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   03-AUG-2022, entry version 122.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA; OrderedLocusNames=jhp_0809;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   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., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC       protect cells from the toxic effects of hydrogen peroxide.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10013};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE001439; AAD06391.1; -; Genomic_DNA.
DR   PIR; F71885; F71885.
DR   RefSeq; WP_000247320.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZKX5; -.
DR   SMR; Q9ZKX5; -.
DR   STRING; 85963.jhp_0809; -.
DR   EnsemblBacteria; AAD06391; AAD06391; jhp_0809.
DR   KEGG; hpj:jhp_0809; -.
DR   PATRIC; fig|85963.30.peg.163; -.
DR   eggNOG; COG0753; Bacteria.
DR   OMA; WTCYVQV; -.
DR   Proteomes; UP000000804; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd08156; catalase_clade_3; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR040333; Catalase_3.
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   InterPro; IPR020835; Catalase_sf.
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   Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase.
FT   CHAIN           1..505
FT                   /note="Catalase"
FT                   /id="PRO_0000084988"
FT   ACT_SITE        56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         339
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
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