ID SODM_MYCPH Reviewed; 138 AA.
AC P53648;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 28-JUN-2023, entry version 83.
DE RecName: Full=Superoxide dismutase [Mn];
DE EC=1.15.1.1;
DE Flags: Fragment;
GN Name=sodA; Synonyms=sod;
OS Mycolicibacterium phlei (Mycobacterium phlei).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1771;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11758 / DSM 43239 / BCRC 10707 / JCM 6385 / NCTC 8151 / NRRL
RC B-14615;
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 -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; Z48211; CAA88244.1; -; Genomic_DNA.
DR PIR; S52379; S52379.
DR AlphaFoldDB; P53648; -.
DR SMR; P53648; -.
DR STRING; 1771.MPHLCCUG_00560; -.
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; 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 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.
PE 3: Inferred from homology;
KW Manganese; Metal-binding; Oxidoreductase.
FT CHAIN <1..>138
FT /note="Superoxide dismutase [Mn]"
FT /id="PRO_0000160057"
FT BINDING 2
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 138
SQ SEQUENCE 138 AA; 15066 MW; 4E765C9D6D5438AE CRC64;
SHSKHHATYV KGVNDAIAKL EEARANGDHG AIFLHEKNLA FHLGGHVNHT IWWKNLSPHG
GDKPTGDLAA AIDDQFGSFD NFRAQFTAAA NGLQGSGWAV LGYDTLGDRL LTFQLYDQQA
NVPLGIIPLL LVDMWEHA
//
