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Protein

Versatile peroxidase VPL1

Gene

vpl1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi66ManganeseBy similarity1
Metal bindingi70ManganeseBy similarity1
Sitei73Transition state stabilizerPROSITE-ProRule annotation1
Active sitei77Proton acceptorPROSITE-ProRule annotation1
Metal bindingi78Calcium 1PROSITE-ProRule annotation1
Metal bindingi90Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi92Calcium 1PROSITE-ProRule annotation1
Metal bindingi94Calcium 1PROSITE-ProRule annotation1
Active sitei194Tryptophan radical intermediateBy similarity1
Metal bindingi199Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi200Calcium 2PROSITE-ProRule annotation1
Metal bindingi205ManganeseBy similarity1
Metal bindingi217Calcium 2PROSITE-ProRule annotation1
Metal bindingi219Calcium 2PROSITE-ProRule annotation1
Metal bindingi222Calcium 2; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi224Calcium 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

BioCyciMetaCyc:MONOMER-14478.

Protein family/group databases

CAZyiAA2. Auxiliary Activities 2.
mycoCLAPiVPO2A_PLEER.
PeroxiBasei2301. PerVP05-1_CBS613.

Names & Taxonomyi

Protein namesi
Recommended name:
Versatile peroxidase VPL1 (EC:1.11.1.161 Publication)
Alternative name(s):
Versatile liquid phase peroxidase 1
Gene namesi
Name:vpl1
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
PropeptideiPRO_000030817023 – 301 Publication8
ChainiPRO_500005324631 – 361Versatile peroxidase VPL1Add BLAST331

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Organic radical, Zymogen

Proteomic databases

PRIDEiQ9UR19.

Structurei

Secondary structure

1361
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 – 185Combined sources11
Helixi189 – 195Combined sources7
Helixi196 – 201Combined sources6
Beta strandi203 – 208Combined sources6
Beta strandi214 – 218Combined sources5
Helixi226 – 230Combined sources5
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
1A20model-A31-359[»]
4BLKX-ray1.05A31-361[»]
4BLLX-ray1.10A31-361[»]
4BLNX-ray1.15A31-361[»]
4BLXX-ray1.25A31-361[»]
4BLYX-ray1.79A31-361[»]
4BLZX-ray2.00A/B31-361[»]
4BM0X-ray2.20A31-361[»]
ProteinModelPortaliQ9UR19.
SMRiQ9UR19.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Q9UR19-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFKTLSALA LALGAAVQFA SAAVPLVQKR ATCADGRTTA NAACCVLFPI
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 RMSDAGFSPV 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):37,596
Last modified:May 1, 2000 - v1
Checksum:i5E8297DAFD971BDE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF007221 mRNA. Translation: AAD01401.1.
AF007223 Genomic DNA. Translation: AAD01403.1.

Genome annotation databases

KEGGiag:AAD01401.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF007221 mRNA. Translation: AAD01401.1.
AF007223 Genomic DNA. Translation: AAD01403.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A20model-A31-359[»]
4BLKX-ray1.05A31-361[»]
4BLLX-ray1.10A31-361[»]
4BLNX-ray1.15A31-361[»]
4BLXX-ray1.25A31-361[»]
4BLYX-ray1.79A31-361[»]
4BLZX-ray2.00A/B31-361[»]
4BM0X-ray2.20A31-361[»]
ProteinModelPortaliQ9UR19.
SMRiQ9UR19.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA2. Auxiliary Activities 2.
mycoCLAPiVPO2A_PLEER.
PeroxiBasei2301. PerVP05-1_CBS613.

Proteomic databases

PRIDEiQ9UR19.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAD01401.

Phylogenomic databases

KOiK20205.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14478.

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 nameiVPL1_PLEER
AccessioniPrimary (citable) accession number: Q9UR19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 80 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.