Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P56216

- VAOX_PENSI

UniProt

P56216 - VAOX_PENSI

Protein

Vanillyl-alcohol oxidase

Gene

VAOA

Organism
Penicillium simplicissimum
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (15 Jul 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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-SubCell

    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 – 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.
    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.

    P56216-1 [UniParc]FASTAAdd to Basket

    « Hide

    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

    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 1, 2014
    This is version 87 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