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Database: UniProt
Entry: D3KVM5
LinkDB: D3KVM5
Original site: D3KVM5 
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   05-DEC-2018, entry version 24.
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
RP   152-168, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND 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
RT   preclude the auto-oxidation step in 4-aminophenol metabolism by
RT   Burkholderia sp. 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
CC       systems (By similarity). Involved in the metabolism of 4-
CC       aminophenol. May have an indirect role in hydroxyquinol metabolism
CC       by scavenging and detoxifying reactive species that promote its
CC       auto-oxidation (PubMed:20480210). {ECO:0000250|UniProtKB:P0AGD3,
CC       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
CC       family. {ECO:0000305}.
DR   EMBL; AB518002; BAI77484.1; -; Genomic_DNA.
DR   ProteinModelPortal; D3KVM5; -.
DR   SMR; D3KVM5; -.
DR   BioCyc; MetaCyc:MONOMER-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; 2.40.500.20; -; 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       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000441891.
FT   METAL        27     27       Iron. {ECO:0000250|UniProtKB:P09223}.
FT   METAL        74     74       Iron. {ECO:0000250|UniProtKB:P09223}.
FT   METAL       157    157       Iron. {ECO:0000250|UniProtKB:P09223}.
FT   METAL       161    161       Iron. {ECO:0000250|UniProtKB:P09223}.
FT   CONFLICT     17     20       PHMS -> DPMM (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    168    168       R -> A (in Ref. 1; AA sequence).
FT                                {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
//
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