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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi66 – 661ManganeseBy similarity
Metal bindingi70 – 701ManganeseBy similarity
Sitei73 – 731Transition state stabilizerPROSITE-ProRule annotation
Active sitei77 – 771Proton acceptorPROSITE-ProRule annotation
Metal bindingi78 – 781Calcium 1PROSITE-ProRule annotation
Metal bindingi90 – 901Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi92 – 921Calcium 1PROSITE-ProRule annotation
Metal bindingi94 – 941Calcium 1PROSITE-ProRule annotation
Active sitei194 – 1941Tryptophan radical intermediateBy similarity
Metal bindingi199 – 1991Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi200 – 2001Calcium 2PROSITE-ProRule annotation
Metal bindingi205 – 2051ManganeseBy similarity
Metal bindingi217 – 2171Calcium 2PROSITE-ProRule annotation
Metal bindingi219 – 2191Calcium 2PROSITE-ProRule annotation
Metal bindingi222 – 2221Calcium 2; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi224 – 2241Calcium 2PROSITE-ProRule annotation

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Propeptidei23 – 3081 PublicationPRO_0000308170
Chaini31 – 361331Versatile peroxidase VPL1PRO_5000053246Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 ↔ 45PROSITE-ProRule annotation
Disulfide bondi44 ↔ 308PROSITE-ProRule annotation
Disulfide bondi64 ↔ 144PROSITE-ProRule annotation
Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence analysis
Disulfide bondi272 ↔ 337PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein, Organic radical, Zymogen

Proteomic databases

PRIDEiQ9UR19.

Structurei

Secondary structure

1
361
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi42 – 465Combined sources
Helixi47 – 5711Combined sources
Turni60 – 623Combined sources
Helixi66 – 7914Combined sources
Turni84 – 863Combined sources
Beta strandi90 – 934Combined sources
Helixi94 – 974Combined sources
Helixi99 – 1024Combined sources
Helixi106 – 1083Combined sources
Turni109 – 1113Combined sources
Helixi112 – 12413Combined sources
Beta strandi125 – 1273Combined sources
Helixi129 – 14214Combined sources
Helixi175 – 18511Combined sources
Helixi189 – 1957Combined sources
Helixi196 – 2016Combined sources
Beta strandi203 – 2086Combined sources
Beta strandi214 – 2185Combined sources
Helixi226 – 2305Combined sources
Beta strandi250 – 2523Combined sources
Helixi259 – 2668Combined sources
Turni268 – 2703Combined sources
Helixi271 – 2766Combined sources
Turni277 – 2793Combined sources
Helixi281 – 29616Combined sources
Turni297 – 2993Combined sources
Helixi302 – 3043Combined sources
Beta strandi305 – 3073Combined sources
Helixi309 – 3113Combined sources
Helixi330 – 3323Combined sources
Beta strandi338 – 3403Combined sources
Beta strandi349 – 3513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 31-349.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni203 – 2075Heme bindingBy similarity

Sequence similaritiesi

Belongs to the peroxidase family. Ligninase subfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

KOiK20205.

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.

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
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. Positions 31-349.
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

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]
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: September 7, 2016
This is version 77 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.