(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 70.
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}.
DR   EMBL; CP000675; ABQ54267.1; -; Genomic_DNA.
DR   RefSeq; WP_011945441.1; NC_009494.2.
DR   SMR; A5IA67; -.
DR   PRIDE; A5IA67; -.
DR   EnsemblBacteria; ABQ54267; ABQ54267; LPC_0271.
DR   KEGG; lpc:LPC_0271; -.
DR   HOGENOM; HOG000218110; -.
DR   KO; K03782; -.
DR   OMA; EEIFWGP; -.
DR   BioCyc; LPNE400673:LPC_RS01280-MONOMER; -.
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;
DR   PRODOM; A5IA67.
DR   SWISS-2DPAGE; A5IA67.
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   METAL           270
FT                   /note="Iron (heme axial ligand)"
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
//

If you have problems or comments...

PBIL Back to PBIL home page