CATA_HELPY
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 03-AUG-2022, entry version 137.
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; Proteobacteria; 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}.
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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.C694_04480; -.
DR DrugBank; DB01942; Formic acid.
DR PaxDb; P77872; -.
DR EnsemblBacteria; AAD07923; AAD07923; HP_0875.
DR KEGG; hpy:HP_0875; -.
DR PATRIC; fig|85962.47.peg.930; -.
DR eggNOG; COG0753; Bacteria.
DR OMA; WTCYVQV; -.
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 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 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
