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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. flavin adenine dinucleotide binding Source: InterPro
  2. UDP-N-acetylmuramate dehydrogenase activity 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 1 Publication. Cytoplasm 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 560560Vanillyl-alcohol oxidasePRO_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

1
560
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 3215Combined sources
Helixi34 – 363Combined sources
Beta strandi37 – 393Combined sources
Helixi43 – 453Combined sources
Beta strandi51 – 544Combined sources
Beta strandi56 – 583Combined sources
Beta strandi68 – 703Combined sources
Beta strandi72 – 754Combined sources
Helixi80 – 9314Combined sources
Beta strandi97 – 1026Combined sources
Turni106 – 1116Combined sources
Beta strandi119 – 1224Combined sources
Turni124 – 1263Combined sources
Beta strandi130 – 1345Combined sources
Turni135 – 1384Combined sources
Beta strandi139 – 1424Combined sources
Helixi148 – 15710Combined sources
Turni161 – 1633Combined sources
Beta strandi170 – 1723Combined sources
Helixi176 – 1816Combined sources
Helixi189 – 1913Combined sources
Helixi194 – 1963Combined sources
Beta strandi197 – 2048Combined sources
Beta strandi209 – 2113Combined sources
Helixi213 – 2164Combined sources
Helixi223 – 2253Combined sources
Helixi230 – 2323Combined sources
Turni237 – 2415Combined sources
Beta strandi246 – 2483Combined sources
Helixi251 – 2544Combined sources
Beta strandi255 – 26814Combined sources
Beta strandi276 – 2838Combined sources
Helixi286 – 2883Combined sources
Helixi289 – 30113Combined sources
Beta strandi310 – 3134Combined sources
Helixi314 – 3218Combined sources
Helixi324 – 3263Combined sources
Helixi336 – 34611Combined sources
Beta strandi350 – 35910Combined sources
Helixi361 – 37515Combined sources
Beta strandi382 – 3843Combined sources
Helixi386 – 3883Combined sources
Helixi394 – 4018Combined sources
Turni402 – 4043Combined sources
Helixi409 – 4168Combined sources
Beta strandi417 – 4193Combined sources
Beta strandi420 – 4256Combined sources
Beta strandi427 – 4293Combined sources
Helixi433 – 45018Combined sources
Beta strandi456 – 4605Combined sources
Beta strandi465 – 47410Combined sources
Helixi478 – 49720Combined sources
Beta strandi502 – 5043Combined sources
Helixi507 – 5093Combined sources
Helixi510 – 5167Combined sources
Helixi519 – 53517Combined sources
Helixi545 – 5473Combined sources
Helixi555 – 5584Combined sources

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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56216.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini67 – 272206FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation
To bacterial flavocytochrome p-cresol methyl hydroxylase.Curated

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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKTQEFRPL TLPPKLSLSD FNEFIQDIIR IVGSENVEVI SSKDQIVDGS
60 70 80 90 100
YMKPTHTHDP HHVMDQDYFL ASAIVAPRNV ADVQSIVGLA NKFSFPLWPI
110 120 130 140 150
SIGRNSGYGG AAPRVSGSVV LDMGKNMNRV LEVNVEGAYC VVEPGVTYHD
160 170 180 190 200
LHNYLEANNL RDKLWLDVPD LGGGSVLGNA VERGVGYTPY GDHWMMHSGM
210 220 230 240 250
EVVLANGELL RTGMGALPDP KRPETMGLKP EDQPWSKIAH LFPYGFGPYI
260 270 280 290 300
DGLFSQSNMG IVTKIGIWLM PNPRGYQSYL ITLPKDGDLK QAVDIIRPLR
310 320 330 340 350
LGMALQNVPT IRHILLDAAV LGDKRSYSSR TEPLSDEELD KIAKQLNLGR
360 370 380 390 400
WNFYGALYGP EPIRRVLWET IKDAFSAIPG VKFYFPEDTP ENSVLRVRDK
410 420 430 440 450
TMQGIPTYDE LKWIDWLPNG AHLFFSPIAK VSGEDAMMQY AVTKKRCQEA
460 470 480 490 500
GLDFIGTFTV GMREMHHIVC IVFNKKDLIQ KRKVQWLMRT LIDDCAANGW
510 520 530 540 550
GEYRTHLAFM DQIMETYNWN NSSFLRFNEV LKNAVDPNGI IAPGKSGVWP
560
SQYSHVTWKL
Length:560
Mass (Da):63,035
Last modified:July 15, 1998 - v1
Checksum:iC3B4E4A966C1BCEE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti274 – 2741R → G in CAA75722. (PubMed:9525880)Curated
Sequence conflicti330 – 3301R → K in CAA75722. (PubMed:9525880)Curated

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: October 29, 2014
This is version 88 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