VPL2_PLEER
ID VPL2_PLEER Reviewed; 361 AA.
AC O94753;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Versatile peroxidase VPL2;
DE EC=1.11.1.16 {ECO:0000269|PubMed:12884090, ECO:0000269|PubMed:16246366, ECO:0000269|PubMed:9987124};
DE AltName: Full=Versatile liquid phase peroxidase 2;
DE Flags: Precursor;
GN Name=vpl2;
OS Pleurotus eryngii (Boletus of the steppes).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=5323;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 31-47,
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 90787 / CBS 613.91 / IJFM A169 / KCTC 26061;
RX PubMed=9987124; DOI=10.1046/j.1365-2958.1999.01164.x;
RA Ruiz-Duenas F.J., Martinez M.J., Martinez A.T.;
RT "Molecular characterization of a novel peroxidase isolated from the
RT ligninolytic fungus Pleurotus eryngii.";
RL Mol. Microbiol. 31:223-235(1999).
RN [2]
RP STRUCTURE BY NMR, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP COFACTOR, AND MUTAGENESIS OF ASP-205.
RC STRAIN=ATCC 90787 / CBS 613.91 / IJFM A169 / KCTC 26061;
RX PubMed=12884090; DOI=10.1007/s00775-003-0476-1;
RA Banci L., Camarero S., Martinez A.T., Martinez M.J., Perez-Boada M.,
RA Pierattelli R., Ruiz-Duenas F.J.;
RT "NMR study of manganese(II) binding by a new versatile peroxidase from the
RT white-rot fungus Pleurotus eryngii.";
RL J. Biol. Inorg. Chem. 8:751-760(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 31-361 OF WILD-TYPE AND MUTANT
RP SER-194 IN COMPLEX WITH HEME; MANGANESE AND CALCIUM IONS, DISULFIDE BONDS,
RP RADICAL INTERMEDIATE, CATALYTIC ACTIVITY, CATALYTIC MECHANISM, AND
RP MUTAGENESIS OF PRO-106; TRP-194 AND HIS-262.
RC STRAIN=ATCC 90787 / CBS 613.91 / IJFM A169 / KCTC 26061;
RX PubMed=16246366; DOI=10.1016/j.jmb.2005.09.047;
RA Perez-Boada M., Ruiz-Duenas F.J., Pogni R., Basosi R., Choinowski T.,
RA Martinez M.J., Piontek K., Martinez A.T.;
RT "Versatile peroxidase oxidation of high redox potential aromatic compounds:
RT site-directed mutagenesis, spectroscopic and crystallographic investigation
RT of three long-range electron transfer pathways.";
RL J. Mol. Biol. 354:385-402(2005).
CC -!- FUNCTION: A versatile ligninolytic peroxidase that combines the
CC substrate specificity characteristics of the two other ligninolytic
CC peroxidases, manganese peroxidase and lignin peroxidase.
CC {ECO:0000269|PubMed:9987124}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-
CC diol + H2O2 = glycolaldehyde + guaiacol + H2O + vanillin;
CC Xref=Rhea:RHEA:22396, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17071, ChEBI:CHEBI:18346, ChEBI:CHEBI:28591,
CC ChEBI:CHEBI:53650; EC=1.11.1.16;
CC Evidence={ECO:0000269|PubMed:12884090, ECO:0000269|PubMed:16246366,
CC ECO:0000269|PubMed:9987124};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + H2O2 + 2 Mn(2+) = 2 H2O + 2 Mn(3+);
CC Xref=Rhea:RHEA:22776, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:29035, ChEBI:CHEBI:29041;
CC EC=1.11.1.16; Evidence={ECO:0000269|PubMed:12884090,
CC ECO:0000269|PubMed:16246366, ECO:0000269|PubMed:9987124};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297,
CC ECO:0000269|PubMed:12884090};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:12884090};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297,
CC ECO:0000269|PubMed:12884090};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00297, ECO:0000269|PubMed:12884090};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19 uM for manganese {ECO:0000269|PubMed:12884090};
CC KM=3000 uM for veratryl alcohol {ECO:0000269|PubMed:12884090};
CC KM=4 uM for reactive black 5 {ECO:0000269|PubMed:12884090};
CC KM=3 uM for 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonate) (ABTS)
CC {ECO:0000269|PubMed:12884090};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297,
CC ECO:0000269|PubMed:9987124}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
CC {ECO:0000305}.
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DR EMBL; AF007222; AAD01402.1; -; mRNA.
DR EMBL; AF007224; AAD01404.1; -; Genomic_DNA.
DR PDB; 2BOQ; X-ray; 1.33 A; A=31-361.
DR PDB; 2VKA; X-ray; 2.00 A; A=31-347.
DR PDB; 2W23; X-ray; 1.94 A; A=31-346.
DR PDB; 3FJW; X-ray; 2.80 A; A/B=31-361.
DR PDB; 3FKG; X-ray; 1.81 A; A=31-361.
DR PDB; 3FM1; X-ray; 1.78 A; A=31-361.
DR PDB; 3FM4; X-ray; 2.11 A; A=31-361.
DR PDB; 3FM6; X-ray; 1.13 A; A=31-361.
DR PDB; 3FMU; X-ray; 1.04 A; A=31-361.
DR PDB; 4FCN; X-ray; 1.70 A; A=31-349.
DR PDB; 4FCS; X-ray; 1.50 A; A=31-345.
DR PDB; 4FDQ; X-ray; 1.60 A; A=31-345.
DR PDB; 4FEF; X-ray; 2.00 A; A=31-345.
DR PDB; 4G05; X-ray; 2.35 A; A=31-347.
DR PDB; 5ABN; X-ray; 2.19 A; A=31-361.
