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P56216

- VAOX_PENSI

UniProt

P56216 - VAOX_PENSI

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Protein
Vanillyl-alcohol oxidase
Gene
VAOA
Organism
Penicillium simplicissimum
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

Vanillyl alcohol + O2 = vanillin + H2O2.

Cofactori

Binds 1 FAD covalently per subunit.

Enzyme regulationi

Competitively inhibited by cinnamyl and coniferyl alcohols and by isoeugenol.

pH dependencei

Optimum pH is about 10.

Temperature dependencei

Optimum temperature is 38 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei108 – 1081
Sitei170 – 1701Important for the catalytic mechanism; Involved in substrate deprotonation
Active sitei503 – 5031
Active sitei504 – 5041

GO - Molecular functioni

  1. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro
  2. flavin adenine dinucleotide binding Source: InterPro
  3. vanillyl-alcohol oxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. methanol metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Methanol utilization

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17583.
SABIO-RKP56216.

Names & Taxonomyi

Protein namesi
Recommended name:
Vanillyl-alcohol oxidase (EC:1.1.3.38)
Alternative name(s):
4-allylphenol oxidase
Aryl-alcohol oxidase
Gene namesi
Name:VAOA
OrganismiPenicillium simplicissimum
Taxonomic identifieri69488 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

Subcellular locationi

Peroxisome. Cytoplasm 1 Publication

GO - Cellular componenti

  1. peroxisome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 560560Vanillyl-alcohol oxidase
PRO_0000065763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei422 – 4221Tele-8alpha-FAD histidine

Expressioni

Inductioni

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

Interactioni

Subunit structurei

Homooctamer (tetramer of tightly interacting dimers).

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 3215
Helixi34 – 363
Beta strandi37 – 393
Helixi43 – 453
Beta strandi51 – 544
Beta strandi56 – 583
Beta strandi68 – 703
Beta strandi72 – 754
Helixi80 – 9314
Beta strandi97 – 1026
Turni106 – 1116
Beta strandi119 – 1224
Turni124 – 1263
Beta strandi130 – 1345
Turni135 – 1384
Beta strandi139 – 1424
Helixi148 – 15710
Turni161 – 1633
Beta strandi170 – 1723
Helixi176 – 1816
Helixi189 – 1913
Helixi194 – 1963
Beta strandi197 – 2048
Beta strandi209 – 2113
Helixi213 – 2164
Helixi223 – 2253
Helixi230 – 2323
Turni237 – 2415
Beta strandi246 – 2483
Helixi251 – 2544
Beta strandi255 – 26814
Beta strandi276 – 2838
Helixi286 – 2883
Helixi289 – 30113
Beta strandi310 – 3134
Helixi314 – 3218
Helixi324 – 3263
Helixi336 – 34611
Beta strandi350 – 35910
Helixi361 – 37515
Beta strandi382 – 3843
Helixi386 – 3883
Helixi394 – 4018
Turni402 – 4043
Helixi409 – 4168
Beta strandi417 – 4193
Beta strandi420 – 4256
Beta strandi427 – 4293
Helixi433 – 45018
Beta strandi456 – 4605
Beta strandi465 – 47410
Helixi478 – 49720
Beta strandi502 – 5043
Helixi507 – 5093
Helixi510 – 5167
Helixi519 – 53517
Helixi545 – 5473
Helixi555 – 5584

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP56216.
SMRiP56216. Positions 6-560.

Miscellaneous databases

EvolutionaryTraceiP56216.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini67 – 272206FAD-binding PCMH-type
Add
BLAST

Sequence similaritiesi

To bacterial flavocytochrome p-cresol methyl hydroxylase.

Family and domain databases

Gene3Di1.10.45.10. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.40.462.10. 1 hit.
InterProiIPR016169. 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]
PfamiPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF55103. SSF55103. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P56216-1 [UniParc]FASTAAdd to Basket

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MSKTQEFRPL TLPPKLSLSD FNEFIQDIIR IVGSENVEVI SSKDQIVDGS    50
YMKPTHTHDP HHVMDQDYFL ASAIVAPRNV ADVQSIVGLA NKFSFPLWPI 100
SIGRNSGYGG AAPRVSGSVV LDMGKNMNRV LEVNVEGAYC VVEPGVTYHD 150
LHNYLEANNL RDKLWLDVPD LGGGSVLGNA VERGVGYTPY GDHWMMHSGM 200
EVVLANGELL RTGMGALPDP KRPETMGLKP EDQPWSKIAH LFPYGFGPYI 250
DGLFSQSNMG IVTKIGIWLM PNPRGYQSYL ITLPKDGDLK QAVDIIRPLR 300
LGMALQNVPT IRHILLDAAV LGDKRSYSSR TEPLSDEELD KIAKQLNLGR 350
WNFYGALYGP EPIRRVLWET IKDAFSAIPG VKFYFPEDTP ENSVLRVRDK 400
TMQGIPTYDE LKWIDWLPNG AHLFFSPIAK VSGEDAMMQY AVTKKRCQEA 450
GLDFIGTFTV GMREMHHIVC IVFNKKDLIQ KRKVQWLMRT LIDDCAANGW 500
GEYRTHLAFM DQIMETYNWN NSSFLRFNEV LKNAVDPNGI IAPGKSGVWP 550
SQYSHVTWKL 560
Length:560
Mass (Da):63,035
Last modified:July 15, 1998 - v1
Checksum:iC3B4E4A966C1BCEE
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti274 – 2741R → G in CAA75722. 1 Publication
Sequence conflicti330 – 3301R → K in CAA75722. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y15627 Genomic DNA. Translation: CAA75722.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y15627 Genomic DNA. Translation: CAA75722.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P56216.
SMRi P56216. Positions 6-560.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-17583.
SABIO-RK P56216.

Miscellaneous databases

EvolutionaryTracei P56216.

Family and domain databases

Gene3Di 1.10.45.10. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.40.462.10. 1 hit.
InterProi 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 ]
Pfami PF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view ]
SUPFAMi SSF55103. SSF55103. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEi PS51387. FAD_PCMH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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.

Entry informationi

Entry nameiVAOX_PENSI
AccessioniPrimary (citable) accession number: P56216
Secondary accession number(s): O60049
Entry historyi
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 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

External Data

Dasty 3

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