DYP_MYCEP
ID DYP_MYCEP Reviewed; 526 AA.
AC I2DBY3; P86835;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Dye-decolorizing peroxidase {ECO:0000303|PubMed:23111597};
DE Short=MepDyP {ECO:0000303|PubMed:23111597};
DE EC=1.11.1.19 {ECO:0000269|PubMed:23111597};
DE EC=1.11.1.7 {ECO:0000269|PubMed:23111597};
DE Flags: Precursor;
GN Name=dyp1 {ECO:0000312|EMBL:AFJ79725.1};
OS Mycena epipterygia (Yellow-stemmed mycena).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Mycenaceae; Mycena.
OX NCBI_TaxID=230806 {ECO:0000312|EMBL:AFJ79725.1};
RN [1] {ECO:0000312|EMBL:AFJ79725.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 64-73; 325-346 AND 384-420,
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K2 {ECO:0000303|PubMed:23111597};
RX PubMed=23111597; DOI=10.1007/s00253-012-4521-2;
RA Liers C., Pecyna M.J., Kellner H., Worrich A., Zorn H., Steffen K.T.,
RA Hofrichter M., Ullrich R.;
RT "Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and
RT litter-degrading agaricomycetes compared to other fungal and plant heme-
RT peroxidases.";
RL Appl. Microbiol. Biotechnol. 97:5839-5849(2013).
CC -!- FUNCTION: Manganese-independent peroxidase that is able to convert a
CC large number of compounds, but its physiological substrate is not
CC known. In addition to classic peroxidase substrates (e.g. 2,6-
CC dimethoxyphenol), oxidizes dyes such as Reactive Blue 5 and Reactive
CC Black 5. {ECO:0000269|PubMed:23111597}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O2 + Reactive Blue 5 = 2,2'-disulfonyl azobenzene + 3-[(4-
CC amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H(+) + 2
CC H2O + phthalate; Xref=Rhea:RHEA:28086, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:17563,
CC ChEBI:CHEBI:63950, ChEBI:CHEBI:63955, ChEBI:CHEBI:64278;
CC EC=1.11.1.19; Evidence={ECO:0000269|PubMed:23111597};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC Evidence={ECO:0000269|PubMed:23111597};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:I2DBY1};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently.
CC {ECO:0000250|UniProtKB:I2DBY1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=405 nm {ECO:0000269|PubMed:23111597};
CC Kinetic parameters:
CC KM=11 uM for H(2)O(2) {ECO:0000269|PubMed:23111597};
CC pH dependence:
CC Optimum pH is 4 with 2,6-dimethoxyphenol as substrate. Retains 90% of
CC its activity after 4 hours at pH 2.5. {ECO:0000269|PubMed:23111597};
CC Temperature dependence:
CC Thermostable. Retains 50%-90% of its activity after heating for 2
CC hours at 60 degrees Celsius, while no decrease in activity is
CC observed within the same time at 30 or 40 degrees Celsius.
CC {ECO:0000269|PubMed:23111597};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23111597}.
CC -!- SIMILARITY: Belongs to the DyP-type peroxidase family. {ECO:0000305}.
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DR EMBL; JQ650252; AFJ79725.1; -; mRNA.
DR AlphaFoldDB; I2DBY3; -.
DR SMR; I2DBY3; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR006314; Dyp_peroxidase.
DR Pfam; PF04261; Dyp_perox; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
DR TIGRFAMs; TIGR01413; Dyp_perox_fam; 1.
DR PROSITE; PS51404; DYP_PEROXIDASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Heme; Iron; Metal-binding;
KW Oxidoreductase; Peroxidase; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..63
FT /evidence="ECO:0000305|PubMed:23111597"
FT /id="PRO_0000444022"
FT CHAIN 64..526
FT /note="Dye-decolorizing peroxidase"
FT /evidence="ECO:0000305"
FT /id="PRO_5003656618"
FT ACT_SITE 231
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:I2DBY1"
FT BINDING 376
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:0000250|UniProtKB:I2DBY1"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 526 AA; 56644 MW; FEBB09E205BAA937 CRC64;
MRKSISTFIL LSVLSVGQLV AARPRSTNAP PRRRTPQPRR TTSLFINPPA LPDLPTVQAV
DKLDDALDID NIQSDILVGM KKTKELFFFF GVEDAATFKS KLASDILPLI TTTTEILSTD
TQPITAVNIA FSHTGLVALG VNDDIGDTDF VSGQFSEATT VGDRPTLWDP AFAGTKIHGV
FLLASNTTED INTELANIQS ILGSSITEIH RLQGAARPGA EEGHEHFGFL DGISQPAVNG
FTDTVLPGQT PVDPGLFLLG ESGDPSQDSR PSWAVDGSFL VFRQLQQFVP EFNQFLADHP
LDIPGRTAEE GSELLGARMV GRWKSGAPVF LSPTQDDPVL GADKNRNNDF NYLVASDPDP
GTENHFNQTA CPFGAHIRKV HPRGDLSPSA ENPHFIIRSS IPYGPEVTDA EAASSTTSVD
RGLAFVSYQS NIFNGFVFLQ SIWINNVNFI FGKVDPTIGV DPIIGTLGGG PHNISGLNPL
IPVNETVDFQ DDPWNDVVIP RDFVVSHGGE YFFSPSLSGI SAIAAA
