ID   KATG_ECOLX              Reviewed;         736 AA.
AC   P0C8F0; P77038;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
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};
DE   Flags: Precursor;
GN   Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; Synonyms=katP;
OS   Escherichia coli.
OG   Plasmid pO103.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=O103:H2 / 5714/96 / EHEC;
RA   Brunder W., Ripke I.;
RT   "The large plasmid of enterohemorrhagic Escherichia coli (EHEC) O103:H2.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC       peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961}.
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; AJ243564; CAC80498.1; -; Genomic_DNA.
DR   RefSeq; WP_000592771.1; NZ_WSWV01000078.1.
DR   RefSeq; YP_002756743.1; NC_012487.1.
DR   AlphaFoldDB; P0C8F0; -.
DR   SMR; P0C8F0; -.
DR   OMA; EEIFWGP; -.
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;
KW   Plasmid; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CHAIN           24..736
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_5000146557"
FT   ACT_SITE        103
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         264
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            99
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        102..223
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   249)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        223..249
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   102)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   736 AA;  81794 MW;  F3EA593D3FDEDB8D CRC64;
     MIKKTLPVLI LLALSGSFST AVAADKKETQ NFYYPETLDL TPLRLHSPES NPWGADFDYA
     TRFQQLDMEA LKKDIKDLLT TSQDWWPADY GHYGPFFIRM AWHGAGTYRT YDGRGGASGG
     QQRFEPLNSW PDNVNLDKAR RLLWPVKKKY GSSISWGDLM VLTGNVALES MGFKTLGFAG
     GREDDWESDL VYWGPDNKPL ADNRDKNGKL QKPLAATQMG LIYVNPEGPG GKPDPLASAK
     DIREAFSRMA MDDEETVALI AGGHTFGKAH GAASPEKCIG AGPDGAPVEE QGLGWKNKCG
     TGNGKYTITS GLEGAWSTSP TQFTMQYLKN LYKYEWELHK SPAGAYQWKP KKAANIVQDA
     HDPSVLHPLM MFTTDIALKV DPEYKKITTR FLNDPKAFEQ AFARAWFKLT HRDMGPAARY
     LGNEVPAESF IWQDPLPAAD YTMIDGKDIK SLKEQVMDLG IPASELIKTA WASASTFRVT
     DYRGGNNGAR IRLQPEINWE VNEPEKLKKV LASLTSLQRE FNKKQSDGKK VSLADLIVLS
     GNAAIEDAAR KAGVELEIPF TPGRTDASQE QTDVASFSVL EPTADGFRNY YSKSRSHISP
     VESLIDKASQ LDLTVPEMTA LLGGLRVMDI NTNNSSLGVF TDTPGVLDNK FFVNLLDMST
     RWSKADKEDT YNGFDRKTGA LKWKASSVDL IFSSNPELRA VAEVYASDDA RNKFIHDFVK
     SWNKVMNSDR FDLNNK