ID   CATA_HELPJ              Reviewed;         505 AA.
AC   Q9ZKX5;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA; OrderedLocusNames=jhp_0809;
OS   Helicobacter pylori J99 (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=99120557; PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G.,
RA   Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C.,
RA   Gibson R., Merberg D., Mills S.D., Jiang Q., Taylor D.E., Vovis G.F.,
RA   Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human
RT   gastric pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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   -!- COFACTOR: Heme group.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the catalase family.
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DR   EMBL; AE001439; AAD06391.1; -; Genomic_DNA.
DR   PIR; F71885; F71885.
DR   RefSeq; NP_223527.1; -.
DR   HSSP; P42321; 2CAG.
DR   SMR; Q9ZKX5; 1-491.
DR   PRIDE; Q9ZKX5; -.
DR   GeneID; 890086; -.
DR   GenomeReviews; AE001439_GR; jhp_0809.
DR   KEGG; hpj:jhp0809; -.
DR   NMPDR; fig|85963.1.peg.805; -.
DR   HOGENOM; Q9ZKX5; -.
DR   OMA; Q9ZKX5; NCPFRAR.
DR   BioCyc; HPYL85963:JHP0809-MON; -.
DR   BRENDA; 1.11.1.6; 295085.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004096; F:catalase activity; IEA:EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002226; Catalase.
DR   InterPro; IPR010582; Catalase-rel_immune_responsive.
DR   InterPro; IPR011614; Catalase_N.
DR   InterPro; IPR018028; Catalase_rel_subgroup.
DR   Gene3D; G3DSA:2.40.180.10; Catalase_N; 1.
DR   PANTHER; PTHR11465; Catalase; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PRINTS; PR00067; CATALASE.
DR   ProDom; PD000510; Catalase; 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   Complete proteome; Cytoplasm; Heme; Hydrogen peroxide; Iron;
KW   Metal-binding; Oxidoreductase; Peroxidase.
FT   CHAIN         1    505       Catalase.
FT                                /FTId=PRO_0000084988.
FT   ACT_SITE     56     56       By similarity.
FT   ACT_SITE    129    129       By similarity.
FT   METAL       339    339       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   505 AA;  58527 MW;  475A07EF6EF9B309 CRC64;
     MVNKDVKQTT AFGAPVWDDN NVITAGPRGP VLLQSTWFLE KLAAFDRERI PERVVHAKGS
     GAYGTFTVTK DITKYTKAKI FSKVGKKTEC FFRFSTVAGE KGSADAVRDP RGFAMKYYTE
     EGNWDLVGNN TPVFFIRDAI KFPDFIHTQK RDPQTNLPNP DMVWDFWSNV PESLYQVTWV
     MSDRGIPKSF RHMDGFGSHT FSLINAKGER FWVKFHFETM QGVKHLTNEE AAEVRKYDPD
     SNQRDLFDAI AGGDFPKWKM SIQVMPEEDA KKYRFHPFDV TKIWYLQDYP LMEVGIVELN
     KNPENYFAEV EQAAFTPANV VPGIGYSPDR MLQGRLFSYG DTHRYRLGVN YPQIPVNRPR
     CPFHSSSRDG YMQNGYYGSL QNYTPSSLPG YKEDKSARDP KFNLAHIEKE FEVWNWDYRA
     EDSDYYTQPG DYYRSLPADE KERLYDTIGG SLAHVTHKEI VDKQLEHFKK ADPKYAEGVK
     KALEKHQKMM KDMHAKDMHH MKKKK
//