KATG_TALMA
ID KATG_TALMA Reviewed; 748 AA.
AC Q8NJN2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 84.
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}; Synonyms=cpeA;
OS Talaromyces marneffei (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=37727;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=16178368; DOI=10.1080/13693780400007144;
RA Pongpom P., Cooper C.R. Jr., Vanittanakom N.;
RT "Isolation and characterization of a catalase-peroxidase gene from the
RT pathogenic fungus, Penicillium marneffei.";
RL Med. Mycol. 43:403-411(2005).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity (By similarity). May be involved in protection from
CC the host during host infection. {ECO:0000255|HAMAP-Rule:MF_03108}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + H2O2 = 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 = 2 H2O + O2; 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;
CC Evidence={ECO:0000255|HAMAP-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 -!- INDUCTION: Induced by temperature shift to 37 degrees Celsius, the
CC condition whereby the pathogenic yeast phase is formed.
CC {ECO:0000269|PubMed:16178368}.
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; AF537129; AAN04057.1; -; mRNA.
DR AlphaFoldDB; Q8NJN2; -.
DR SMR; Q8NJN2; -.
DR PeroxiBase; 2182; PmCP01.
DR PRIDE; Q8NJN2; -.
DR VEuPathDB; FungiDB:PMAA_101750; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
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 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 PANTHER; PTHR30555; PTHR30555; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00460; BPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 2.
DR TIGRFAMs; TIGR00198; cat_per_HPI; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase.
FT CHAIN 1..748
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354108"
FT ACT_SITE 97
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT BINDING 270
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 93
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT CROSSLNK 96..229
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 255)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT CROSSLNK 229..255
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 96)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
SQ SEQUENCE 748 AA; 82374 MW; 81E0D77ECBC676E0 CRC64;
MAESKCPAHQ HVLKANVGGA GTSNQDWWPD RLKLNILRQN NPVSNPLGEE FDYAAAFNSL
DYFALKKDIQ DLMTDSQDWW PADFGHYGGL FIRMAWHSAG TYRVADGRGG GGGGQQRFAP
LNSWPDNVGL DKARRLLWPI KQKYGNKISW ADLLLLTGNV ALESMGFKTF GFSGGRADTW
EVDESANWGG ETTWLGNDVR YSGGKADHKD IHNRDLDKPL AAAHMGLIYV NPEGPDGNPD
PIAAAKDIRT TFGRMAMNDE ETVALIAGGH TFGKTHGAGP ADKLGPEPEA ADMAQQGLGW
TNSFKSGKGP DTTTSGLEVT WTKTPTKWSN QFLEYLFRYD WELTKSPAGA HQWVAKNAEA
FIPDAFDPSK KRKPMMLTTD LSLRYDPIYE KISRRFLEHP DQFADAFARA WFKLLHRDLG
PRALYIGPEV PAEVLPWQDP VPAVDHPLIS NEDASALKQR ILASGVKPSS LISTAWASAS
TFRGSDKRGG ANGARIRLSP QREWAVNNQP WLRETLSVLE AIQKQFNTSQ SGGKKVSIAD
LIVLAGVAAV EKAARDAGYA VTVPFTPGRT DASQEQTDVQ SFSDMEPIAD GFRNYGSSTS
RVRAEEWLID KAQLLTLSAP ELAVLIGGLR VLNTNYDGSA HGVFTQRPGK LTNDFFVNLL
DMNTAWKSIG GVDLYEGTDR KTGAKKWTAT RNDLVFGSNA ELRAIAEVYG SSDGQEKFVK
DFVAAWDKVM NLDRFDLKKK QSTSSHRL
