ID   CATA_BORPE              Reviewed;         482 AA.
AC   P0A323; P48062;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA; OrderedLocusNames=BP3852;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION OF ITS ROLE IN
RP   SURVIVAL IN HUMAN POLYMORPHONUCLEAR LEUKOCYTES.
RC   STRAIN=BP504;
RX   PubMed=7830550; DOI=10.1111/j.1365-2958.1994.tb01272.x;
RA   DeShazer D., Wood G.E., Friedman R.L.;
RT   "Molecular characterization of catalase from Bordetella pertussis:
RT   identification of the katA promoter in an upstream insertion sequence.";
RL   Mol. Microbiol. 14:123-130(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Essential for protection against exogenous H(2)O(2);
CC       however its absence does not affect survival of B.pertussis within
CC       human polymorphonuclear leukocytes.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; U07800; AAA18481.1; -; Unassigned_DNA.
DR   EMBL; BX640422; CAE44107.1; -; Genomic_DNA.
DR   PIR; S60757; S60757.
DR   RefSeq; NP_882347.1; NC_002929.2.
DR   AlphaFoldDB; P0A323; -.
DR   SMR; P0A323; -.
DR   STRING; 257313.BP3852; -.
DR   KEGG; bpe:BP3852; -.
DR   PATRIC; fig|257313.5.peg.4162; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_2_0_4; -.
DR   OMA; WTCYVQV; -.
DR   SABIO-RK; P0A323; -.
DR   Proteomes; UP000002676; Chromosome.
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   1: Evidence at protein level;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW   Reference proteome.
FT   CHAIN           1..482
FT                   /note="Catalase"
FT                   /id="PRO_0000084979"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         340
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   482 AA;  54508 MW;  7CB73E08975C219F CRC64;
     MNAMTNKTLT TAAGAPVADN NNTMTAGPRG PALLQDVWFL EKLAHFDRER IPERVVHAKG
     SGAYGTFTVT HDISRYTRAR IFAEVGKQTP LFLRFSTVAG ERGAADAERD VRGFAIKFYT
     DEGNWDLVGN NTPVFFIRDP LKFPDFIHTQ KRDPKTNLRN ATAAWDFWSL NPESLHQVTI
     LMSDRGLPQN YRQQHGFGSH TYSFVNDAGE RFYVKFHFKS QQGIACYTDG EAAELVGRDR
     ESAQRDLFQN IEQGQFPRWT LKVQVMPEAE AATYHINPFD LTKVWPHADY PLIEVGVLEL
     NKNPENYFAE VEQAAFTPAN VVPGIGFSPD KMLQGRLFSY GDTHRYRLGI NHHQIPVNAP
     RCPFHSFHRD GMGRVDGNGG ATLNYEPNSF GEWREAKHAA EPPLALDGQA ADRWNHRVDE
     DYYSQPGALF RLMNDDQKQQ LFGNIGRHMA GVPEEIQRRQ LEHFRRADPA YAAGVAKALG
     LK