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P56216 (VAOX_PENSI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vanillyl-alcohol oxidase

EC=1.1.3.38
Alternative name(s):
4-allylphenol oxidase
Aryl-alcohol oxidase
Gene names
Name:VAOA
OrganismPenicillium simplicissimum
Taxonomic identifier69488 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

Protein attributes

Sequence length560 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of vanillin alcohol to vanillin, and also the conversion of a wide range of phenolic compounds bearing side chains of variable size at the para position of the aromatic ring. Crucial for the degradation of the secondary metabolites derived from the degradation of the lignin. Catalyzes besides the oxidation of 4-hydroxybenzyl alcohols, the oxidative deamination of 4-hydroxybenzylamines, the oxidative demethylation of 4-(methoxy-methyl)phenols and the oxidative hydration of 4-allylphenols. Most active with 4-allylphenols.

Catalytic activity

Vanillyl alcohol + O2 = vanillin + H2O2.

Cofactor

Binds 1 FAD covalently per subunit.

Enzyme regulation

Competitively inhibited by cinnamyl and coniferyl alcohols and by isoeugenol.

Subunit structure

Homooctamer (tetramer of tightly interacting dimers).

Subcellular location

Peroxisome. Cytoplasm Ref.7.

Induction

By 4-methoxybenzyl alcohols, anisyl and veratryl alcohols. Repressed by carbon catabolite.

Sequence similarities

Contains 1 FAD-binding PCMH-type domain.

To bacterial flavocytochrome p-cresol methyl hydroxylase.

Biophysicochemical properties

pH dependence:

Optimum pH is about 10.

Temperature dependence:

Optimum temperature is 38 degrees Celsius.

Ontologies

Keywords
   Biological processMethanol utilization
   Cellular componentCytoplasm
Peroxisome
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processmethanol metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionUDP-N-acetylmuramate dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

vanillyl-alcohol oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 560560Vanillyl-alcohol oxidase
PRO_0000065763

Regions

Domain67 – 272206FAD-binding PCMH-type

Sites

Active site1081
Active site5031
Active site5041
Site1701Important for the catalytic mechanism; Involved in substrate deprotonation

Amino acid modifications

Modified residue4221Tele-8alpha-FAD histidine

Experimental info

Sequence conflict2741R → G in CAA75722. Ref.1
Sequence conflict3301R → K in CAA75722. Ref.1

Secondary structure

.......................................................................................................... 560
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56216 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: C3B4E4A966C1BCEE

FASTA56063,035
        10         20         30         40         50         60 
MSKTQEFRPL TLPPKLSLSD FNEFIQDIIR IVGSENVEVI SSKDQIVDGS YMKPTHTHDP 

        70         80         90        100        110        120 
HHVMDQDYFL ASAIVAPRNV ADVQSIVGLA NKFSFPLWPI SIGRNSGYGG AAPRVSGSVV 

       130        140        150        160        170        180 
LDMGKNMNRV LEVNVEGAYC VVEPGVTYHD LHNYLEANNL RDKLWLDVPD LGGGSVLGNA 

       190        200        210        220        230        240 
VERGVGYTPY GDHWMMHSGM EVVLANGELL RTGMGALPDP KRPETMGLKP EDQPWSKIAH 

       250        260        270        280        290        300 
LFPYGFGPYI DGLFSQSNMG IVTKIGIWLM PNPRGYQSYL ITLPKDGDLK QAVDIIRPLR 

       310        320        330        340        350        360 
LGMALQNVPT IRHILLDAAV LGDKRSYSSR TEPLSDEELD KIAKQLNLGR WNFYGALYGP 

       370        380        390        400        410        420 
EPIRRVLWET IKDAFSAIPG VKFYFPEDTP ENSVLRVRDK TMQGIPTYDE LKWIDWLPNG 

       430        440        450        460        470        480 
AHLFFSPIAK VSGEDAMMQY AVTKKRCQEA GLDFIGTFTV GMREMHHIVC IVFNKKDLIQ 

       490        500        510        520        530        540 
KRKVQWLMRT LIDDCAANGW GEYRTHLAFM DQIMETYNWN NSSFLRFNEV LKNAVDPNGI 

