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Database: UniProt
Entry: Q59714
LinkDB: Q59714
Original site: Q59714 
ID   CATA_PSEPU              Reviewed;         479 AA.
AC   Q59714;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   26-NOV-2014, entry version 67.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA; Synonyms=catA;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Corvallis;
RX   PubMed=9358059; DOI=10.1016/S0378-1119(97)00370-3;
RA   Kim Y.C., Miller C.D., Anderson A.J.;
RT   "Identification of adjacent genes encoding the major catalase and a
RT   bacterioferritin from the plant-beneficial bacterium Pseudomonas
RT   putida.";
RL   Gene 199:219-224(1997).
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen;
CC       serves to protect cells from the toxic effects of hydrogen
CC       peroxide.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC       {ECO:0000255|PROSITE-ProRule:PRU10013}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- ENZYME REGULATION: Activated by peroxide.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; U63511; AAB88219.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q59714; -.
DR   SMR; Q59714; 2-479.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.180.10; -; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR020835; Catalase-like_dom.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   PANTHER; PTHR11465; PTHR11465; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; SSF56634; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase.
FT   CHAIN         1    479       Catalase.
FT                                /FTId=PRO_0000084995.
FT   ACT_SITE     53     53       {ECO:0000255|PROSITE-ProRule:PRU10013}.
FT   ACT_SITE    126    126       {ECO:0000255|PROSITE-ProRule:PRU10013}.
FT   METAL       336    336       Iron (heme axial ligand). {ECO:0000250}.
SQ   SEQUENCE   479 AA;  53381 MW;  EFE3CBDE67778571 CRC64;
     MSKILTTASG APVADNQNSR SAGPRGPLLL DDFHLIEKLA HFNRENIPER RVHAKGSGAY
     GTFTVTRDIT GYTSAKLFEQ VGKQTETFLR FSTVGGERGS ADTERDPRGF AVKFYTEEGN
     WDIVGNNTPV FFIRDPLKFP DFIHTQKRHP QSNLKNAQIF WDSWSHSPEA LHQVTILFSD
     RGIPDGYRHM HGFGSHTYSL INAQGERTWV KWHFKTQQGI KNLAPADAAR LAGTDPDYAQ
     RDLFEAIERG DYPRWTVCIQ VMSEAEAASR DENPFDVTKT WSQKDYPLIE VGVLELNRNP
     LNYFAEVEQA AFGPSNMVPG VGLSPDRMLQ GRVFAYADAH RYRVGTNHQQ LPVNAPRCPV
     NSYQRDGSMA TGSYGSAPNY EPNSYAAAPK QSPRHAEPAL ALNGSADRYD HREDADYYSH
     AGALFRLMSD EQKALLISNI AGTMAGVSEN VIQRQLQYFF KADPAYGEGI AKGLGINLA
//
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