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Q9UVP6

- VPS1_PLEER

UniProt

Q9UVP6 - VPS1_PLEER

Protein

Versatile peroxidase VPS1

Gene

vps1

Organism
Pleurotus eryngii (Boletus of the steppes)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

    Reactive Black 5 + H2O2 = oxidized Reactive Black 5 + 2 H2O.
    Donor + H2O2 = oxidized donor + 2 H2O.PROSITE-ProRule annotation

    Cofactori

    Binds 1 heme B (iron-protoporphyrin IX) group per subunit.PROSITE-ProRule annotation
    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)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi67 – 671ManganeseBy similarity
    Metal bindingi71 – 711ManganeseBy similarity
    Sitei74 – 741Transition state stabilizerPROSITE-ProRule annotation
    Active sitei78 – 781Proton acceptorPROSITE-ProRule annotation
    Metal bindingi79 – 791Calcium 1PROSITE-ProRule annotation
    Metal bindingi97 – 971Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
    Metal bindingi99 – 991Calcium 1PROSITE-ProRule annotation
    Metal bindingi101 – 1011Calcium 1PROSITE-ProRule annotation
    Active sitei201 – 2011Tryptophan radical intermediateBy similarity
    Metal bindingi206 – 2061Iron (heme axial ligand)PROSITE-ProRule annotation
    Metal bindingi207 – 2071Calcium 2PROSITE-ProRule annotation
    Metal bindingi212 – 2121ManganeseBy similarity
    Metal bindingi224 – 2241Calcium 2PROSITE-ProRule annotation
    Metal bindingi226 – 2261Calcium 2PROSITE-ProRule annotation
    Metal bindingi229 – 2291Calcium 2; via carbonyl oxygen
    Metal bindingi231 – 2311Calcium 2PROSITE-ProRule annotation

    GO - Molecular functioni

    1. heme binding Source: InterPro
    2. metal ion binding Source: UniProtKB-KW
    3. reactive-black-5:hydrogen-peroxide oxidoreductase activity Source: UniProtKB-EC

    GO - Biological processi

    1. hydrogen peroxide catabolic process Source: UniProtKB-KW
    2. lignin catabolic process Source: UniProtKB-KW

    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

    mycoCLAPiVPO2C_PLEER.
    PeroxiBasei2302. PerVP02.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Versatile peroxidase VPS1 (EC:1.11.1.16)
    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

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Propeptidei21 – 31112 PublicationsPRO_0000308169Add
    BLAST
    Chaini32 – 370339Versatile peroxidase VPS1PRO_5000056981Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi34 ↔ 46PROSITE-ProRule annotation
    Disulfide bondi45 ↔ 315PROSITE-ProRule annotation
    Disulfide bondi65 ↔ 151PROSITE-ProRule annotation
    Glycosylationi133 – 1331N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi279 ↔ 344PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Organic radical, Zymogen

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BQWmodel-A32-318[»]
    1QJRmodel-A32-370[»]
    ProteinModelPortaliQ9UVP6.
    SMRiQ9UVP6. Positions 33-358.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni210 – 2145Heme bindingBy similarity

    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.

    Q9UVP6-1 [UniParc]FASTAAdd to Basket

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    MAFAKLSAFV LALGATVALG ESPTHRCLNK RVTCATGQTT ANEACCALFP    50
    ILDDIQTNLF DGAQCGEEVH ESLRLTFHDA IAFSPALTNA GQFGGGGADG 100
    SMIIFSDTEP NFHANLGIDE IVEAQKPFIA RHNISAADFI QFAGAIGVSN 150
    CAGAPRLNFF LGRPDATQIP PDGLVPEPFD DVTKILSRMG DAGFSTVEVV 200
    WLLASHTIAA ADHVDPSIPG TPFDSTPSTF DSQFFLETML QGTAFPGTPG 250
    NQGEVESPLA GEMRLQSDFL LARDSRSACE WQSMVNNMPK IQNRFTQVMK 300
    KLSLLGHNQA DLIDCSDVIP VPKTLTKAAT FPAGKSQADV EIVCNAAATP 350
    FPALASDPGP VTAVPPVPPS 370
    Length:370
    Mass (Da):39,046
    Last modified:May 1, 2000 - v1
    Checksum:i86DA6F99C79D08B9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF175710 Genomic DNA. Translation: AAD54310.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF175710 Genomic DNA. Translation: AAD54310.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BQW model - A 32-318 [» ]
    1QJR model - A 32-370 [» ]
    ProteinModelPortali Q9UVP6.
    SMRi Q9UVP6. Positions 33-358.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    mycoCLAPi VPO2C_PLEER.
    PeroxiBasei 2302. PerVP02.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 1.11.1.16. 4910.

    Family and domain databases

    InterProi IPR010255. Haem_peroxidase.
    IPR002016. Haem_peroxidase_pln/fun/bac.
    IPR001621. Ligninase.
    IPR024589. Ligninase_C.
    IPR019794. Peroxidases_AS.
    IPR019793. Peroxidases_heam-ligand_BS.
    [Graphical view ]
    Pfami PF11895. DUF3415. 1 hit.
    PF00141. peroxidase. 1 hit.
    [Graphical view ]
    PRINTSi PR00462. LIGNINASE.
    PR00458. PEROXIDASE.
    SUPFAMi SSF48113. SSF48113. 1 hit.
    PROSITEi PS00435. PEROXIDASE_1. 1 hit.
    PS00436. PEROXIDASE_2. 1 hit.
    PS50873. PEROXIDASE_4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The cloning of a new peroxidase found in lignocellulose cultures of Pleurotus eryngii and sequence comparison with other fungal peroxidases."
      Camarero S., Ruiz-Duenas F.J., Sarkar S., Martinez M.J., Martinez A.T.
      FEMS Microbiol. Lett. 191:37-43(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 32-51.
      Strain: ATCC 90787 / IJFM A169 / CBS 613.91.
      Tissue: Mycelium.
    2. "Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites."
      Camarero S., Sarkar S., Ruiz-Duenas F.J., Martinez M.J., Martinez A.T.
      J. Biol. Chem. 274:10324-10330(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 32-40, FUNCTION, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING OF 32-370.
      Strain: ATCC 90787 / IJFM A169 / CBS 613.91.
      Tissue: Mycelium.

    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: October 1, 2014
    This is version 67 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

    External Data

    Dasty 3