ID   KATG1_LEGPC             Reviewed;         721 AA.
AC   A5IF70;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Catalase-peroxidase 1 {ECO:0000255|HAMAP-Rule:MF_01961};
DE            Short=CP 1 {ECO:0000255|HAMAP-Rule:MF_01961};
DE            EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE   AltName: Full=Peroxidase/catalase 1 {ECO:0000255|HAMAP-Rule:MF_01961};
GN   Name=katG1 {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=LPC_2090;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) 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; CP000675; ABQ56020.1; -; Genomic_DNA.
DR   RefSeq; WP_011947306.1; NC_009494.2.
DR   AlphaFoldDB; A5IF70; -.
DR   SMR; A5IF70; -.
DR   KEGG; lpc:LPC_2090; -.
DR   HOGENOM; CLU_025424_2_0_6; -.
DR   OMA; MILAGNC; -.
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..721
FT                   /note="Catalase-peroxidase 1"
FT                   /id="PRO_0000354816"
FT   ACT_SITE        99
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            95
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        98..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                   98)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   721 AA;  80488 MW;  DE864894F5075A59 CRC64;
     MDGKVGNTTT GCPVMHGGMT SAGTSNTAWW PNALNLDILH QHDTKTNPMG KDFNYREEVK
     KLNFEALKKD LHALMTDSQA WWPADWGHYG GLMIRMSWHA AGSYRVADGR GGAGTGNQRF
     APLNSWPDNV NLDKARRLLW PIKKKYGNKI SWADLIVLAG TIAYESMGLK TFGFGFGRED
     IWHPEKDVYW GSEQEWLGAK RYDDKDRQSL ETPLAAVQMG LIYVNPEGVN GQPDPLRTAQ
     DVRVTFGRMA MNDEETVALT AGGHTVGKCH GNGNAKFLGP EPEAADIEDQ GLGWINKTTR
     GIGRNTVSSG IEGAWTTHPT QWDNGYFYLL LNYDWELKKS PAGAWQWEPI HIKEEDKPVD
     VEDPAIRHNP IMTDADMAIK MDPVYRKIAE RFYKDPDYFA EVFARAWFKL THRDMGPKTR
     YIGPDVPKED LIWQDPVPAG NRAYDIAAAK AKIAASNLTI GEMVSTAWDS ARTFRGSDKR
     GGANGARIRL KPQKDWEGNE PQRLTKVLRI LEDIAADTGA SVADVIVLAG NVGIEKAAKA
     AGFDIIVPFA PGRGDATDDM TDAESFDVLE PLHDGYRNWL KKAYDVRPEE LMLDRTQLMG
     LTAHEMTVLV GGLRVLGTNH NNTQHGVFTD RVGALTNDFF VNLTDMANVW IPSKDNLYEI
     RDRKAGNIKW TATRVDLVFG SNSILRSYAE VYAQDDNKGK FIQDFVAAWT KVMNADRFDL
     A