ID   CATA_BOTFU              Reviewed;         479 AA.
AC   P55304;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Catalase A;
DE            EC=1.11.1.6;
GN   Name=catA;
OS   Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=40559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=SAS56;
RX   AGRICOLA=IND20605717; DOI=10.1006/pmpp.1996.0067;
RA   Van der Vlugt-Bergmans C.J.B., Wagemakers C.A.M., Dees D.C.T.,
RA   van Kan J.A.L.;
RT   "Catalase A from Botrytis cinerea is not expressed during infection on
RT   tomato leaves.";
RL   Physiol. Mol. Plant Pathol. 50:1-15(1997).
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   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; Z54346; CAA91159.1; -; mRNA.
DR   AlphaFoldDB; P55304; -.
DR   SMR; P55304; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; PTHR11465; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   PIRSF; PIRSF038928; Catalase_clade1-3; 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   2: Evidence at transcript level;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW   Peroxisome.
FT   CHAIN           1..479
FT                   /note="Catalase A"
FT                   /id="PRO_0000084917"
FT   ACT_SITE        63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         346
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   479 AA;  53686 MW;  B8CD0D8391A244CC CRC64;
     MAQTNGVLQE PAITTMNGAP VLKPASTQRI GNQLRATLLL QDINLLELIQ HITHERIPER
     VVHARGTSAH GYFEVTDDIS DVTSAAFLNR VGKQTDIFCR FSTVAGRAES AETVRDTRGF
     AFKMFTEEGN LDWLFLSTPV FPIRDGAKFP SFTHATKKNP RSGLPDHKAF WDYFTHNQEG
     IHFLMFLFSD RATPVDFQHA DIFSINTYKF TKSDGSFTYV KIHLKTNQGV KNFTQDEANQ
     KAGVDPDFQT RSLYEDIENQ KYPTWDVFAQ IIDPVKAENY HINIFDATKT FPFSEFPLRK
     FGKITLNRNV DNFFAEQEQS AFSPTNLVPG WALTPDPIIQ TRALAYADTQ RYRLGANFVQ
     LPVNAPYKKP FTPLIRDGAA TVNGNLGGTP NYFPSSFYNV GAATQYAQPD EEQFQGTVVN
     FESEVVDADY VQPRIFWEKT LAEEPGQQDN LISNVAGHLS AVTGDKGLGS STSGLCNVR