ID CATA_HELPY Reviewed; 505 AA. AC P77872; P94823; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 27-MAR-2024, entry version 145. DE RecName: Full=Catalase; DE EC=1.11.1.6; GN Name=katA; OrderedLocusNames=HP_0875; OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85962; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=RU1; RX PubMed=9546115; DOI=10.1046/j.1523-5378.1998.08030.x; RA Manos J., Kolesnikow T., Hazell S.L.; RT "An investigation of the molecular basis of the spontaneous occurrence of a RT catalase-negative phenotype in Helicobacter pylori."; RL Helicobacter 3:28-38(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=P1; RX PubMed=8955320; DOI=10.1128/jb.178.23.6960-6967.1996; RA Odenbreit S., Wieland B., Haas R.; RT "Cloning and genetic characterization of Helicobacter pylori catalase and RT construction of a catalase-deficient mutant strain."; RL J. Bacteriol. 178:6960-6967(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). 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 -!- INTERACTION: CC P77872; O25542: HP_0874; NbExp=3; IntAct=EBI-7585674, EBI-7585664; 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; U67458; AAC16068.1; -; Genomic_DNA. DR EMBL; Z70679; CAA94567.1; -; Genomic_DNA. DR EMBL; AE000511; AAD07923.1; -; Genomic_DNA. DR PIR; C64629; C64629. DR RefSeq; NP_207669.1; NC_000915.1. DR RefSeq; WP_000247370.1; NC_018939.1. DR PDB; 1QWL; X-ray; 1.60 A; A/B=1-505. DR PDB; 1QWM; X-ray; 1.60 A; A/B=1-505. DR PDB; 2A9E; X-ray; 1.76 A; A/B=1-505. DR PDB; 2IQF; X-ray; 1.86 A; A/B=1-505. DR PDBsum; 1QWL; -. DR PDBsum; 1QWM; -. DR PDBsum; 2A9E; -. DR PDBsum; 2IQF; -. DR AlphaFoldDB; P77872; -. DR SMR; P77872; -. DR DIP; DIP-3559N; -. DR IntAct; P77872; 2. DR MINT; P77872; -. DR STRING; 85962.HP_0875; -. DR DrugBank; DB01942; Formic acid. DR MetOSite; P77872; -. DR PaxDb; 85962-C694_04480; -. DR EnsemblBacteria; AAD07923; AAD07923; HP_0875. DR KEGG; hpy:HP_0875; -. DR PATRIC; fig|85962.47.peg.930; -. DR eggNOG; COG0753; Bacteria. DR InParanoid; P77872; -. DR OrthoDB; 3169619at2; -. DR PhylomeDB; P77872; -. DR SABIO-RK; P77872; -. DR EvolutionaryTrace; P77872; -. DR Proteomes; UP000000429; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004096; F:catalase activity; IBA:GO_Central. DR GO; GO:0020037; F:heme binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:CACAO. DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central. DR CDD; cd08156; catalase_clade_3; 1. DR Gene3D; 2.40.180.10; Catalase core domain; 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; CATALASE; 1. DR PANTHER; PTHR11465:SF61; CATALASE; 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; Heme-dependent catalase-like; 1. DR PROSITE; PS00437; CATALASE_1; 1. DR PROSITE; PS00438; CATALASE_2; 1. DR PROSITE; PS51402; CATALASE_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; KW Oxidoreductase; Peroxidase; Reference proteome. FT CHAIN 1..505 FT /note="Catalase" FT /id="PRO_0000084987" 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" FT CONFLICT 82 FT /note="S -> F (in Ref. 1; AAC16068)" FT /evidence="ECO:0000305" FT CONFLICT 234 FT /note="V -> I (in Ref. 2; CAA94567)" FT /evidence="ECO:0000305" FT CONFLICT 237 FT /note="Y -> H (in Ref. 2; CAA94567)" FT /evidence="ECO:0000305" FT CONFLICT 248 FT /note="N -> D (in Ref. 2; CAA94567)" FT /evidence="ECO:0000305" FT