KATG_CHAGB
ID KATG_CHAGB Reviewed; 749 AA.
AC Q2H7U1;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=CHGG_05274;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {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 -!- 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; CH408031; EAQ88655.1; -; Genomic_DNA.
DR RefSeq; XP_001221369.1; XM_001221368.1.
DR AlphaFoldDB; Q2H7U1; -.
DR SMR; Q2H7U1; -.
DR STRING; 38033.XP_001221369.1; -.
DR PeroxiBase; 3408; CgCP01.
DR PRIDE; Q2H7U1; -.
DR EnsemblFungi; EAQ88655; EAQ88655; CHGG_05274.
DR GeneID; 4391274; -.
DR eggNOG; ENOG502QTDY; Eukaryota.
DR HOGENOM; CLU_025424_2_0_1; -.
DR InParanoid; Q2H7U1; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 352289at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase; Reference proteome.
FT CHAIN 1..749
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354105"
FT ACT_SITE 91
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT BINDING 279
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 87
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT CROSSLNK 90..238
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 264)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT CROSSLNK 238..264
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 90)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
SQ SEQUENCE 749 AA; 82096 MW; ED0BA56EA1FB6617 CRC64;
MGECPVNHAN VAGGGTRNND WWPNQLRLNI LRQHQPASSP YSKEFDYAAA FKSLDYEALK
KDITAVMTDS QDWWPADFGH YGGLFIRMAW HSAGTYRVFD GRGGGSQGQQ RFAPLNSWPD
NVSLDKARRL LWPVKQKYGD KISWADLLLL TGNVALESMG FKTFGFAGGR PDTWEADESA
YWGGEKTWLG NDVRYGQGNE GVAGQGVVDG DESKKGHRDI HSRDLESPLA AAHMGLIYVN
PEGPDGIPDP VAAGRDIRTT FGRMAMNDEE TVALIAGGHT FGKTHGAAPA VNVSKEPEAA
PLEQQGLGWS NKHGTGKGPD TITSGLEVIW TKEPTKWTHN FFEYLFKFEW ELTKSPAGAN
QWVAKNTEPI IPDAFDPNKK HLPRMLTTDL ALRFDPEYEK ISRRFLENPD QFADAFARAW
FKLLHRDLGP RSRWLGPEIP SEVLIWEDPV PAVNHPLVDE QDVTTLKRAI LATGVAPAKL
ISTAWASAST FRGGDKRGGA NGARIRLAPQ KDWKVNNPPQ LAEVLKALEG VQAQFNGASQ
SKKVSLADLI VLGGVAALEQ AAGVSVPFTP GRTDASQEQT EVESFAHLEP HVDGFRSYGR
GTSRVSTEQF LVDRAHLLTL TPPELAVLVG GLRVLGANYD GSSNGVFTTR PGKLTNDYFV
NLLDMATAWK SVDGEVFEGN DRKTGEKKWT GTRADLVFGA HAELRAISEV YGSSSGQDKF
VKDFVAAWSK VMNLDRYDLA QPGSSGPKL
