SODM_PROFR
ID SODM_PROFR Reviewed; 201 AA.
AC P80293;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Superoxide dismutase [Mn/Fe];
DE EC=1.15.1.1 {ECO:0000269|PubMed:7575431};
GN Name=sodA;
OS Propionibacterium freudenreichii subsp. shermanii.
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Propionibacterium.
OX NCBI_TaxID=1752;
RN [1]
RP PROTEIN SEQUENCE, AND SUBUNIT.
RC STRAIN=PZ3;
RX PubMed=8307013; DOI=10.1111/j.1432-1033.1994.tb19960.x;
RA Meier B., Sehn A.P., Schinina M.E., Barra D.;
RT "In vivo incorporation of copper into the iron-exchangeable and manganese-
RT exchangeable superoxide dismutase from Propionibacterium shermanii. Amino
RT acid sequence and identity of the protein moieties.";
RL Eur. J. Biochem. 219:463-468(1994).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP ACTIVITY REGULATION.
RC STRAIN=PZ3;
RX PubMed=7575431; DOI=10.1042/bj3100945;
RA Meier B., Michel C., Saran M., Huettermann J., Parak F., Rotilio G.;
RT "Kinetic and spectroscopic studies on a superoxide dismutase from
RT Propionibacterium shermanii that is active with iron or manganese: pH-
RT dependence.";
RL Biochem. J. 310:945-950(1995).
RN [3]
RP COFACTOR, AND ACTIVITY REGULATION.
RC STRAIN=PZ3;
RX PubMed=9531477; DOI=10.1042/bj3310403;
RA Meier B., Scherk C., Schmidt M., Parak F.;
RT "pH-dependent inhibition by azide and fluoride of the iron superoxide
RT dismutase from Propionibacterium shermanii.";
RL Biochem. J. 331:403-407(1998).
RN [4] {ECO:0007744|PDB:1AR4, ECO:0007744|PDB:1AR5}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH IRON AND MANGANESE,
RP AND COFACTOR.
RC STRAIN=PZ3;
RX DOI=10.1007/s007750050089;
RA Schmidt M., Meier B., Parak F.;
RT "X-ray structure of the cambialistic superoxide dismutase from
RT Propionibacterium shermanii active with Fe or Mn.";
RL J. Biol. Inorg. Chem. 1:532-541(1996).
RN [5] {ECO:0007744|PDB:1BS3, ECO:0007744|PDB:1BSM, ECO:0007744|PDB:1BT8}
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH IRON, AND COFACTOR.
RX PubMed=10231372; DOI=10.1046/j.1432-1327.1999.00359.x;
RA Schmidt M.;
RT "Manipulating the coordination mumber of the ferric iron within the
RT cambialistic superoxide dismutase of Propionibacterium shermanii by
RT changing the pH-value. A crystallographic analysis.";
RL Eur. J. Biochem. 262:117-127(1999).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2
CC by successive reduction and oxidation of the transition metal ion at
CC the active site. {ECO:0000269|PubMed:7575431}.
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 Evidence={ECO:0000269|PubMed:7575431};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697;
CC Evidence={ECO:0000305|PubMed:7575431};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:7575431, ECO:0000269|PubMed:9531477,
CC ECO:0000269|Ref.4};
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000269|PubMed:10231372, ECO:0000269|PubMed:7575431,
CC ECO:0000269|PubMed:9531477, ECO:0000269|Ref.4};
CC Note=Binds 1 Mn(2+) or Fe(3+) ion per subunit.
CC {ECO:0000269|PubMed:10231372, ECO:0000269|Ref.4};
CC -!- ACTIVITY REGULATION: Shows decreasing activity with increasing pH
CC (PubMed:7575431). Slightly inhibited by azide and fluoride at pH 7-8;
CC the inhibition is drastically increased towards lower pH
CC (PubMed:9531477). {ECO:0000269|PubMed:7575431,
CC ECO:0000269|PubMed:9531477}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.54 mM for superoxide (at pH 9.5, with the Fe-SOD form)
CC {ECO:0000269|PubMed:7575431};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8307013}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR PIR; JC4396; JC4396.
DR PDB; 1AR4; X-ray; 1.90 A; A/B=1-201.
DR PDB; 1AR5; X-ray; 1.60 A; A/B=1-201.
DR PDB; 1AVM; X-ray; 1.55 A; A/B=1-201.
DR PDB; 1BS3; X-ray; 1.55 A; A/B=1-201.
DR PDB; 1BSM; X-ray; 1.35 A; A/B=1-201.
DR PDB; 1BT8; X-ray; 1.85 A; A/B=1-201.
DR PDBsum; 1AR4; -.
DR PDBsum; 1AR5; -.
DR PDBsum; 1AVM; -.
DR PDBsum; 1BS3; -.
DR PDBsum; 1BSM; -.
DR PDBsum; 1BT8; -.
DR AlphaFoldDB; P80293; -.
DR SMR; P80293; -.
DR EvolutionaryTrace; P80293; -.
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 3D-structure; Direct protein sequencing; Iron; Manganese; Metal-binding;
KW Oxidoreductase.
FT CHAIN 1..201
FT /note="Superoxide dismutase [Mn/Fe]"
FT /id="PRO_0000160066"
FT BINDING 27
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0007744|PDB:1AR5, ECO:0007744|PDB:1BS3,
FT ECO:0007744|PDB:1BSM, ECO:0007744|PDB:1BT8"
FT BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0007744|PDB:1AR4"
FT BINDING 75
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0007744|PDB:1AR5, ECO:0007744|PDB:1BS3,
FT ECO:0007744|PDB:1BSM, ECO:0007744|PDB:1BT8"
FT BINDING 75
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0007744|PDB:1AR4"
FT BINDING 161
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0007744|PDB:1AR5, ECO:0007744|PDB:1BS3,
FT ECO:0007744|PDB:1BSM, ECO:0007744|PDB:1BT8"
FT BINDING 161
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0007744|PDB:1AR4"
FT BINDING 165
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0007744|PDB:1AR5, ECO:0007744|PDB:1BS3,
FT ECO:0007744|PDB:1BT8"
FT BINDING 165
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0007744|PDB:1AR4"
FT TURN 12..18
FT /evidence="ECO:0007829|PDB:1BSM"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:1BSM"
FT HELIX 31..52
FT /evidence="ECO:0007829|PDB:1BSM"
FT HELIX 58..80
FT /evidence="ECO:0007829|PDB:1BSM"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:1BSM"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:1BSM"
FT STRAND 122..132
FT /evidence="ECO:0007829|PDB:1BSM"
FT TURN 133..136
FT /evidence="ECO:0007829|PDB:1BSM"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:1BSM"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:1BSM"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:1BSM"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1BSM"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:1BSM"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:1BSM"
FT HELIX 188..197
FT /evidence="ECO:0007829|PDB:1BSM"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:1BT8"
SQ SEQUENCE 201 AA; 22633 MW; 5BFEF424C7B32E00 CRC64;
AVYTLPELPY DYSALEPYIS GEIMELHHDK HHKAYVDGAN TALDKLAEAR DKADFGAINK
LEKDLAFNLA GHVNHSVFWK NMAPKGSAPE RPTDELGAAI DEFFGSFDNM KAQFTAAATG
IQGSGWASLV WDPLGKRINT LQFYDHQNNL PAGSIPLLQL DMWEHAFYLQ YKNVKGDYVK
SWWNVVNWDD VALRFSEARV A
