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Q9UVP6 (VPS1_PLEER) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Versatile peroxidase VPS1
EC=1.11.1.16
Alternative name(s):
Versatile solid phase peroxidase 1
Gene names
Name:vps1
Synonyms:ps1
OrganismPleurotus eryngii (Boletus of the steppes)
Taxonomic identifier5323 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Agaricomycetes › Agaricomycetidae › Agaricales › Pleurotaceae › Pleurotus

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

A versatile ligninolytic peroxidase that combines the substrate-specificity characteristics of the two other ligninolytic peroxidases, manganese peroxidase and lignin peroxidase. Ref.2

Catalytic activity

Reactive Black 5 + H2O2 = oxidized Reactive Black 5 + 2 H2O.

Donor + H2O2 = oxidized donor + 2 H2O.

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity.

Binds 2 calcium ions per subunit By similarity.

Subcellular location

Secreted.

Sequence similarities

Belongs to the peroxidase family. Ligninase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=48 µM for manganese Ref.2

KM=9 µM for H2O2 (in manganese oxidation)

KM=2 µM for H2O2 (in manganese-independent oxidations)

KM=17 µM for methoxyhydroquinone

KM=200 µM for syringol

KM=3500 µM for veratryl alcohol

KM=2 µM for reactive black 5

pH dependence:

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 3111
PRO_0000308169
Chain32 – 370339Versatile peroxidase VPS1
PRO_5000056981

Regions

Region210 – 2145Heme binding By similarity

Sites

Active site781Proton acceptor By similarity
Active site2011Tryptophan radical intermediate By similarity
Metal binding671Manganese By similarity
Metal binding711Manganese By similarity
Metal binding791Calcium 1 By similarity
Metal binding971Calcium 1; via carbonyl oxygen By similarity
Metal binding991Calcium 1 By similarity
Metal binding1011Calcium 1 By similarity
Metal binding2061Iron (heme axial ligand) By similarity
Metal binding2071Calcium 2 By similarity
Metal binding2121Manganese By similarity
Metal binding2241Calcium 2 By similarity
Metal binding2261Calcium 2 By similarity
Metal binding2291Calcium 2; via carbonyl oxygen
Metal binding2311Calcium 2 By similarity
Site741Transition state stabilizer By similarity

Amino acid modifications

Glycosylation1331N-linked (GlcNAc...) Potential
Disulfide bond34 ↔ 46 By similarity
Disulfide bond45 ↔ 315 By similarity
Disulfide bond65 ↔ 151 By similarity
Disulfide bond279 ↔ 344 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9UVP6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 86DA6F99C79D08B9

FASTA37039,046
        10         20         30         40         50         60 
MAFAKLSAFV LALGATVALG ESPTHRCLNK RVTCATGQTT ANEACCALFP ILDDIQTNLF 

        70         80         90        100        110        120 
DGAQCGEEVH ESLRLTFHDA IAFSPALTNA GQFGGGGADG SMIIFSDTEP NFHANLGIDE 

       130        140        150        160        170        180 
IVEAQKPFIA RHNISAADFI QFAGAIGVSN CAGAPRLNFF LGRPDATQIP PDGLVPEPFD 

       190        200        210        220        230        240 
DVTKILSRMG DAGFSTVEVV WLLASHTIAA ADHVDPSIPG TPFDSTPSTF DSQFFLETML 

       250        260        270        280        290        300 
QGTAFPGTPG NQGEVESPLA GEMRLQSDFL LARDSRSACE WQSMVNNMPK IQNRFTQVMK 

       310        320        330        340        350        360 
KLSLLGHNQA DLIDCSDVIP VPKTLTKAAT FPAGKSQADV EIVCNAAATP FPALASDPGP 

       370 
VTAVPPVPPS

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF175710 Genomic DNA. Translation: AAD54310.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BQWmodel-A32-318[»]
1QJRmodel-A32-370[»]
ProteinModelPortalQ9UVP6.
SMRQ9UVP6. Positions 33-358.
ModBaseSearch...

Protein family/group databases

mycoCLAPVPOC_PLEER.
PeroxiBase2302. PerVP02.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA1.11.1.16. 4910.

Family and domain databases

InterProIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamPF11895. DUF3415. 1 hit.
PF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSPR00462. LIGNINASE.
PR00458. PEROXIDASE.
SUPFAMSSF48113. Peroxidase_super. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVPS1_PLEER
AccessionPrimary (citable) accession number: Q9UVP6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: May 1, 2000
Last modified: April 3, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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