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   16-JUN-2009, entry version 27.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA; OrderedLocusNames=BP3852;
OS   Bordetella pertussis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=520;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION OF ITS ROLE IN
RP   SURVIVAL IN HUMAN POLYMORPHONUCLEAR LEUKOCYTES.
RC   STRAIN=BP504;
RX   MEDLINE=95131725; PubMed=7830550;
RX   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
RT   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   MEDLINE=22827954; 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.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., 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;
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 (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- MISCELLANEOUS: Essential for protection against exogenous
CC       H(2)O(2); however its absence does not affect survival of
CC       B.pertussis within human polymorphonuclear leukocytes.
CC   -!- SIMILARITY: Belongs to the catalase family.
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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; -.
DR   HSSP; P42321; 1M85.
DR   PRIDE; P0A323; -.
DR   GeneID; 2664864; -.
DR   GenomeReviews; BX470248_GR; BP3852.
DR   KEGG; bpe:BP3852; -.
DR   HOGENOM; P0A323; -.
DR   OMA; P0A323; NIARHIN.
DR   BioCyc; BPER257313:BP3852-MON; -.
DR   BRENDA; 1.11.1.6; 21511.
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   1: Evidence at protein level;
KW   Complete proteome; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Peroxidase.
FT   CHAIN         1    482       Catalase.
FT                                /FTId=PRO_0000084979.
FT   ACT_SITE     57     57       By similarity.
FT   ACT_SITE    130    130       By similarity.
FT   METAL       340    340       Iron (heme axial ligand) (By similarity).
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
//