ID   CATA_PENJA              Reviewed;         670 AA.
AC   P11934;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
OS   Penicillium janthinellum (Penicillium vitale).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5079;
RN   [1]
RP   PROTEIN SEQUENCE, AND X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).
RX   PubMed=3712443; DOI=10.1016/0022-2836(86)90479-1;
RA   Vainshtein B.K., Melik-Adamyan W.R., Barynin V.V., Vagin A.A.,
RA   Grebenko A.I., Borisov V.V., Bartels K.S., Fita I., Rossmann M.G.;
RT   "Three-dimensional structure of catalase from Penicillium vitale at 2.0-A
RT   resolution.";
RL   J. Mol. Biol. 188:49-61(1986).
RN   [2]
RP   SIMILARITY TO BOVINE CATALASE.
RX   PubMed=3712444; DOI=10.1016/0022-2836(86)90480-8;
RA   Melik-Adamyan W.R., Barynin V.V., Vagin A.A., Borisov V.V.,
RA   Vainshtein B.K., Fita I., Murthy M.R.N., Rossmann M.G.;
RT   "Comparison of beef liver and Penicillium vitale catalases.";
RL   J. Mol. Biol. 188:63-72(1986).
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   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC   -!- CAUTION: This is an X-ray determined sequence, alanine is indicated in
CC       position where no side chain could be observed. {ECO:0000305}.
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DR   PIR; A25001; A25001.
DR   PDB; 4CAT; X-ray; 3.00 A; A/B=-.
DR   PDBsum; 4CAT; -.
DR   AlphaFoldDB; P11934; -.
DR   SMR; P11934; -.
DR   EvolutionaryTrace; P11934; -.
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   Gene3D; 1.20.1370.20; -; 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; IPR020835; Catalase_sf.
DR   PANTHER; PTHR42821; PTHR42821; 1.
DR   Pfam; PF00199; Catalase; 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   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW   Metal-binding; Oxidoreductase; Peroxidase; Peroxisome.
FT   CHAIN           1..670
FT                   /note="Catalase"
FT                   /id="PRO_0000084924"
FT   ACT_SITE        61
FT   ACT_SITE        132
FT   BINDING         345
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:0000269|PubMed:3712443"
SQ   SEQUENCE   670 AA;  70260 MW;  5EA0E355EC01BED6 CRC64;
     AAAQRRQNDS SVFLAIMVAA AVESESSLTD GDAGALLLQD ISEWDEVFRF DRLEAVERAA
     HAAAAAAFGA FVARGDWTAS AAAAFQAAGK QIAFMAAFST VAGAKGSATV RDADAFAAKF
     ASAAALQELV GNNSPISFFI FDLLFAAILF ASKAKAANQA AFAAAAELAA ESLFVRLPSL
     HQVSFFALAG FAAVAAHRHM NGYGSHTFKL VAKDGSVYCS KFWYKADQGQ AAEVWKDAEE
     VAAEDVDYFR DLNFQAEAAG RYPLWELASQ VMTFSDFEID PFNENIPTKV VPRESVPLIV
     DAELLLNRNP LNMFAEVEQV FMDVAAASKG ADEVEDPLIQ RQFAYIDTHL SELTASYGIP
     VCRPYATVLN DQEDGARYDD VQDVLVIAPN AFSASAVEVQ IPAAAAFNLA AARVAAAGDV
     RVNAVVEADQ RKQSRQFWAS DVNAQKKRLV DAFRMEVASA VSASIQVDVT VEFSFVAAAA
     AARIAAAVGS AAAGALANRR QIKVIASLAV LAKADAKVRQ KNALESSSQA VAVDAKAAAQ
     DIVDSSDAAN VVTVAREFAV LPQTAAADAA EFVAAASAKA FSSFPAMEVI SVAAAAGAVA
     EPARASLDLN MAMFFSRIVA SRGAAANAIA ALVKASRDGV FVAAVLAKAA ANNRAAEAIF
     KFEVRQAVDA