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Protein

Versatile peroxidase VPL2

Gene

vpl2

Organism
Pleurotus eryngii (Boletus of the steppes)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O.3 Publications
2 manganese(II) + 2 H+ + H2O2 = 2 manganese(III) + 2 H2O.3 Publications

Cofactori

Protein has several cofactor binding sites:
  • heme bPROSITE-ProRule annotation1 PublicationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.PROSITE-ProRule annotation1 Publication
  • Ca2+PROSITE-ProRule annotation1 PublicationNote: Binds 2 calcium ions per subunit.PROSITE-ProRule annotation1 Publication

Kineticsi

  1. KM=19 µM for manganese1 Publication
  2. KM=3000 µM for veratryl alcohol1 Publication
  3. KM=4 µM for reactive black 51 Publication
  4. KM=3 µM for 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonate) (ABTS)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi66 – 661Manganese1 Publication
    Metal bindingi70 – 701ManganeseBy similarity
    Sitei73 – 731Transition state stabilizerPROSITE-ProRule annotation
    Active sitei77 – 771Proton acceptorPROSITE-ProRule annotation
    Metal bindingi78 – 781Calcium 1
    Metal bindingi90 – 901Calcium 1; via carbonyl oxygen
    Metal bindingi92 – 921Calcium 1
    Metal bindingi94 – 941Calcium 1
    Active sitei194 – 1941Tryptophan radical intermediate
    Metal bindingi199 – 1991Iron (heme axial ligand)
    Metal bindingi200 – 2001Calcium 2
    Metal bindingi205 – 2051Manganese1 Publication
    Metal bindingi217 – 2171Calcium 2
    Metal bindingi219 – 2191Calcium 2
    Metal bindingi222 – 2221Calcium 2; via carbonyl oxygen
    Metal bindingi224 – 2241Calcium 2

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide, Lignin degradation

    Keywords - Ligandi

    Calcium, Heme, Iron, Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14479.
    BRENDAi1.11.1.16. 4910.
    1.11.1.7. 4910.

    Protein family/group databases

    CAZyiAA2. Auxiliary Activities 2.
    mycoCLAPiVPO2B_PLEER.
    PeroxiBasei2299. PerVP05-2_CBS613.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Versatile peroxidase VPL2 (EC:1.11.1.163 Publications)
    Alternative name(s):
    Versatile liquid phase peroxidase 2
    Gene namesi
    Name:vpl2
    OrganismiPleurotus eryngii (Boletus of the steppes)
    Taxonomic identifieri5323 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesPleurotaceaePleurotus

    Subcellular locationi

    • Secreted PROSITE-ProRule annotation1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi106 – 1061P → H: Minor effects on activity. 1 Publication
    Mutagenesisi194 – 1941W → H or S: Complete loss of activity toward veratryl alcohol and reactive black 5. No effect on manganese oxidation. 1 Publication
    Mutagenesisi205 – 2051D → A: Complete loss of oxidation activity toward manganese. 1 Publication
    Mutagenesisi262 – 2621H → F: Minor effects on activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence analysisAdd
    BLAST
    Propeptidei23 – 3081 PublicationPRO_0000308171
    Chaini31 – 361331Versatile peroxidase VPL2PRO_5000053247Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi33 ↔ 45PROSITE-ProRule annotation1 Publication
    Disulfide bondi44 ↔ 308PROSITE-ProRule annotation1 Publication
    Disulfide bondi64 ↔ 144PROSITE-ProRule annotation1 Publication
    Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence analysis
    Disulfide bondi272 ↔ 337PROSITE-ProRule annotation1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Organic radical, Zymogen

    Structurei

    Secondary structure

    1
    361
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 363Combined sources
    Helixi42 – 465Combined sources
    Helixi47 – 5711Combined sources
    Turni60 – 623Combined sources
    Helixi66 – 7914Combined sources
    Turni84 – 863Combined sources
    Beta strandi90 – 934Combined sources
    Helixi94 – 974Combined sources
    Helixi99 – 1024Combined sources
    Helixi106 – 1083Combined sources
    Turni109 – 1113Combined sources
    Helixi112 – 12413Combined sources
    Beta strandi125 – 1273Combined sources
    Helixi129 – 14214Combined sources
    Helixi175 – 18410Combined sources
    Helixi189 – 1957Combined sources
    Helixi196 – 2016Combined sources
    Beta strandi203 – 2086Combined sources
    Beta strandi214 – 2185Combined sources
    Helixi226 – 2305Combined sources
    Beta strandi239 – 2424Combined sources
    Beta strandi250 – 2523Combined sources
    Helixi259 – 2668Combined sources
    Turni268 – 2703Combined sources
    Helixi271 – 2766Combined sources
    Turni277 – 2793Combined sources
    Helixi281 – 29616Combined sources
    Turni297 – 2993Combined sources
    Helixi302 – 3043Combined sources
    Beta strandi305 – 3073Combined sources
    Helixi309 – 3113Combined sources
    Helixi330 – 3323Combined sources
    Beta strandi338 – 3403Combined sources
    Beta strandi349 – 3513Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    4FCNX-ray1.70A31-349[»]
    4FCSX-ray1.50A31-345[»]
    4FDQX-ray1.60A31-345[»]
    4FEFX-ray2.00A31-345[»]
    4G05X-ray2.35A31-347[»]
    5ABNX-ray2.19A31-361[»]
    5ABOX-ray1.09A33-361[»]
    5ABQX-ray2.29A33-361[»]
    ProteinModelPortaliO94753.
    SMRiO94753. Positions 31-349.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO94753.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni203 – 2075Heme binding

