ID   SODM_MYCS2              Reviewed;         207 AA.
AC   A0R652; I7GFS1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; Synonyms=sodB; OrderedLocusNames=MSMEG_6427, MSMEI_6260;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   PROTEASOME SUBSTRATE, PUPYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=19028679; DOI=10.1074/jbc.m808032200;
RA   Burns K.E., Liu W.-T., Boshoff H.I.M., Dorrestein P.C., Barry C.E. III;
RT   "Proteasomal protein degradation in mycobacteria is dependent upon a
RT   prokaryotic ubiquitin-like protein.";
RL   J. Biol. Chem. 284:3069-3075(2009).
RN   [5]
RP   PUPYLATION AT LYS-38 AND LYS-90, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20094657; DOI=10.1039/b916104j;
RA   Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V.,
RA   Barry C.E. III, Bark S., Dorrestein P.C.;
RT   "Expansion of the mycobacterial 'PUPylome'.";
RL   Mol. Biosyst. 6:376-385(2010).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological systems.
CC       {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- PTM: Pupylated by the prokaryotic ubiquitin-like protein Pup, which
CC       leads to its degradation by the proteasome.
CC       {ECO:0000269|PubMed:19028679, ECO:0000269|PubMed:20094657}.
CC   -!- MISCELLANEOUS: Was identified as a natural substrate of the M.smegmatis
CC       proteasome.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000480; ABK71950.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP42686.1; -; Genomic_DNA.
DR   RefSeq; WP_011731275.1; NZ_SIJM01000013.1.
DR   RefSeq; YP_890640.1; NC_008596.1.
DR   AlphaFoldDB; A0R652; -.
DR   SMR; A0R652; -.
DR   STRING; 246196.MSMEI_6260; -.
DR   EnsemblBacteria; ABK71950; ABK71950; MSMEG_6427.
DR   EnsemblBacteria; AFP42686; AFP42686; MSMEI_6260.
DR   GeneID; 66737704; -.
DR   KEGG; msg:MSMEI_6260; -.
DR   KEGG; msm:MSMEG_6427; -.
DR   PATRIC; fig|246196.19.peg.6254; -.
DR   eggNOG; COG0605; Bacteria.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; 1440645at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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   1: Evidence at protein level;
KW   Isopeptide bond; Manganese; Metal-binding; Oxidoreductase;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..207
FT                   /note="Superoxide dismutase [Mn]"
FT                   /id="PRO_0000383478"
FT   CROSSLNK        38
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-Cter in protein Pup)"
FT                   /evidence="ECO:0000269|PubMed:20094657"
FT   CROSSLNK        90
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-Cter in protein Pup)"
FT                   /evidence="ECO:0000269|PubMed:20094657"
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