KATG2_LEGPL
ID KATG2_LEGPL Reviewed; 749 AA.
AC Q5WZY1;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Catalase-peroxidase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE Flags: Precursor;
GN Name=katG2 {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=lpl0250;
OS Legionella pneumophila (strain Lens).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=297245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lens;
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; CR628337; CAH14481.1; -; Genomic_DNA.
DR RefSeq; WP_011214515.1; NC_006369.1.
DR AlphaFoldDB; Q5WZY1; -.
DR SMR; Q5WZY1; -.
DR PeroxiBase; 2397; LpnCP01_Lens.
DR EnsemblBacteria; CAH14481; CAH14481; lpl0250.
DR KEGG; lpf:lpl0250; -.
DR LegioList; lpl0250; -.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; KWTATRM; -.
DR Proteomes; UP000002517; Chromosome.
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 Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CHAIN 28..749
FT /note="Catalase-peroxidase 2"
FT /id="PRO_0000354819"
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 270
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 104
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 107..229
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 255)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 229..255
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 107)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 749 AA; 82899 MW; F679F6E45F67F5D0 CRC64;
MFKRTIPLFA AFTLAISPSI FPNYAHAQED KPKTNQYWWP KMLDLSPLRQ PNATSNPMGE
KFNYAEEFNS LDLNAVIEDL KKLMTTSQDW WPADYGNYGP LFIRMSWHAA GTYRIYDGRG
GANGGFQRFA PQNSWPDNAN LDKARRLLWP IKQKYGRKIS WADLLVLAGN VAMESMGFKT
IGFAGGREDA WEAININWGT EGKWLESKRQ DKVGKLEKPL AATVMGLIYV NPEGPNGVPD
PLAAAEKIRE TFGRMAMNDE ETVALIAGGH AFGKTHGAAS GKYLGPAPEA AGIEEQGFGW
KNSYGSGKGK DTITSGLEGA WTVTPTHWSH NYLQNLFNFN WVKTKSPGGA IQWVPENSNA
SSMVPDAFDP SKRHAPVMLT TDLALKFDPV YSKIAKRFLD NPKEFDDAFA RAWFKLIHRD
MGPRSRYLGS LVPKEIMIWQ DPVPPVDYKL VDANDIANLK GKILNSGLTT PELVKTAWAS
ASTFRGTDMR GGANGARIRL APQKDWPAND PQELAKVLKT LESIQNNFNN AQADGKKISL
ADLIVLGGNA AIEQAAKQAG YDIIVPFTPG RTDATQGMTD VKSFEVLEPK ADGFRNYFDK
SNNMSPPEML VDKASLLKLS VPEMTVLVGG MRVLNANTGQ NQYGVFTDKP GTLNNDFFIN
LLSMSTEWKK SSETEGIYEG YDRKTGKLKW KATSVDLIFG ANSELRAVAE AYATDDAKDK
FIQDFVNAWV KVMTADRFDI KAANANINS
