KATG2_LEGPC
ID KATG2_LEGPC Reviewed; 749 AA.
AC A5IA67;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=LPC_0271;
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; ABQ54267.1; -; Genomic_DNA.
DR RefSeq; WP_011945441.1; NC_009494.2.
DR AlphaFoldDB; A5IA67; -.
DR SMR; A5IA67; -.
DR KEGG; lpc:LPC_0271; -.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; EEIFWGP; -.
DR BioCyc; LPNE400673:LPC_RS01280-MON; -.
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_0000354817"
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; 82915 MW; 1DD32DE849B95182 CRC64;
MFKRTIPLFA AFTLAISPSV FPNYAHAQED KPKTNQYWWP KMLDLSPLRQ PNATSNPMGE
KFNYAEEFNS LDLNAVIEDL KKLMTTSQDW WPADYGNYGP LFIRMSWHAA GTYRIYDGRG
GANGGFQRFA PQNSWPDNAN LDKARRLLWP IKQKYGRKIS WADLLVLAGN VAMESMGFKT
IGFAGGREDA WEAININWGP EGKWLESKRQ DKDGKLEKPL AATVMGLIYV NPEGPNGVPD
PLAAAEKIRE TFGRMAMNDE ETVALIAGGH AFGKTHGAAS GKYLGPAPEA AGIEEQGFGW
KNSYGSGKGK DTITSGLEGA WTVTPTHWSH NYLQNLFNFN WVKTKSPGGA IQWVPENSNA
SSMVPDAFDP SKRHAPVMLT TDLALKFDPV YSKIAKRFLD NPKEFDDAFA RAWFKLIHRD
MGPRSRYLGS LVPKEVMIWQ DPVPPVDYKL VDANDIANLK GKILNSGLTT SELVKTAWAS
ASTFRGTDMR GGANGARIRL APQKDWPAND PQELAKVLKT LESIQNNFNN AQADGKKISL
ADLIVLGGNA AIEQAAKQAG YDIIVPFMPG RTDATQGMTD VKSFEVLEPK ADGFRNYFDK
SNNMSPPEML VEKASLLKLS VPEMTVLVGG MRVLNANTGQ NQYGVFTDKP GILNNDFFVN
LLSMSTEWKK SSETEGIYEG YDRKTGKLKW KATSVDLIFG ANSELRAVAE AYATDDAKDK
FIQDFVNAWV KVMTADRFDI KAANANINS
