ID   KATG_BURCE              Reviewed;         760 AA.
AC   Q9AP06;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_01961};
DE            Short=CP {ECO:0000255|HAMAP-Rule:MF_01961};
DE            EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE   AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
GN   Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; Synonyms=katA;
OS   Burkholderia cepacia (Pseudomonas cepacia).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=C5424;
RX   PubMed=15942004; DOI=10.1099/mic.0.27704-0;
RA   Lefebre M.D., Flannagan R.S., Valvano M.A.;
RT   "A minor catalase/peroxidase from Burkholderia cenocepacia is required for
RT   normal aconitase activity.";
RL   Microbiology 151:1975-1985(2005).
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC       peroxidase activity. Required for maintaining the normal activity of
CC       the TCA cycle. {ECO:0000255|HAMAP-Rule:MF_01961,
CC       ECO:0000269|PubMed:15942004}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01961};
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=1.11.1.21;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC       {ECO:0000255|HAMAP-Rule:MF_01961};
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC   -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is important
CC       for the catalase, but not the peroxidase activity of the enzyme.
CC       {ECO:0000255|HAMAP-Rule:MF_01961}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
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DR   EMBL; AF317697; AAG60688.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AP06; -.
DR   SMR; Q9AP06; -.
DR   PeroxiBase; 2323; BcCP01.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
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   HAMAP; MF_01961; Catal_peroxid; 1.
DR   InterPro; IPR000763; Catalase_peroxidase.
DR   InterPro; IPR002016; Haem_peroxidase.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   PANTHER; PTHR30555; PTHR30555; 1.
DR   Pfam; PF00141; peroxidase; 2.
DR   PRINTS; PR00460; BPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; SSF48113; 2.
DR   TIGRFAMs; TIGR00198; cat_per_HPI; 1.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   3: Inferred from homology;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT   CHAIN           1..760
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_0000354738"
FT   ACT_SITE        92
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         268
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   SITE            88
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        91..227
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   253)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        227..253
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   91)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   760 AA;  83315 MW;  5ECA94CF843676C4 CRC64;
     MSNEGQCPFN HANGGGTTNR DWWPNELRLD LLSQHSSKTD PLDPGFNYAE AFNSLDLDAL
     RKDLAALMTD SQDWWPADFG HYGPLFVRMA WHSAGTYRMG DGRGGAGRGQ QRFAPLNSWP
     DNVSLDKARR LLWPIKQKYG QKISWADLLI LTGDVALTTM GFKTFGYAGG REDTWEPDRD
     VYWGSETTWL GGDLRYDKGG ACESQHGGNA GRNLENPLAA VQMDLIYNPE GGPDGNPDPV
     AAAYDIREVF GRMAMNDEET VALIAGGHAF GKTHGAGPAD NVGLEPEAAG LEQQGLGWKN
     SFGTGKGADT ITSGLEVTWS DTPTQWGMGF FKNLFGYEWE LTKSPAGAHQ WVAKNAEPTI
     PHAHDPSKKL LPTMLTTDLS LRFDPVYEKI SRHFMDNPDV FADAFARAWF KLTHRDMGPR
     ARYLGPDVPT EELIWQDPIP AVDHVLTTRN VAPLKETILA SGLSVAELVS TAWASASTFR
     GSDKRGGANG ARIRLAPQKD WAVNEPARLA KVLKVLERIQ GEFNSTQPGG KKISLADLIV
     LAGGAGIEQA AKRAGHDVVV PFAPGRMDAS QEQTDAHSFA VLEPVADGFR NFVKGKFAVP
     AEALLIDKAQ LLTLTAPQMT ALVGGLRVLN VQTGDEKHGV FTDQPETLTV DFFRNLLDMA
     TEWKPIAGED TYEGRDRRTG ELKWTGTRVD LVFGSNAVLR ALSEVYASAD GEAKFIRDFV
     AAWVKVMNLD RFDLACKKRW YIDASGLPGE PALSARIQWR