DYP_EXIGL
ID DYP_EXIGL Reviewed; 501 AA.
AC I2DBY2; P86836;
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=EglDyP {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:AFJ79724.1};
OS Exidia glandulosa (Black witch's butter).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=5219 {ECO:0000312|EMBL:AFJ79724.1};
RN [1] {ECO:0000312|EMBL:AFJ79724.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 61-71; 252-279; 321-342;
RP 376-385 AND 442-482, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=DSMZ 1012 {ECO:0000312|EMBL:AFJ79724.1};
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=14 uM for H(2)O(2) {ECO:0000269|PubMed:23111597};
CC pH dependence:
CC Optimum pH is 4.5 with 2,6-dimethoxyphenol as substrate. Retains more
CC than 50% of its activity after 4 hours at pH 2.5.
CC {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; JQ650251; AFJ79724.1; -; mRNA.
DR AlphaFoldDB; I2DBY2; -.
DR SMR; I2DBY2; -.
DR BRENDA; 1.11.1.19; 15117.
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..60
FT /evidence="ECO:0000305|PubMed:23111597"
FT /id="PRO_0000444025"
FT CHAIN 61..501
FT /note="Dye-decolorizing peroxidase"
FT /evidence="ECO:0000305|PubMed:23111597"
FT /id="PRO_5003657273"
FT ACT_SITE 228
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:I2DBY1"
FT BINDING 367
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 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 501 AA; 52641 MW; 13023F5418B5DC95 CRC64;
MRLSPSFLSL ALVIFVGEVV ARNVVARASN PASVTGTRKV SLLKNVAGLP AVPTAQQVAV
SSLNTDDIQG DILVGMHKQQ QRFYFFTIND AATFKTHLAA DIAPVVASVT QLSSVSTQPL
VALNIAFSQT GLNALGVTDN VGDALFTAGQ ASNTVGNLKE TTDNWVAQFK TPGIHGVILL
ASDDKSLIDQ QEASIQSTFG AAISKVYSLD GAIRPGAEAG HEMFGFLDGI AQPAISGLGT
PLPGQLVVDE GVIIVGGTND PIARPADGWM TGGSFLAFRQ LEQLVPEFNK YLLDNAPAVD
GKSLQDRADL LGARMVGRWK SGAPIDLTPL ADDPALGADP QRNNNFDFTH ANFSITTDQT
HCPFSAHIRK TRPRADLVAP ANSIIRSGIP YGSEVSAAEA AANATTNERG LAFVSYQSQL
NKGFQFLQNT WANNPGFIFG KNVQPGQDPI IGQNSGAIRS VVGLDPANPT GALSMGQFVV
SRGGEYFFSP PISALTGKLA A
