ID   KATG2_LEGPA             Reviewed;         749 AA.
AC   Q5X8J8;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   01-MAY-2013, entry version 64.
DE   RecName: Full=Catalase-peroxidase 2;
DE            Short=CP 2;
DE            EC=1.11.1.21;
DE   AltName: Full=Peroxidase/catalase 2;
DE   Flags: Precursor;
GN   Name=katG2; OrderedLocusNames=lpp0252;
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.,
RA   Etienne J., Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of
RT   host cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-
CC       spectrum peroxidase activity (By similarity).
CC   -!- CATALYTIC ACTIVITY: Donor + H(2)O(2) = oxidized donor + 2 H(2)O.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC   -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per dimer
CC       (By similarity).
CC   -!- SUBUNIT: Homodimer or homotetramer (By similarity).
CC   -!- PTM: The covalent Trp-Tyr-Met adduct is important for the
CC       catalase, but not the peroxidase activity of the enzyme (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC       subfamily.
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DR   EMBL; CR628336; CAH11399.1; -; Genomic_DNA.
DR   RefSeq; YP_122595.1; NC_006368.1.
DR   HSSP; O59651; 1ITK.
DR   ProteinModelPortal; Q5X8J8; -.
DR   SMR; Q5X8J8; 34-740.
DR   STRING; 297246.lpp0252; -.
DR   PeroxiBase; 2398; LpnCP01_Paris.
DR   PRIDE; Q5X8J8; -.
DR   EnsemblBacteria; CAH11399; CAH11399; lpp0252.
DR   GeneID; 3117738; -.
DR   KEGG; lpp:lpp0252; -.
DR   PATRIC; 22320678; VBILegPne27771_0420.
DR   LegioList; lpp0252; -.
DR   eggNOG; COG0376; -.
DR   HOGENOM; HOG000218110; -.
DR   KO; K03782; -.
DR   OMA; WKNKCGK; -.
DR   ProtClustDB; PRK15061; -.
DR   GO; GO:0004096; F:catalase activity; IEA:HAMAP.
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   HAMAP; MF_01961; Catal-peroxid; 1; -.
DR   InterPro; IPR000763; Catalase_peroxidase.
DR   InterPro; IPR010255; Haem_peroxidase.
DR   InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   Pfam; PF00141; peroxidase; 2.
DR   PRINTS; PR00460; BPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; Peroxidase_super; 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   Complete proteome; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Peroxidase; Signal.
FT   SIGNAL        1     27       Potential.
FT   CHAIN        28    749       Catalase-peroxidase 2.
FT                                /FTId=PRO_0000354821.
FT   ACT_SITE    108    108       Proton acceptor (By similarity).
FT   METAL       270    270       Iron (heme axial ligand) (By similarity).
FT   SITE        104    104       Transition state stabilizer (By
FT                                similarity).
FT   CROSSLNK    107    229       Tryptophyl-tyrosyl-methioninium (Trp-Tyr)
FT                                (with M-255) (By similarity).
FT   CROSSLNK    229    255       Tryptophyl-tyrosyl-methioninium (Tyr-Met)
FT                                (with W-107) (By similarity).
SQ   SEQUENCE   749 AA;  82988 MW;  4665876E0BA2FE15 CRC64;
     MFKRTIPLFA AFTLAISPSV FPNYAYAQED KPKTNQYWWP KMLDLSPLRQ PNATSNPMGE
     QFNYAEEFNS 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 LVPKEIMIWQ DPVPPVDYKL VDANDIANLK GKILNSGLST SELVKTAWAS
     ASTFRGTDMR GGANGARIRL SPQKDWPAND PQELAKVLKT LESIQNNFNN AQADGKKISL
     ADLIVLGGNA AIEQAAKQAG YDIIVPFMPG RTDATQGMTD VKSFEVLEPK ADGFRNYFDK
     SNNMSPPEML VEKASLLKLS VPQMTVLVGG MRVLNANTGQ NQYGVFTDKP GTLNNDFFVN
     LLSMSTEWKK SSETEGIYEG YDRKTGKLKW KATSVDLIFG ANSELRAVAE AYATDDAKEK
     FIQDFVNAWV KVMTADRFDI KAANTNINS
//