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Q9UVP6

- VPS1_PLEER

UniProt

Q9UVP6 - VPS1_PLEER

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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

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
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

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-KW
Complete GO annotation...

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

« 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:
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 29, 2014
This is version 68 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