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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)DescriptionActionsGraphical viewLength
    Metal bindingi66Manganese1 Publication1
    Metal bindingi70ManganeseBy similarity1
    Sitei73Transition state stabilizerPROSITE-ProRule annotation1
    Active sitei77Proton acceptorPROSITE-ProRule annotation1
    Metal bindingi78Calcium 11
    Metal bindingi90Calcium 1; via carbonyl oxygen1
    Metal bindingi92Calcium 11
    Metal bindingi94Calcium 11
    Active sitei194Tryptophan radical intermediate1
    Metal bindingi199Iron (heme axial ligand)1
    Metal bindingi200Calcium 21
    Metal bindingi205Manganese1 Publication1
    Metal bindingi217Calcium 21
    Metal bindingi219Calcium 21
    Metal bindingi222Calcium 2; via carbonyl oxygen1
    Metal bindingi224Calcium 21

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi106P → H: Minor effects on activity. 1 Publication1
    Mutagenesisi194W → H or S: Complete loss of activity toward veratryl alcohol and reactive black 5. No effect on manganese oxidation. 1 Publication1
    Mutagenesisi205D → A: Complete loss of oxidation activity toward manganese. 1 Publication1
    Mutagenesisi262H → F: Minor effects on activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 22Sequence analysisAdd BLAST22
    PropeptideiPRO_000030817123 – 301 Publication8
    ChainiPRO_500005324731 – 361Versatile peroxidase VPL2Add BLAST331

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi33 ↔ 45PROSITE-ProRule annotation1 Publication
    Disulfide bondi44 ↔ 308PROSITE-ProRule annotation1 Publication
    Disulfide bondi64 ↔ 144PROSITE-ProRule annotation1 Publication
    Glycosylationi126N-linked (GlcNAc...)Sequence analysis1
    Disulfide bondi272 ↔ 337PROSITE-ProRule annotation1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Organic radical, Zymogen

    Structurei

    Secondary structure

    1361
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi34 – 36Combined sources3
    Helixi42 – 46Combined sources5
    Helixi47 – 57Combined sources11
    Turni60 – 62Combined sources3
    Helixi66 – 79Combined sources14
    Turni84 – 86Combined sources3
    Beta strandi90 – 93Combined sources4
    Helixi94 – 97Combined sources4
    Helixi99 – 102Combined sources4
    Helixi106 – 108Combined sources3
    Turni109 – 111Combined sources3
    Helixi112 – 124Combined sources13
    Beta strandi125 – 127Combined sources3
    Helixi129 – 142Combined sources14
    Helixi175 – 184Combined sources10
    Helixi189 – 195Combined sources7
    Helixi196 – 201Combined sources6
    Beta strandi203 – 208Combined sources6
    Beta strandi214 – 218Combined sources5
    Helixi226 – 230Combined sources5
    Beta strandi239 – 242Combined sources4
    Beta strandi250 – 252Combined sources3
    Helixi259 – 266Combined sources8
    Turni268 – 270Combined sources3
    Helixi271 – 276Combined sources6
    Turni277 – 279Combined sources3
    Helixi281 – 296Combined sources16
    Turni297 – 299Combined sources3
    Helixi302 – 304Combined sources3
    Beta strandi305 – 307Combined sources3
    Helixi309 – 311Combined sources3
    Helixi330 – 332Combined sources3
    Beta strandi338 – 340Combined sources3
    Beta strandi349 – 351Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    5FNBX-ray1.79A/B31-359[»]
    5FNEX-ray1.50A31-359[»]
    ProteinModelPortaliO94753.
    SMRiO94753.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO94753.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni203 – 207Heme binding5

    Sequence similaritiesi

    Belongs to the peroxidase family. Ligninase subfamily.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    CDDicd00692. ligninase. 1 hit.
    InterProiIPR010255. Haem_peroxidase.
    IPR002016. Haem_peroxidase_pln/fun/bac.
    IPR001621. Ligninase.
    IPR024589. Ligninase_C.
    IPR019794. Peroxidases_AS.
    IPR019793. Peroxidases_heam-ligand_BS.
    [Graphical view]
    PfamiPF00141. peroxidase. 1 hit.
    PF11895. Peroxidase_ext. 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
    PDB 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[»]
    5FNBX-ray1.79A/B31-359[»]
    5FNEX-ray1.50A31-359[»]
    ProteinModelPortaliO94753.
    SMRiO94753.
    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

    CDDicd00692. ligninase. 1 hit.
    InterProiIPR010255. Haem_peroxidase.
    IPR002016. Haem_peroxidase_pln/fun/bac.
    IPR001621. Ligninase.
    IPR024589. Ligninase_C.
    IPR019794. Peroxidases_AS.
    IPR019793. Peroxidases_heam-ligand_BS.
    [Graphical view]
    PfamiPF00141. peroxidase. 1 hit.
    PF11895. Peroxidase_ext. 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: November 30, 2016
    This is version 90 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.