SODF_BURSP
ID SODF_BURSP Reviewed; 193 AA.
AC D3KVM5;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Superoxide dismutase [Fe] {ECO:0000305};
DE EC=1.15.1.1 {ECO:0000269|PubMed:20480210};
DE AltName: Full=SOD-like protein {ECO:0000303|PubMed:20480210};
OS Burkholderia sp.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=36773;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-23 AND 152-168,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=AK-5;
RX PubMed=20480210; DOI=10.1007/s10532-010-9369-5;
RA Takenaka S., Koshiya J., Okugawa S., Takata A., Murakami S., Aoki K.;
RT "Fe-superoxide dismutase and 2-hydroxy-1,4-benzoquinone reductase preclude
RT the auto-oxidation step in 4-aminophenol metabolism by Burkholderia sp.
RT strain AK-5.";
RL Biodegradation 22:1-11(2011).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems (By
CC similarity). Involved in the metabolism of 4-aminophenol. May have an
CC indirect role in hydroxyquinol metabolism by scavenging and detoxifying
CC reactive species that promote its auto-oxidation (PubMed:20480210).
CC {ECO:0000250|UniProtKB:P0AGD3, ECO:0000269|PubMed:20480210}.
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:20480210};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:20480210};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:20480210};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:20480210};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20480210}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AB518002; BAI77484.1; -; Genomic_DNA.
DR AlphaFoldDB; D3KVM5; -.
DR SMR; D3KVM5; -.
DR BioCyc; MetaCyc:MON-17536; -.
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 Direct protein sequencing; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..193
FT /note="Superoxide dismutase [Fe]"
FT /id="PRO_0000441891"
FT BINDING 27
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09223"
FT BINDING 74
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09223"
FT BINDING 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09223"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09223"
FT CONFLICT 17..20
FT /note="PHMS -> DPMM (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="R -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 193 AA; 21513 MW; 263E1749D9905E17 CRC64;
MEHTLPPLPF DKNALAPHMS EETLEYHYGK HHQTYVTNLN KLIPGTEFEN LSLEEIVKKS
SGGVFNNSAQ VWNHTFFWNS LSPKGGGAPT GALADAINAK YGSFDKFKEE FAKVATGTFG
SGWTWLVKKT DGTVDIVSTS NAATPLTTDA KALLTIDVWE HAYYIDYRNA RPKFIEAYWN
IANWDFAAKN FGA