KATG_BLUHO
ID KATG_BLUHO Reviewed; 730 AA.
AC Q8X1N3;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_03108};
DE Short=CP {ECO:0000255|HAMAP-Rule:MF_03108};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_03108};
DE AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_03108};
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_03108}; Synonyms=CPX;
OS Blumeria hordei (Barley powdery mildew) (Blumeria graminis f. sp. hordei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria.
OX NCBI_TaxID=2867405;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IM82;
RX PubMed=20565628; DOI=10.1111/j.1364-3703.2004.00251.x;
RA Zhang Z., Henderson C., Gurr S.J.;
RT "Blumeria graminis secretes an extracellular catalase during infection of
RT barley: potential role in suppression of host defence.";
RL Mol. Plant Pathol. 5:537-547(2004).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_03108}.
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_03108};
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_03108};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03108};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.
CC {ECO:0000255|HAMAP-Rule:MF_03108};
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_03108}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03108}.
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_03108}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03108}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL56991.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF329396; AAL56991.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q8X1N3; -.
DR SMR; Q8X1N3; -.
DR PeroxiBase; 1960; BgCP.
DR EnsemblFungi; BLGH_02667-mRNA-1; BLGH_02667-mRNA-1; BLGH_02667.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase.
FT CHAIN 1..730
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354104"
FT ACT_SITE 93
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT BINDING 266
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_03108"
FT SITE 89
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT CROSSLNK 92..225
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 251)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT CROSSLNK 225..251
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 92)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
SQ SEQUENCE 730 AA; 81024 MW; 7C547BA50B90F4F7 CRC64;
MGDSKCPYRD ANVAGGGTHN KDWWPETLKL DALRQHTAES NPLGKDFDYA SAFKTLDYEG
LKKDLKDLMT DSQDWWPADF GHYGGFFVRM AWHSAGTYRS IDGRGGGGQG QHRFAPLNSW
PDNGNLDKAR RLLWPIKQKY GNKISWADLY LLTGNVAIES MGGKTFGFAC GRPDTWEADD
ATFWGNETKW LGNDARYKNG SKDPKDIYTR QLEKPLSAVH MGLIYVNPEG PDGIPDPVAS
ARDIRTTFRR MAMNDEETVA LIAGGHTFGK THGAAPATHL GKEPEGAPIE AQGLGWANSY
RSGKGPDTIT SGLEVIWTKT PINWSNHYLE YLFKYDWELT KSPGGANQWT AKNAEAFIPD
AFDPNKKHPP RMLTTDLALR HDKEYEKISL RFLENPDQFA DAFARAWFKL LHRDMGPRSR
WLGPEIPKEE LIWEDPIPEI DHPIISQEDI NNLKKEILSS GVGHNKLIQT AWASASTFRG
GDKRGGANGA RIRLAPQKDW KVNNPPQLTC VLETLGKIQS SFNSSQTGGK IVSLADLIIL
AGCAALEKAA GVPVPFSPGR ADASQEQTDI KSFSNLEPVA DGFRNFGRST PRARAEHMLV
DRAQLLTLTP PELTALVGGL RVLDTNFDGS SCGVFTKRPG QLTNDFFVNL LDPAISWKGI
DEDEFFEGID RKTDEKKWIG SRADLVFGSQ AELRAIAEVY GSADGNEKLI KDFIAAWNKV
MNLDLFNLAH
