ID   KATG_ASPTN              Reviewed;         737 AA.
AC   Q0CD12;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   02-SEP-2026, entry version 95.
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}; ORFNames=ATEG_08422;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC       peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_03108}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O2 + AH2 = 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 = O2 + 2 H2O; 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; Evidence={ECO:0000255|HAMAP-
CC         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}.
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DR   EMBL; CH476605; EAU31595.1; -; Genomic_DNA.
DR   RefSeq; XP_001217043.1; XM_001217043.1.
DR   AlphaFoldDB; Q0CD12; -.
DR   SMR; Q0CD12; -.
DR   STRING; 341663.Q0CD12; -.
DR   PeroxiBase; 3413; AteCP01.
DR   EnsemblFungi; EAU31595; EAU31595; ATEG_08422.
DR   GeneID; 4353293; -.
DR   VEuPathDB; FungiDB:ATEG_08422; -.
DR   eggNOG; ENOG502QTDY; Eukaryota.
DR   HOGENOM; CLU_025424_2_0_1; -.
DR   OMA; GPETTWL; -.
DR   OrthoDB; 407695at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:TreeGrafter.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:TreeGrafter.
DR   CDD; cd00649; catalase_peroxidase_1; 1.
DR   CDD; cd08200; catalase_peroxidase_2; 1.
DR   FunFam; 1.10.420.10:FF:000002; Catalase-peroxidase; 1.
DR   FunFam; 1.10.420.10:FF:000004; Catalase-peroxidase; 1.
DR   FunFam; 1.10.520.10:FF:000002; Catalase-peroxidase; 1.
DR   Gene3D; 1.10.520.10; -; 2.
DR   Gene3D; 1.10.420.10; Peroxidase, domain 2; 2.
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   NCBIfam; TIGR00198; cat_per_HPI; 1.
DR   NCBIfam; NF011635; PRK15061.1; 1.
DR   PANTHER; PTHR30555:SF0; CATALASE-PEROXIDASE; 1.
DR   PANTHER; PTHR30555; HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE; 1.
DR   Pfam; PF00141; peroxidase; 2.
DR   PRINTS; PR00460; BPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 2.
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; Reference proteome.
FT   CHAIN           1..737
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_0000354103"
FT   ACT_SITE        90
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT   BINDING         260
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            86
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT   CROSSLNK        89..219
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   245)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT   CROSSLNK        219..245
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   89)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
SQ   SEQUENCE   737 AA;  81333 MW;  59F5B80D7B3F9425 CRC64;
     MGESKCPVNF AGGGTRNKDW WPDQLRLNIL RQHTSASNPL DADFDYAAAF NSLDYNALKK
     DLEALMTDSQ DWWPADFGHY GGLFIRMAWH SAGTYRVFDG RGGAGQGQQR FAPLNSWPDN
     ASLDKARRLL WPIKQKYGNK ISWADLMILA GNVALESMGF KPFGFSGGRA DTWEADESVY
     WGGEKTWFPK GNDVRYPNDD IYTRDLENPL AASHMGLIYV NPEGPNGNPD PKAAARDIRV
     TFGRMAMNDE ETVALIAGGH SFGKTHGASS GDHCGPEPEA AGLEAQGLGW QSKYGSGSGR
     DAITSGLEVT WTKTPTRWST NFLEYLFAFD WELTKSPAGA NQWVAKNADA IIPDAFDPSK
     KHKPQMLTTD LALRYDPAYE KIARRFLENP DQFADAFARA WFKLTHRDMG PRARYVGPEV
     PSEVLIWQDP IPAVNHPLVD ASDIASLKQA ILNSGVDRSK FVSTAWAAAS TFRGGDKRGG
     ANGARIRLAP QRDWEVNNQP WLKESLAALE KIQSSFNGSR SDRKKISLAD LIVLAGCAAV
     ESAAQEAGHA VSVPFTPGRM DASQEETDVE SFSHMEPVAD GFRNYSTAPT RRRAEHYLVD
     KAQMLTLSAP EMTALVGGLR ALNANYDGSA HGVFTSRPGY LTNDFFVNLL DMGTTWKPTD
     ASGELYEGAD RRTGSKKWTA TRVDLVFGSH AELRAIAEVY GSSDGERKFV KDFVAAWNKV
     MNLDRFDLKR ENVPARL
//