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 27-MAR-2024, entry version 99.
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; Actinomycetota; Actinomycetes; Mycobacteriales; 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.MSMEG_6427; -.
DR PaxDb; 246196-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 OrthoDB; 9803125at2; -.
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; 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 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
//
