Vanillyl-alcohol oxidase - Penicillium simplicissimum

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P56216 (VAOX_PENSI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 84. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Vanillyl-alcohol oxidase
EC=1.1.3.38

Alternative name(s):
4-allylphenol oxidase
Aryl-alcohol oxidase

Gene names

Name:

VAOA

Organism

Penicillium simplicissimum

Taxonomic identifier

69488 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Penicillium

Protein attributes

Sequence length	560 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Methanol utilization
Cellular component	Cytoplasm Peroxisome
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	methanol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	UDP-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: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 560

560

Vanillyl-alcohol oxidase

PRO_0000065763

Regions

Domain

67 – 272

206

FAD-binding PCMH-type

Sites

Active site

Active site

Active site

Site

Important for the catalytic mechanism; Involved in substrate deprotonation

Amino acid modifications

Modified residue

422

Tele-8alpha-FAD histidine

Experimental info

Sequence conflict

274

R → G in CAA75722. Ref.1

Sequence conflict

330

R → K in CAA75722. Ref.1

Secondary structure

560

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P56216 [UniParc].

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

FASTA

560

63,035

        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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AHU	X-ray	2.70	A/B	1-560	[»]
1AHV	X-ray	3.10	A/B	1-560	[»]
1AHZ	X-ray	3.30	A/B	1-560	[»]
1DZN	X-ray	2.80	A/B	1-560	[»]
1E0Y	X-ray	2.75	A/B	1-560	[»]
1E8F	X-ray	2.90	A/B	1-560	[»]
1E8G	X-ray	2.10	A/B	1-560	[»]
1E8H	X-ray	2.60	A/B	1-560	[»]
1QLT	X-ray	2.20	A/B	1-560	[»]
1QLU	X-ray	2.40	A/B	1-560	[»]
1VAO	X-ray	2.50	A/B	1-560	[»]
1W1J	X-ray	2.70	A/B	1-560	[»]
1W1K	X-ray	2.55	A/B	1-560	[»]
1W1L	X-ray	2.70	A/B	1-560	[»]
1W1M	X-ray	3.00	A/B	1-560	[»]
2VAO	X-ray	2.80	A/B	1-560	[»]

ProteinModelPortal

P56216.

SMR

P56216. Positions 6-560.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-17583.

SABIO-RK

P56216.

Family and domain databases

Gene3D

1.10.45.10. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.40.462.10. 1 hit.

InterPro

IPR016169. 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]

Pfam

PF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]

SUPFAM

SSF55103. FAD-binding_2. 1 hit.
SSF56176. FAD-binding_2. 1 hit.

PROSITE

PS51387. FAD_PCMH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P56216.

Entry information

Entry name

VAOX_PENSI

Accession

Primary (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:	April 3, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents