ID   KATG1_LEGPA             Reviewed;         721 AA.
AC   Q5X2D9;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=lpp2454;
OS   Legionella pneumophila (strain Paris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Paris;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
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; CR628336; CAH13607.1; -; Genomic_DNA.
DR   RefSeq; WP_015961570.1; NC_006368.1.
DR   AlphaFoldDB; Q5X2D9; -.
DR   SMR; Q5X2D9; -.
DR   PeroxiBase; 2641; LpnCP02_Paris.
DR   KEGG; lpp:lpp2454; -.
DR   LegioList; lpp2454; -.
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_0000354820"
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;  80503 MW;  353ACF8C86D71A60 CRC64;
     MDGKVGNTAT GCPVIHGGMT SAETSNTAWW PNALNLDILH QHDTKTNPMG KDFNYREEVK
     KLDFVAFKKD 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 LIWQDPVPSG NRAYDIAAAK AKIAASNLTI GEMVSTAWDS ARTFRGSDKR
     GGANGARIRL KPQKDWEGNE PQRLTKVLRI LEGIAADTGA SVADVIVLAG NVGIEKAAKA
     AGFDIIVPFA PGRGDATDDM TDAESFDVLE PLHDGYRNWL KKAYDVRPEE LMLDRTQLMG
     LTAHEMTVLV GGLRVLGTNH NNTQHGVFTD RVGVLTNDFF VNLTDMANVW IPSKDNLYEI
     RDRKAGNIKW TATRVDLVFG SNSILRSYAE VYAQDDNKGK FIQDFVAAWT KVMNADRFDL
     A