ID   KATG_EDWTA              Reviewed;         724 AA.
AC   Q4G4B1;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 68.
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};
OS   Edwardsiella tarda.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PPD130/91;
RX   PubMed=16000720; DOI=10.1099/mic.0.28005-0;
RA   Tan Y.P., Zheng J., Tung S.L., Rosenshine I., Leung K.Y.;
RT   "Role of type III secretion in Edwardsiella tarda virulence.";
RL   Microbiology 151:2301-2313(2005).
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; AY643478; AAY43639.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4G4B1; -.
DR   SMR; Q4G4B1; -.
DR   STRING; 667121.ET1_20_00150; -.
DR   PeroxiBase; 3619; EtaCP01_PPD130.
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   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; 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..724
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_0000354770"
FT   ACT_SITE        99
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         267
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            95
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        98..226
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   252)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        226..252
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   98)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   724 AA;  79880 MW;  46D7DF00FB03F10D CRC64;
     MGNNNEFSSG KCPVMHGGMT SAGMASKDWW PNALNLDILH QHDTKTNPMG QQFNYREALK
     QLDVQALKDD LRALMTDSQP WWPADWGHYG GLMVRMAWHS AGSYRIADGR GGAGTGNQRF
     APLNSWPDNV NLDKARRLLW PIKKKYGNKI SWADLIVLAG TMAYESMGLK TFGFAFGRED
     IWHPEIDTYW GSEKEWLAPS GSEGSRYSGE RDLENPLAAV MMGLIYVNPE GVDGHPDPQK
     TANDVRVTFA RMAMNDEETV ALTAGGHTVG KCHGNGSAAN LGAAPEGADL QEQGLGWNNH
     TTRGIDRDTV SSGIEGAWTS KPTQWDNGYF DMLLGHEWTL TKSPAGAWQW VPIQIAEEDK
     PVDVEDPSIR LLPIMTDADM AMKVDPTYRQ IAERFRQDPA YFSDVFARAW FKLTHRDLGP
     KSRYFGPDVP QEALIWQDPV PAGRSEYDVA AVKAKIAASG LSIADMVSTA WDSARTFRGS
     DKRGGANGAR IRLAPQNTWE GNEPARLAKV LAVLEPIAAE FNVSVADVIV LAGNLGIEQA
     AKAAGVAIEV PFAPGRGDAT QAMTDEASFE VLEPLADGFR NWLKKDYVVT AEELLLDRAQ
     LMRLTACEMT VLIGGMRVLG ANYGGSKVGV FTDRIGVLSN DFFVNLTDMS YTWKPTASNL
     YEIRERANGA LKWTASRVDL VFGSNSILRA YAEVYAQDDN KEKFVRDFVA AWTKVMNADR
     YDLR