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O94753 (VPL2_PLEER) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Versatile peroxidase VPL2
EC=1.11.1.16
Alternative name(s):
Versatile liquid phase peroxidase 2
Gene names
Name:vpl2
OrganismPleurotus eryngii (Boletus of the steppes)
Taxonomic identifier5323 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Agaricomycetidae › Agaricales › Pleurotaceae › Pleurotus

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

A versatile ligninolytic peroxidase that combines the substrate-specificity characteristics of the two other ligninolytic peroxidases, manganese peroxidase and lignin peroxidase. Ref.1

Catalytic activity

Reactive Black 5 + H2O2 = oxidized Reactive Black 5 + 2 H2O.

Donor + H2O2 = oxidized donor + 2 H2O.

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per subunit. Ref.2

Binds 2 calcium ions per subunit. Ref.2

Subcellular location

Secreted Ref.1.

Sequence similarities

Belongs to the peroxidase family. Ligninase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=19 µM for manganese Ref.2

KM=3000 µM for veratryl alcohol

KM=4 µM for reactive black 5

KM=3 µM for 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonate) (ABTS)

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 308
PRO_0000308171
Chain31 – 361331Versatile peroxidase VPL2
PRO_5000053247

Regions

Region203 – 2075Heme binding

Sites

Active site771Proton acceptor By similarity
Active site1941Tryptophan radical intermediate
Metal binding661Manganese
Metal binding701Manganese By similarity
Metal binding781Calcium 1
Metal binding901Calcium 1; via carbonyl oxygen
Metal binding921Calcium 1
Metal binding941Calcium 1
Metal binding1991Iron (heme axial ligand)
Metal binding2001Calcium 2
Metal binding2051Manganese
Metal binding2171Calcium 2
Metal binding2191Calcium 2
Metal binding2221Calcium 2; via carbonyl oxygen
Metal binding2241Calcium 2
Site731Transition state stabilizer By similarity

Amino acid modifications

Glycosylation1261N-linked (GlcNAc...) Potential
Disulfide bond33 ↔ 45 Ref.3
Disulfide bond44 ↔ 308 Ref.3
Disulfide bond64 ↔ 144 Ref.3
Disulfide bond272 ↔ 337 Ref.3

Experimental info

Mutagenesis1061P → H: Minor effects on activity. Ref.3
Mutagenesis1941W → H or S: Complete loss of activity toward veratryl alcohol and reactive black 5. No effect on manganese oxidation. Ref.3
Mutagenesis2051D → A: Complete loss of oxidation activity toward manganese. Ref.2
Mutagenesis2621H → F: Minor effects on activity. Ref.3

Secondary structure

1 ..................................................... 361
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O94753 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 18C4C6900F22A1E5

FASTA36137,624
        10         20         30         40         50         60 
MSFKTLSALA LALGAAVQFA SAAVPLVQKR ATCDDGRTTA NAACCILFPI LDDIQENLFD 

        70         80         90        100        110        120 
GAQCGEEVHE SLRLTFHDAI GFSPTLGGGG ADGSIIAFDT IETNFPANAG IDEIVSAQKP 

       130        140        150        160        170        180 
FVAKHNISAG DFIQFAGAVG VSNCPGGVRI PFFLGRPDAV AASPDHLVPE PFDSVDSILA 

       190        200        210        220        230        240 
RMGDAGFSPV EVVWLLASHS IAAADKVDPS IPGTPFDSTP GVFDSQFFIE TQLKGRLFPG 

       250        260        270        280        290        300 
TADNKGEAQS PLQGEIRLQS DHLLARDPQT ACEWQSMVNN QPKIQNRFAA TMSKMALLGQ 

       310        320        330        340        350        360 
DKTKLIDCSD VIPTPPALVG AAHLPAGFSL SDVEQACAAT PFPALTADPG PVTSVPPVPG 


S

« Hide

References

[1]"Molecular characterization of a novel peroxidase isolated from the ligninolytic fungus Pleurotus eryngii."
Ruiz-Duenas F.J., Martinez M.J., Martinez A.T.
Mol. Microbiol. 31:223-235(1999) [PubMed: 9987124] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 31-47, FUNCTION, SUBCELLULAR LOCATION.
Strain: ATCC 90787 / IJFM A169 / CBS 613.91.
[2]"NMR study of manganese(II) binding by a new versatile peroxidase from the white-rot fungus Pleurotus eryngii."
Banci L., Camarero S., Martinez A.T., Martinez M.J., Perez-Boada M., Pierattelli R., Ruiz-Duenas F.J.
J. Biol. Inorg. Chem. 8:751-760(2003) [PubMed: 12884090] [Abstract]
Cited for: STRUCTURE BY NMR, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, MUTAGENESIS OF ASP-205.
Strain: ATCC 90787 / IJFM A169 / CBS 613.91.
[3]"Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallographic investigation of three long-range electron transfer pathways."
Perez-Boada M., Ruiz-Duenas F.J., Pogni R., Basosi R., Choinowski T., Martinez M.J., Piontek K., Martinez A.T.
J. Mol. Biol. 354:385-402(2005) [PubMed: 16246366] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 31-361 OF WILD-TYPE AND MUTANT SER-194 IN COMPLEX WITH HEME; MANGANESE AND CALCIUM IONS, DISULFIDE BONDS, RADICAL INTERMEDIATE, CATALYTIC MECHANISM, MUTAGENESIS OF PRO-106; TRP-194 AND HIS-262.
Strain: ATCC 90787 / IJFM A169 / CBS 613.91.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF007222 mRNA. Translation: AAD01402.1.
AF007224 Genomic DNA. Translation: AAD01404.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BOQX-ray1.33A31-361[»]
2VKAX-ray2.00A31-347[»]
2W23X-ray1.94A31-346[»]
3FJWX-ray2.80A/B31-361[»]
3FKGX-ray1.81A31-361[»]
3FM1X-ray1.78A31-361[»]
3FM4X-ray2.11A31-361[»]
3FM6X-ray1.13A31-361[»]
3FMUX-ray1.04A31-361[»]
ProteinModelPortalO94753.
SMRO94753. Positions 31-349.
ModBaseSearch...

Protein family/group databases

PeroxiBase2299. PerVP02.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14479.
BRENDA1.11.1.16. 4910.

Family and domain databases

InterProIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamPF11895. DUF3415. 1 hit.
PF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSPR00462. LIGNINASE.
PR00458. PEROXIDASE.
SUPFAMSSF48113. Peroxidase_super. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVPL2_PLEER
AccessionPrimary (citable) accession number: O94753
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: May 1, 1999
Last modified: December 14, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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