ID A0A0P7BMX6_9HYPO Unreviewed; 776 AA.
AC A0A0P7BMX6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 13-SEP-2023, entry version 25.
DE RecName: Full=Catalase-peroxidase {ECO:0000256|HAMAP-Rule:MF_03108, ECO:0000256|RuleBase:RU003451};
DE Short=CP {ECO:0000256|HAMAP-Rule:MF_03108};
DE EC=1.11.1.21 {ECO:0000256|HAMAP-Rule:MF_03108, ECO:0000256|RuleBase:RU003451};
DE AltName: Full=Peroxidase/catalase {ECO:0000256|HAMAP-Rule:MF_03108};
DE Flags: Precursor;
GN Name=katG {ECO:0000256|HAMAP-Rule:MF_03108};
GN ORFNames=AK830_g4848 {ECO:0000313|EMBL:KPM41693.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM41693.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM41693.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM41693.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. Confers resistance to H(2)O(2) in hyphae. May play
CC an antioxidative role in fungal defense against the host-produced
CC H(2)O(2) (oxidative burst) at the early stage of plant infection.
CC {ECO:0000256|HAMAP-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:0000256|ARBA:ARBA00001378, ECO:0000256|HAMAP-
CC Rule:MF_03108, ECO:0000256|RuleBase:RU003451};
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:0000256|HAMAP-
CC Rule:MF_03108, ECO:0000256|RuleBase:RU003451};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03108};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.
CC {ECO:0000256|HAMAP-Rule:MF_03108};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|HAMAP-
CC Rule:MF_03108}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|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:0000256|HAMAP-Rule:MF_03108}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03108,
CC ECO:0000256|RuleBase:RU003451}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPM41693.1}.
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DR EMBL; LKCW01000060; KPM41693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7BMX6; -.
DR STRING; 78410.A0A0P7BMX6; -.
DR OrthoDB; 317402at2759; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; 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 CDD; cd08200; catalase_peroxidase_2; 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 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 Disulfide bond {ECO:0000256|HAMAP-Rule:MF_03108};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_03108};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324, ECO:0000256|HAMAP-
KW Rule:MF_03108};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_03108};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03108};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_03108};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP-
KW Rule:MF_03108}; Reference proteome {ECO:0000313|Proteomes:UP000050424};
KW Secreted {ECO:0000256|HAMAP-Rule:MF_03108};
KW Signal {ECO:0000256|HAMAP-Rule:MF_03108, ECO:0000256|RuleBase:RU003451}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108,
FT ECO:0000256|RuleBase:RU003451"
FT CHAIN 22..776
FT /note="Catalase-peroxidase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108,
FT ECO:0000256|RuleBase:RU003451"
FT /id="PRO_5006987380"
FT DOMAIN 163..447
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 130
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108"
FT BINDING 303
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:0000256|HAMAP-Rule:MF_03108"
FT SITE 126
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108"
FT CROSSLNK 129..262
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with Met-
FT 288)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108"
FT CROSSLNK 262..288
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 129)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108"
SQ SEQUENCE 776 AA; 84941 MW; 48F67A473B4AE494 CRC64;
MHADLPGWLL LALGLVSLVD ANSCPFSKRA IDIDREIPED FGRCSAISNA AGGGTRSRDW
WPCQLKLDVL RQFAPQINPL GGDFDYTAAF ESLDYEALKK DLHELMTTSQ DWWPADFGHY
GGFFIRMAWH SAGTYRAIDG RGGGGMGQQR FAPLNSWPDN QNLDKARRLL WPIKQKYGNK
ISWADLILLT GNVALESMDF TPIGFAAGRP DTWQSDESVY WGGEATFVPK GNDVRYNGST
DIYGRAEHLE KPLGATHMGL IYVNPEGPDG SSDPKASAGD IRVAFDRMGM NDEETVALIA
GGHAFGKTHG AVASSNIGPE PEAADLGSMG LGWHNSVGDG NGPNTQTSGL EVIWSKTPTK
WSNDFLNSLV KNNWTLVESP AGAHQWEALN GTVDYPDPFD KTKFRRATML TSDLALINDP
SYKKICNRWV EHPEELVDAF AKAWFKLLHR DLGPVSRYLG PEKPTEHFAW QDPLPARTGA
VLSDADISTL KSELLAASGL DVSKLVSTAW NAASTYRHSD KRGGANGARI ALDPQRSWKA
NNPAQLEKVL TALKGIQKKF NKGTKKVSVA DLIVLGGSAA VEKAAHDAGF KSITVPFTPG
RVDATQNQTD IESFGYLEPV ADGFRNYGKG TSRARTEEIL VDKAALLTLT PPELTVLVGG
LRVLGANYDG SSLGVLTENK GKLTNDFFVN LLDSSFTWTK KDAQGELWTG VDRATKATKW
TATRADLVFG SHAELRAISE VYGSQDAKEK FVKDFVTTWV KVMNLDRFDI EAEKKY
//
