ID   SODM_MYCSM              Reviewed;         207 AA.
AC   P53649; Q9S612;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; Synonyms=sod;
OS   Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=1-2C;
RX   PubMed=9933629; DOI=10.1074/jbc.274.7.4281;
RA   Harth G., Horwitz M.A.;
RT   "Export of recombinant Mycobacterium tuberculosis superoxide dismutase is
RT   dependent upon both information in the protein and mycobacterial export
RT   machinery. A model for studying export of leaderless proteins by pathogenic
RT   mycobacteria.";
RL   J. Biol. Chem. 274:4281-4292(1999).
RN   [2]
RP   SEQUENCE REVISION TO 117 AND 202.
RA   Tullius M.V., Harth G., Horwitz M.A.;
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-165.
RC   STRAIN=ATCC 14468 / DSM 43277 / NCIB 9953 / NCTC 10265 / W-113;
RA   Bull T.J., Shanson D.C., Archard L.C.;
RT   "Rapid identification of mycobacteria from AIDS patients by capillary
RT   electrophoretic profiling of amplified SOD gene.";
RL   Clin. Mol. Pathol. 48:124-132(1995).
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: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Partially secreted.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; AF061031; AAD15825.2; -; Genomic_DNA.
DR   EMBL; Z48214; CAA88247.1; -; Genomic_DNA.
DR   PIR; S52366; S52366.
DR   RefSeq; WP_011731275.1; NZ_UGQO01000001.1.
DR   AlphaFoldDB; P53649; -.
DR   SMR; P53649; -.
DR   GeneID; 66737704; -.
DR   OMA; KWGSFDK; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   Manganese; Metal-binding; Oxidoreductase; Secreted.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..207
FT                   /note="Superoxide dismutase [Mn]"
FT                   /id="PRO_0000160059"
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;  22936 MW;  828BEF2B1F3A3E2E CRC64;
     MAEYTLPDLD YDYGALEPHI SGQINELHHS KHHATYVKGV NDAIAKLEEA RANGDHAAIF
     LNEKNLAFHL GGHINHSIWW KNLSPNGGDK PTGELAAAID DQFGSFDKFQ AQFTAAANGL
     QGSGWAVLGY DSLGGRLLTF QLYDQQANVP LGIIPLLQVD MWEHAFYLQY KNVKADYVKA
     FWNVVNWDDV QNRFAAATSK TSGLIFG