DR PDB; 5ABO; X-ray; 1.09 A; A=33-361.
DR PDB; 5ABQ; X-ray; 2.29 A; A=33-361.
DR PDB; 5FNB; X-ray; 1.79 A; A/B=31-359.
DR PDB; 5FNE; X-ray; 1.50 A; A=31-359.
DR PDBsum; 2BOQ; -.
DR PDBsum; 2VKA; -.
DR PDBsum; 2W23; -.
DR PDBsum; 3FJW; -.
DR PDBsum; 3FKG; -.
DR PDBsum; 3FM1; -.
DR PDBsum; 3FM4; -.
DR PDBsum; 3FM6; -.
DR PDBsum; 3FMU; -.
DR PDBsum; 4FCN; -.
DR PDBsum; 4FCS; -.
DR PDBsum; 4FDQ; -.
DR PDBsum; 4FEF; -.
DR PDBsum; 4G05; -.
DR PDBsum; 5ABN; -.
DR PDBsum; 5ABO; -.
DR PDBsum; 5ABQ; -.
DR PDBsum; 5FNB; -.
DR PDBsum; 5FNE; -.
DR AlphaFoldDB; O94753; -.
DR SMR; O94753; -.
DR CAZy; AA2; Auxiliary Activities 2.
DR CLAE; VPO2B_PLEER; -.
DR PeroxiBase; 2299; PerVP05-2_CBS613.
DR BioCyc; MetaCyc:MON-14479; -.
DR BRENDA; 1.11.1.16; 4910.
DR BRENDA; 1.11.1.7; 4910.
DR SABIO-RK; O94753; -.
DR EvolutionaryTrace; O94753; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016689; F:manganese peroxidase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052750; F:reactive-black-5:hydrogen-peroxide oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00692; ligninase; 1.
DR InterPro; IPR044831; Ccp1-like.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR001621; Ligninase.
DR InterPro; IPR024589; Ligninase_C.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR31356; PTHR31356; 1.
DR Pfam; PF00141; peroxidase; 1.
DR Pfam; PF11895; Peroxidase_ext; 1.
DR PRINTS; PR00462; LIGNINASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Heme; Hydrogen peroxide; Iron; Lignin degradation; Manganese;
KW Metal-binding; Organic radical; Oxidoreductase; Peroxidase; Secreted;
KW Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..30
FT /evidence="ECO:0000269|PubMed:9987124"
FT /id="PRO_0000308171"
FT CHAIN 31..361
FT /note="Versatile peroxidase VPL2"
FT /id="PRO_5000053247"
FT ACT_SITE 77
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT ACT_SITE 194
FT /note="Tryptophan radical intermediate"
FT /evidence="ECO:0000269|PubMed:16246366"
FT BINDING 66
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:16246366"
FT BINDING 70
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 199
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 203..207
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT BINDING 205
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:16246366"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT SITE 73
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..45
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:16246366"
FT DISULFID 44..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:16246366"
FT DISULFID 64..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:16246366"
FT DISULFID 272..337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:16246366"
FT MUTAGEN 106
FT /note="P->H: Minor effects on activity."
FT /evidence="ECO:0000269|PubMed:16246366"
FT MUTAGEN 194
FT /note="W->H,S: Complete loss of activity toward veratryl
FT alcohol and reactive black 5. No effect on manganese
FT oxidation."
FT /evidence="ECO:0000269|PubMed:16246366"
FT MUTAGEN 205
FT /note="D->A: Complete loss of oxidation activity toward
FT manganese."
FT /evidence="ECO:0000269|PubMed:12884090"
FT MUTAGEN 262
FT /note="H->F: Minor effects on activity."
FT /evidence="ECO:0000269|PubMed:16246366"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5ABN"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:3FMU"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:3FMU"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:3FMU"
FT HELIX 66..79
FT /evidence="ECO:0007829|PDB:3FMU"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:3FMU"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:3FMU"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:3FMU"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:3FMU"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:3FMU"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:3FMU"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:3FMU"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:3FMU"
FT HELIX 129..142
FT /evidence="ECO:0007829|PDB:3FMU"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:3FMU"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:3FMU"
FT HELIX 196..201
FT /evidence="ECO:0007829|PDB:3FMU"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:3FMU"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:3FMU"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:3FMU"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:5FNB"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:3FMU"
FT HELIX 259..266
FT /evidence="ECO:0007829|PDB:3FMU"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:3FMU"
FT HELIX 271..276
FT /evidence="ECO:0007829|PDB:3FMU"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:3FMU"
FT HELIX 281..296
FT /evidence="ECO:0007829|PDB:3FMU"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:3FMU"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:3FMU"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:3FMU"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:3FMU"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:3FMU"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:5ABO"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:5FNE"
SQ SEQUENCE 361 AA; 37624 MW; 18C4C6900F22A1E5 CRC64;
MSFKTLSALA LALGAAVQFA SAAVPLVQKR ATCDDGRTTA NAACCILFPI LDDIQENLFD
GAQCGEEVHE SLRLTFHDAI GFSPTLGGGG ADGSIIAFDT IETNFPANAG IDEIVSAQKP
FVAKHNISAG DFIQFAGAVG VSNCPGGVRI PFFLGRPDAV AASPDHLVPE PFDSVDSILA
RMGDAGFSPV EVVWLLASHS IAAADKVDPS IPGTPFDSTP GVFDSQFFIE TQLKGRLFPG
TADNKGEAQS PLQGEIRLQS DHLLARDPQT ACEWQSMVNN QPKIQNRFAA TMSKMALLGQ
DKTKLIDCSD VIPTPPALVG AAHLPAGFSL SDVEQACAAT PFPALTADPG PVTSVPPVPG
S