CONFLICT 255 FT /note="F -> Y (in Ref. 2; CAA94567)" FT /evidence="ECO:0000305" FT CONFLICT 286 FT /note="L -> T (in Ref. 2; CAA94567)" FT /evidence="ECO:0000305" FT CONFLICT 313 FT /note="A -> V (in Ref. 1; AAC16068)" FT /evidence="ECO:0000305" FT CONFLICT 316 FT /note="S -> T (in Ref. 1; AAC16068 and 2; CAA94567)" FT /evidence="ECO:0000305" FT STRAND 24..26 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 36..45 FT /evidence="ECO:0007829|PDB:1QWL" FT STRAND 58..68 FT /evidence="ECO:0007829|PDB:1QWL" FT TURN 73..75 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:1QWL" FT STRAND 87..95 FT /evidence="ECO:0007829|PDB:1QWL" FT STRAND 105..109 FT /evidence="ECO:0007829|PDB:1QWL" FT STRAND 112..119 FT /evidence="ECO:0007829|PDB:1QWL" FT STRAND 122..132 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 139..141 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 142..149 FT /evidence="ECO:0007829|PDB:1QWL" FT TURN 153..155 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 160..169 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 171..173 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 174..181 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 183..185 FT /evidence="ECO:0007829|PDB:1QWL" FT STRAND 186..189 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 190..192 FT /evidence="ECO:0007829|PDB:1QWL" FT STRAND 201..204 FT /evidence="ECO:0007829|PDB:1QWL" FT STRAND 210..219 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 228..235 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 241..251 FT /evidence="ECO:0007829|PDB:1QWL" FT STRAND 257..266 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 267..269 FT /evidence="ECO:0007829|PDB:1QWL" FT TURN 270..272 FT /evidence="ECO:0007829|PDB:1QWL" FT TURN 286..288 FT /evidence="ECO:0007829|PDB:1QWL" FT STRAND 292..301 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 306..309 FT /evidence="ECO:0007829|PDB:1QWL" FT TURN 310..312 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 330..347 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 351..353 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 355..357 FT /evidence="ECO:0007829|PDB:1QWL" FT TURN 376..379 FT /evidence="ECO:0007829|PDB:1QWL" FT STRAND 387..389 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 395..397 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 404..406 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 418..421 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 427..435 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 438..452 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 458..471 FT /evidence="ECO:0007829|PDB:1QWL" FT HELIX 473..489 FT /evidence="ECO:0007829|PDB:1QWL" SQ SEQUENCE 505 AA; 58629 MW; 9F029B55B73C26EA CRC64; MVNKDVKQTT AFGAPVWDDN NVITAGPRGP VLLQSTWFLE KLAAFDRERI PERVVHAKGS GAYGTFTVTK DITKYTKAKI FSKVGKKTEC FFRFSTVAGE RGSADAVRDP RGFAMKYYTE EGNWDLVGNN TPVFFIRDAI KFPDFIHTQK RDPQTNLPNH DMVWDFWSNV PESLYQVTWV MSDRGIPKSF RHMDGFGSHT FSLINAKGER FWVKFHFHTM QGVKHLTNEE AAEVRKYDPD SNQRDLFNAI ARGDFPKWKL SIQVMPEEDA KKYRFHPFDV TKIWYLQDYP LMEVGIVELN KNPENYFAEV EQAAFSPANV VPGIGYSPDR MLQGRLFSYG DTHRYRLGVN YPQIPVNKPR CPFHSSSRDG YMQNGYYGSL QNYTPSSLPG YKEDKSARDP KFNLAHIEKE FEVWNWDYRA DDSDYYTQPG DYYRSLPADE KERLHDTIGE SLAHVTHKEI VDKQLEHFKK ADPKYAEGVK KALEKHQKMM KDMHGKDMHH TKKKK //