CATA_BLUHO
ID CATA_BLUHO Reviewed; 718 AA.
AC Q8X1P0;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=CAT1;
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].
RA Zhang Z., Gurr S.J.;
RT "Isolation and characterization of a Blumeria graminis catalase gene
RT involved in antioxidant action in barley/powdery mildew interactions.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
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=1.11.1.6;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10013};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; AF327335; AAL56982.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8X1P0; -.
DR SMR; Q8X1P0; -.
DR PRIDE; Q8X1P0; -.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
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 CDD; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024712; Catalase_clade2.
DR InterPro; IPR043156; Catalase_clade2_helical.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR041399; Catalase_large_C.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR PANTHER; PTHR42821; PTHR42821; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR Pfam; PF18011; Catalase_C; 1.
DR PIRSF; PIRSF038927; Catalase_clade2; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF56634; SSF56634; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT CHAIN 1..718
FT /note="Catalase"
FT /id="PRO_0000084922"
FT ACT_SITE 103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 390
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 718 AA; 79011 MW; 31F4135D69A42544 CRC64;
MRLSLWNLLG LSGLVVASCP YMSGEDQEYH ISHIQARGTD SEFLDQFKVE DSNSYLTTDA
GGPIQDDASL KAGERGPTLL EDFIFRQKIQ HFDHERVPER AVHARGAGAY GTFTSYADWT
NITAASFLNS KGKETPVFVR FSTVAGSRGS ADTVRDVHGF ATRFYTDEGN FDIVGNNIPV
FFIQDAILFP DLVHAVKPSP DSEIPQAATG HDSAWDFFSQ QPSTLHTLFW AMSGHGIPRS
YRHMDGFGVH TMRLVTDDGK SKLVKWHWKT KQGKASLVWE EAQILAGKNP DFHRQDLWDD
INAGNGPEWE LGVQIVDEED VQAFGFDLLD PTKFLPEELV PVTILGKMKL TDNPTNYFAE
TEQVMFQPGH IVRGVDFSDD PLLQGRIYSY LDTQLNRNGG PNFEQLPVNR PRTKVHNNNR
DGAGQMFIHT NKAPYSPNSL SGGNPKQANQ TKGRGFFTAP SRKVVGSLHR GTASSFADVW
SQPRMFYNSL IPSEQQFLVN AIRFEISQLK SDLIKKNTLM QLNRVSNDLA TRVAAVIGYK
PLDPSPEFYT NATTDYVTIF GKPLPSVVGF TVGILASTSS STSISQAAQL ATSFSSRGIR
AVIVGESLLS GTDQTYSSAD ATAFDAVVVT MGAETLFGPV AKPNTLFPSG RPSQILHDAY
RWGKPVGAVS KASVVLEPLP GTKNQGGVYR VESVNELATS IAKGLETFRF VDRFPLDS