ID A0A4U0VB86_9PEZI Unreviewed; 761 AA.
AC A0A4U0VB86;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 13-SEP-2023, entry version 12.
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};
GN Name=katG {ECO:0000256|HAMAP-Rule:MF_03108};
GN ORFNames=B0A54_03658 {ECO:0000313|EMBL:TKA45973.1};
OS Friedmanniomyces endolithicus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Friedmanniomyces.
OX NCBI_TaxID=329885 {ECO:0000313|EMBL:TKA45973.1, ECO:0000313|Proteomes:UP000310066};
RN [1] {ECO:0000313|EMBL:TKA45973.1, ECO:0000313|Proteomes:UP000310066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5311 {ECO:0000313|EMBL:TKA45973.1,
RC ECO:0000313|Proteomes:UP000310066};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:TKA45973.1}.
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DR EMBL; NAJP01000010; TKA45973.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U0VB86; -.
DR STRING; 329885.A0A4U0VB86; -.
DR Proteomes; UP000310066; Unassembled WGS sequence.
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; cd00649; catalase_peroxidase_1; 1.
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; 2.
PE 3: Inferred from homology;
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:UP000310066}.
FT DOMAIN 143..447
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT DOMAIN 478..761
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 205..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108"
FT BINDING 283
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 88
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108"
FT CROSSLNK 242..268
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 91)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108"
SQ SEQUENCE 761 AA; 84825 MW; 47696AF296520E40 CRC64;
MTEQCPVRFA NTGGGGTRNF DWWPNQLRVN ILRQHTQVTN PMGKDFDYAE AFKTIDYEGL
KKDLHSLMTD SQSWWPADFG HYGGLFIRMA WHSSGTYRVY DGRGGGGGGQ QRFAPLNSWP
DNVSLDKSRR LLWPIKQKYG SKLSWADLML LAGNVAMESM GAKPFGFSGG RPDQWEADES
VYWGAEMTWL GNEERYGEGN EGVSADKHGV VDGEQGPKKE HKDIHSRDLE KPLAAAHMGL
IYVNPEGPDG VPDPVASARD IRTTFGRMAM NDYETVALIV GGHTFGKTHG AAPADNLGME
PQAAGIENQG LGWMNKHGQG NGPDAITSGL EVTWTSTPTQ WSNHYLEYLF KFEWELVKSP
AGAHQWEAKD AEETIPNAFD SKKKQKPRML TSDLALRYDE AYEKVSRHFL ENPEELKDAF
VRAWFKLLHR DMGPRTRWVG PEIPTEVMLW EDPVPTLDHA VVDEKEIDAL KKQIMEAGVE
PTKLISTAWG AASCFRGSDK RGGANGARIR LEPQNKWEVN NPSQVKEVLS ALEGVQKKFN
ESASGGKKIS LADLIVLAGC AALEKAAGVR VPFTPGRTDA TQEQTDAQSF EHLEPHADGF
RNYGKSTERV RTEQFLIDRA HLLNLSAPEM TVLVGGLRTL NTNWDGSSHG VLTKRPGQLT
NDFFVNLLDN DTEWKAADQG LPEVFNGTAR KGGEKKWTAT RVDLIFGSHP ELRATAEVYA
MADSKDKFVK DFVAAWDKVM NLDRFDLNKH GQSYNKLESR L
//
