ID A0A094HFH9_9PEZI Unreviewed; 790 AA.
AC A0A094HFH9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 37.
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=V501_04350 {ECO:0000313|EMBL:KFZ12169.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ12169.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ12169.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03108}.
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:KFZ12169.1}.
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DR EMBL; JPKD01001440; KFZ12169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094HFH9; -.
DR STRING; 1420914.A0A094HFH9; -.
DR HOGENOM; CLU_025424_2_0_1; -.
DR Proteomes; UP000029315; 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 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:UP000029315};
KW Secreted {ECO:0000256|HAMAP-Rule:MF_03108};
KW Signal {ECO:0000256|HAMAP-Rule:MF_03108, ECO:0000256|RuleBase:RU003451}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108,
FT ECO:0000256|RuleBase:RU003451"
FT CHAIN 20..790
FT /note="Catalase-peroxidase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108,
FT ECO:0000256|RuleBase:RU003451"
FT /id="PRO_5006986110"
FT DOMAIN 138..463
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108"
FT BINDING 319
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 140
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108"
FT CROSSLNK 278..304
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 143)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108"
SQ SEQUENCE 790 AA; 86470 MW; 5484C31C1A69CE05 CRC64;
MPLGQIVLLA ISALPLTSAV SCPYIGGNGA RDNAPRIPHP ESIVEPRYSP EGPGFGRCPK
KSKVAGGGTR SEDWWPCNLS LAVLRQNGES SNPWDAKFNY ATEFAKLDVS ELKKDLTELQ
TNSQSWWPAD FGNYGPFLVR LSWHNAGTYR SEDGRGGAGM GQQRFAPLNS WPDNAGLDKA
RRLLWPIKQK YGRKLSWADL MVFAGNTAME NMGFPTYGFA FGREDTWQSD EGIFWGSEQE
FFPSPNSNKD RYNGSADIHG RAKNLEEPLS AANMGLIYVD PRGPNGTPDP KASALDIRVT
FGRMGMDDEE TVALIAGGHA FGKTHGAVSG DFIGPEPNAA GIENQGLGWK NSFNTGVGNN
SYTSGLEVIW SKTPTKWANE FLGSLIYNNW TLVKSPDGAP QWEAVNANAS YPDAFIAGKL
HKPTMLTSDL ALIHDPIYNN VSKTFLNDFD YFTEKFALAW YKLLHRDMGP VTRYLGSEVP
KDEHLLWQDP LPAASYKTID DADAKRLKKD ILSAPNVNIS NLITTAWGSA STFRISDKRG
GANGARIALQ PQRSFAVNNP ERLAVVLKSL QAVKDKFNSA NKKKQVSLAD LIVLGGTAAV
EKAAADAGTA IKVPFTPGRV DTTQDLTDVE TFAYLEPRSD AFRNYGHGNS RSLTEEMMVS
RAALLTLSIP EMTVLVGGMR ALDANYDGSA FGILTDRPGQ LTNDFFTNLL DASTVWSPVA
DTNEEKFEGK DLSTGSPKYK ATRADLIFGS HAELRAVAEV YGSGDAQDKF VNDFARAWVK
VMDLDRYDVR
//