       550        560 
IAPGKSGVWP SQYSHVTWKL 

« Hide

References

[1]"Molecular cloning, sequencing, and heterologous expression of the vaoA gene from Penicillium simplicissimum CBS 170.90 encoding vanillyl-alcohol oxidase."
Benen J.A.E., Sanchez-Torres P., Wagemaker M.J.M., Fraaije M.W., van Berkel W.J.H., Visser J.
J. Biol. Chem. 273:7865-7872(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 6-30 AND 130-148.
Strain: ATCC 90172 / CBS 170.90 / PAZ 1.
[2]"Crystallization and preliminary X-ray analysis of the flavoenzyme vanillyl-alcohol oxidase from Penicillium simplicissimum."
Mattevi A., Fraaije M.W., Coda A., van Berkel W.J.H.
Proteins 27:601-603(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Strain: ATCC 90172 / CBS 170.90 / PAZ 1.
[3]"Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase."
Fraaije M.W., van den Heuvel R.H.H., van Berkel W.J.H., Mattevi A.
J. Biol. Chem. 274:35514-35520(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANTS.
Strain: ATCC 90172 / CBS 170.90 / PAZ 1.
[4]"Asp-170 is crucial for the redox properties of vanillyl-alcohol oxidase."
van den Heuvel R.H.H., Fraaije M.W., Mattevi A., van Berkel W.J.H.
J. Biol. Chem. 275:14799-14808(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF D170S MUTANT.
[5]"Inversion of stereospecificity of vanillyl-alcohol oxidase."
van den Heuvel R.H.H., Fraaije M.W., Ferrer M., Mattevi A., van Berkel W.J.H.
Proc. Natl. Acad. Sci. U.S.A. 97:9455-9460(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF D170S/T457E MUTANT.
[6]"Structural analysis of flavinylation in vanillyl-alcohol oxidase."
Fraaije M.W., van den Heuvel R.H.H., van Berkel W.J.H., Mattevi A.
J. Biol. Chem. 275:38654-38658(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANTS.
Strain: ATCC 90172 / CBS 170.90 / PAZ 1.
[7]"Subcellular localization of vanillyl-alcohol oxidase in Penicillium simplicissimum."
Fraaije M.W., Sjollema K.A., Veenhuis M., van Berkel W.J.H.
FEBS Lett. 422:65-68(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"Purification and characterization of vanillyl-alcohol oxidase from Penicillium simplicissimum. A novel aromatic alcohol oxidase containing covalently bound FAD."
de Jong E., van Berkel W.J.H., van der Zwan R.P., de Bont J.A.M.
Eur. J. Biochem. 208:651-657(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: ATCC 90172 / CBS 170.90 / PAZ 1.
[9]"Substrate specificity of flavin-dependent vanillyl-alcohol oxidase from Penicillium simplicissimum. Evidence for the production of 4-hydroxycinnamyl alcohols from 4-allylphenols."
Fraaije M.W., Veeger C., van Berkel W.J.H.
Eur. J. Biochem. 234:271-277(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBSTRATE SPECIFICITY.
Strain: ATCC 90172 / CBS 170.90 / PAZ 1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y15627 Genomic DNA. Translation: CAA75722.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AHUX-ray2.70A/B1-560[»]
1AHVX-ray3.10A/B1-560[»]
1AHZX-ray3.30A/B1-560[»]
1DZNX-ray2.80A/B1-560[»]
1E0YX-ray2.75A/B1-560[»]
1E8FX-ray2.90A/B1-560[»]
1E8GX-ray2.10A/B1-560[»]
1E8HX-ray2.60A/B1-560[»]
1QLTX-ray2.20A/B1-560[»]
1QLUX-ray2.40A/B1-560[»]
1VAOX-ray2.50A/B1-560[»]
1W1JX-ray2.70A/B1-560[»]
1W1KX-ray2.55A/B1-560[»]
1W1LX-ray2.70A/B1-560[»]
1W1MX-ray3.00A/B1-560[»]
2VAOX-ray2.80A/B1-560[»]
ProteinModelPortalP56216.
SMRP56216. Positions 6-560.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17583.
SABIO-RKP56216.

Family and domain databases

Gene3D1.10.45.10. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.40.462.10. 1 hit.
InterProIPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR004113. FAD-linked_oxidase_C.
IPR006094. Oxid_FAD_bind_N.
IPR016170. V_Alc_oxidase/Cytok_DH_C_dom.
IPR016171. Vanillyl_alc_oxidase_C-sub2.
[Graphical view]
PfamPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMSSF55103. SSF55103. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP56216.

Entry information

Entry nameVAOX_PENSI
AccessionPrimary (citable) accession number: P56216
Secondary accession number(s): O60049
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: November 13, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references