KATG_PARPJ
ID KATG_PARPJ Reviewed; 753 AA.
AC B2T4H0;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=Bphyt_2078;
OS Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS (Burkholderia phytofirmans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=398527;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX PubMed=21551308; DOI=10.1128/jb.05055-11;
RA Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.;
RT "Complete genome sequence of the plant growth-promoting endophyte
RT Burkholderia phytofirmans strain PsJN.";
RL J. Bacteriol. 193:3383-3384(2011).
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; CP001052; ACD16481.1; -; Genomic_DNA.
DR RefSeq; WP_012433080.1; NC_010681.1.
DR AlphaFoldDB; B2T4H0; -.
DR SMR; B2T4H0; -.
DR STRING; 398527.Bphyt_2078; -.
DR PeroxiBase; 6384; BphyCP01.
DR EnsemblBacteria; ACD16481; ACD16481; Bphyt_2078.
DR KEGG; bpy:Bphyt_2078; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_4; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000001739; Chromosome 1.
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.
FT CHAIN 1..753
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354746"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 284
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 88
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 91..243
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 269)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 243..269
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 91)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 753 AA; 82213 MW; 331CD6762553EE67 CRC64;
MSSEAKCPFN HAAGGGTTNR DWWPKQLRLD LLSQHSSKSD PLDGSFNYAE AFKTLDLAAV
KKDLAALMTD SQDWWPADFG HYGPLFIRMA WHSAGTYRIG DGRGGAGRGQ QRFAPLNSWP
DNVSLDKARR LLWPIKQKYG QKISWADLLI LTGNVALETM GFKTFGFAGG RPDTWEPDQD
VYWGNEKTWL GGDVRYGKGA AGNEEDGGVI VADVEKHGEE VSRDDNGRIL ENPLGAVQMG
LIYVNPEGPD GNPDPLAAAH DIRETFARMA MNDEETVALI AGGHTFGKTH GAGPADNVGP
EPESAELEEQ GLGWKNSYGS GKGADTITSG LEVTWTTTPT KWSNNFFENL FKYEWELTKS
PAGANQWVAK GADETIPHAH DPSKKQRPTM LTTDLSLRFD PAYEKISRRF LENPDQLADA
FARAWFKLTH RDMGPRARYL GPEVPAEELI WQDPIPAVNH PLVDEQDIAS LKQKILASGL
SVSQLVSTAW ASASTFRGSD KRGGANGARI RLAPQKDWAV NQPEQLSKVL KTLEGIQSEF
NGAQSGGKKV SLADLIVLAG SAGIEQAAKS AGHQVTVPFA PGRMDASQDQ TDVESVGALE
PVADGFRNYV RSDIKVPPEA LLIDKAQLLT LTAPEMTVLI GGLRALNVGT GQNPQGAFTD
KPETLTNDFF RNLLDMGTEW KPTSPARHAF EGRDAKTGSV KWTGSRVDLV FGSHAQLRAL
SEVYASEDGK EKFVRDFVAA WVKVMNLDRF DLA
