BINDING 28
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"
SQ SEQUENCE 207 AA; 23158 MW; 8B37D86D5F71FF17 CRC64;
MAEYTLPDLD WDYAALEPHI SGEINEIHHT KHHAAYVKGV NDALAKLDEA RAKDDHSAIF
LNEKNLAFHL GGHVNHSIWW KNLSPNGGDK PTGGLATDID ETFGSFDKFR AQFSAAANGL
QGSGWAVLGY DTLGNKLLTF QLYDQQANVS LGIIPLLQVD MWEHAFYLQY KNVKADYVKA
FWNVVNWADV QSRYMAATSK TQGLIFD
//
