ID   CAT1_PENJA              Reviewed;         696 AA.
AC   P81138;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 79.
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.
RX   PubMed=9612556;
RA   Kozlov E.A., Levitina T.L., Bobrovskaia M.T., Gudkova L.V., Latyshko N.V.,
RA   Radomskii N.F.;
RT   "Complete amino acid sequence of catalase from the fungus Penicillium
RT   vitale.";
RL   Bioorg. Khim. 24:163-170(1998).
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   AlphaFoldDB; P81138; -.
DR   SMR; P81138; -.
DR   PeroxiBase; 5322; PjaKat01.
DR   PRIDE; P81138; -.
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; IPR024712; Catalase_clade2.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
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; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Peroxidase.
FT   CHAIN           1..696
FT                   /note="Catalase"
FT                   /id="PRO_0000084925"
FT   REGION          187..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        137
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         353
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   696 AA;  77404 MW;  1A663CD3162C21BB CRC64;
     TASGKLQRKF LDRFAISMGR GVALGKTYGT LGAASRGATL LQDLLFTEII FAFDRERVPE
     RAVHARGTGA HGTFLSYEDW SNLTAASFLS AEGKFTPEMT RFSTVSGARG SADTARDVHG
     FATRFYVDEG NFDIVGNNIP VFFIWDVIIE PTLMALHAQK PNPRFHLPRG QQDPNRISDN
     LTARGDSLAQ GSQISSERGS PKAYSNTEPN KHRSFRLVTD NGKQFQCSNH WQPLQGFIDL
     GVEEAWRFPE EGEGYVAENL FESIELLTVG DEELEIQSMS FNNDLRERFN SSEVTKSSVV
     RLVPLITQGK LVFNKNIQML FNEVIGAMFQ PGHIVRGVDF TEDPLLQGRL FSYLDTQLNR
     HGPNIQQLGF NRPPRAPIHN NNRDGAGEMI DLPPFASFVE TQEWGAKDIK QTAVGQNKFD
     QEHRFSHWKF GVNGFVHTRN DDNVTHARGF FTAPERGQQK KRVAAFDRMF TVVGLSVDGQ
     QANSDQYADF DAAAGKKVAK AIGVEAPKPN SNYFHPTDVF GEHIAASGTK YGVPEGNTKG
     VLLASVNKPA SIAQGAKLQV VASSGDFAEF FISAKQLNMR EVTQGIIPLV PVLKLAKLDL
     GKTFRFQLMQ VGNIEELERF GFDLPDLTDK QVDLSAMGMF ETTFRPTSRA AQFEQGKTKL
     VKGLQGKNAF MDRALKQPSN NREKIQRFAD RFAVQD