    Sequence similaritiesi

    Belongs to the peroxidase family. Ligninase subfamily.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR010255. Haem_peroxidase.
    IPR002016. Haem_peroxidase_pln/fun/bac.
    IPR001621. Ligninase.
    IPR024589. Ligninase_C.
    IPR019794. Peroxidases_AS.
    IPR019793. Peroxidases_heam-ligand_BS.
    [Graphical view]
    PfamiPF11895. DUF3415. 1 hit.
    PF00141. peroxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00462. LIGNINASE.
    PR00458. PEROXIDASE.
    SUPFAMiSSF48113. SSF48113. 1 hit.
    PROSITEiPS00435. PEROXIDASE_1. 1 hit.
    PS00436. PEROXIDASE_2. 1 hit.
    PS50873. PEROXIDASE_4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O94753-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSFKTLSALA LALGAAVQFA SAAVPLVQKR ATCDDGRTTA NAACCILFPI
    60 70 80 90 100
    LDDIQENLFD GAQCGEEVHE SLRLTFHDAI GFSPTLGGGG ADGSIIAFDT
    110 120 130 140 150
    IETNFPANAG IDEIVSAQKP FVAKHNISAG DFIQFAGAVG VSNCPGGVRI
    160 170 180 190 200
    PFFLGRPDAV AASPDHLVPE PFDSVDSILA RMGDAGFSPV EVVWLLASHS
    210 220 230 240 250
    IAAADKVDPS IPGTPFDSTP GVFDSQFFIE TQLKGRLFPG TADNKGEAQS
    260 270 280 290 300
    PLQGEIRLQS DHLLARDPQT ACEWQSMVNN QPKIQNRFAA TMSKMALLGQ
    310 320 330 340 350
    DKTKLIDCSD VIPTPPALVG AAHLPAGFSL SDVEQACAAT PFPALTADPG
    360
    PVTSVPPVPG S
    Length:361
    Mass (Da):37,624
    Last modified:May 1, 1999 - v1
    Checksum:i18C4C6900F22A1E5
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF007222 mRNA. Translation: AAD01402.1.
    AF007224 Genomic DNA. Translation: AAD01404.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF007222 mRNA. Translation: AAD01402.1.
    AF007224 Genomic DNA. Translation: AAD01404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    4FCNX-ray1.70A31-349[»]
    4FCSX-ray1.50A31-345[»]
    4FDQX-ray1.60A31-345[»]
    4FEFX-ray2.00A31-345[»]
    4G05X-ray2.35A31-347[»]
    5ABNX-ray2.19A31-361[»]
    5ABOX-ray1.09A33-361[»]
    5ABQX-ray2.29A33-361[»]
    ProteinModelPortaliO94753.
    SMRiO94753. Positions 31-349.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiAA2. Auxiliary Activities 2.
    mycoCLAPiVPO2B_PLEER.
    PeroxiBasei2299. PerVP05-2_CBS613.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14479.
    BRENDAi1.11.1.16. 4910.
    1.11.1.7. 4910.

    Miscellaneous databases

    EvolutionaryTraceiO94753.

    Family and domain databases

    InterProiIPR010255. Haem_peroxidase.
    IPR002016. Haem_peroxidase_pln/fun/bac.
    IPR001621. Ligninase.
    IPR024589. Ligninase_C.
    IPR019794. Peroxidases_AS.
    IPR019793. Peroxidases_heam-ligand_BS.
    [Graphical view]
    PfamiPF11895. DUF3415. 1 hit.
    PF00141. peroxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00462. LIGNINASE.
    PR00458. PEROXIDASE.
    SUPFAMiSSF48113. SSF48113. 1 hit.
    PROSITEiPS00435. PEROXIDASE_1. 1 hit.
    PS00436. PEROXIDASE_2. 1 hit.
    PS50873. PEROXIDASE_4. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiVPL2_PLEER
    AccessioniPrimary (citable) accession number: O94753
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 23, 2007
    Last sequence update: May 1, 1999
    Last modified: September 7, 2016
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.