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Protein

Versatile peroxidase VPS1

Gene

vps1

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.1 Publication
2 manganese(II) + 2 H+ + H2O2 = 2 manganese(III) + 2 H2O.1 Publication

Cofactori

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

Kineticsi

  1. KM=48 µM for manganese1 Publication
  2. KM=9 µM for H2O2 (in manganese oxidation)1 Publication
  3. KM=2 µM for H2O2 (in manganese-independent oxidations)1 Publication
  4. KM=17 µM for methoxyhydroquinone1 Publication
  5. KM=200 µM for syringol1 Publication
  6. KM=3500 µM for veratryl alcohol1 Publication
  7. KM=2 µM for reactive black 51 Publication

    pH dependencei

    Optimum pH is 5 for manganese oxidation reaction, and around 3 for all the manganese-independent reactions.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi67ManganeseBy similarity1
    Metal bindingi71ManganeseBy similarity1
    Sitei74Transition state stabilizerPROSITE-ProRule annotation1
    Active sitei78Proton acceptorPROSITE-ProRule annotation1
    Metal bindingi79Calcium 1PROSITE-ProRule annotation1
    Metal bindingi97Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation1
    Metal bindingi99Calcium 1PROSITE-ProRule annotation1
    Metal bindingi101Calcium 1PROSITE-ProRule annotation1
    Active sitei201Tryptophan radical intermediateBy similarity1
    Metal bindingi206Iron (heme axial ligand)PROSITE-ProRule annotation1
    Metal bindingi207Calcium 2PROSITE-ProRule annotation1
    Metal bindingi212ManganeseBy similarity1
    Metal bindingi224Calcium 2PROSITE-ProRule annotation1
    Metal bindingi226Calcium 2PROSITE-ProRule annotation1
    Metal bindingi229Calcium 2; via carbonyl oxygen1
    Metal bindingi231Calcium 2PROSITE-ProRule annotation1

    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

    BRENDAi1.11.1.16. 4910.

    Protein family/group databases

    CAZyiAA2. Auxiliary Activities 2.
    mycoCLAPiVPO2C_PLEER.
    PeroxiBasei2302. PerVP02.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Versatile peroxidase VPS1 (EC:1.11.1.161 Publication)
    Alternative name(s):
    Versatile solid phase peroxidase 1
    Gene namesi
    Name:vps1
    Synonyms:ps1
    OrganismiPleurotus eryngii (Boletus of the steppes)
    Taxonomic identifieri5323 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesPleurotaceaePleurotus

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 20Sequence analysisAdd BLAST20
    PropeptideiPRO_000030816921 – 312 PublicationsAdd BLAST11
    ChainiPRO_500005698132 – 370Versatile peroxidase VPS1Add BLAST339

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi34 ↔ 46PROSITE-ProRule annotation
    Disulfide bondi45 ↔ 315PROSITE-ProRule annotation
    Disulfide bondi65 ↔ 151PROSITE-ProRule annotation
    Glycosylationi133N-linked (GlcNAc...)Sequence analysis1
    Disulfide bondi279 ↔ 344PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Organic radical, Zymogen

    Structurei

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1BQWmodel-A32-318[»]
    1QJRmodel-A32-370[»]
    ProteinModelPortaliQ9UVP6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni210 – 214Heme bindingBy similarity5

    Sequence similaritiesi

    Belongs to the peroxidase family. Ligninase subfamily.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    KOiK20205.

    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.

    Q9UVP6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAFAKLSAFV LALGATVALG ESPTHRCLNK RVTCATGQTT ANEACCALFP
    60 70 80 90 100
    ILDDIQTNLF DGAQCGEEVH ESLRLTFHDA IAFSPALTNA GQFGGGGADG
    110 120 130 140 150
    SMIIFSDTEP NFHANLGIDE IVEAQKPFIA RHNISAADFI QFAGAIGVSN
    160 170 180 190 200
    CAGAPRLNFF LGRPDATQIP PDGLVPEPFD DVTKILSRMG DAGFSTVEVV
    210 220 230 240 250
    WLLASHTIAA ADHVDPSIPG TPFDSTPSTF DSQFFLETML QGTAFPGTPG
    260 270 280 290 300
    NQGEVESPLA GEMRLQSDFL LARDSRSACE WQSMVNNMPK IQNRFTQVMK
    310 320 330 340 350
    KLSLLGHNQA DLIDCSDVIP VPKTLTKAAT FPAGKSQADV EIVCNAAATP
    360 370
    FPALASDPGP VTAVPPVPPS
    Length:370
    Mass (Da):39,046
    Last modified:May 1, 2000 - v1
    Checksum:i86DA6F99C79D08B9
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF175710 Genomic DNA. Translation: AAD54310.1.

    Genome annotation databases

    KEGGiag:AAD54310.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF175710 Genomic DNA. Translation: AAD54310.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1BQWmodel-A32-318[»]
    1QJRmodel-A32-370[»]
    ProteinModelPortaliQ9UVP6.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiAA2. Auxiliary Activities 2.
    mycoCLAPiVPO2C_PLEER.
    PeroxiBasei2302. PerVP02.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAD54310.

    Phylogenomic databases

    KOiK20205.

    Enzyme and pathway databases

    BRENDAi1.11.1.16. 4910.

    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 nameiVPS1_PLEER
    AccessioniPrimary (citable) accession number: Q9UVP6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 23, 2007
    Last sequence update: May 1, 2000
    Last modified: November 30, 2016
    This is version 78 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.