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Protein

Vanillyl-alcohol oxidase

Gene

VAOA

Organism
Penicillium simplicissimum
Status
Reviewed-Annotation score: 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

FADNote: 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)DescriptionActionsGraphical viewLength
Active sitei1081
Sitei170Important for the catalytic mechanism; Involved in substrate deprotonation1
Active sitei5031
Active sitei5041

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Methanol utilization

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17583.
BRENDAi1.1.3.38. 4640.
SABIO-RKP56216.

Protein family/group databases

CAZyiAA4. Auxiliary Activities 4.

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000657631 – 560Vanillyl-alcohol oxidaseAdd BLAST560

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei422Tele-8alpha-FAD histidine1

Proteomic databases

PRIDEiP56216.

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

1560
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi18 – 32Combined sources15
Helixi34 – 36Combined sources3
Beta strandi37 – 39Combined sources3
Helixi43 – 45Combined sources3
Beta strandi51 – 54Combined sources4
Beta strandi56 – 58Combined sources3
Beta strandi68 – 70Combined sources3
Beta strandi72 – 75Combined sources4
Helixi80 – 93Combined sources14
Beta strandi97 – 102Combined sources6
Turni106 – 111Combined sources6
Beta strandi119 – 122Combined sources4
Turni124 – 126Combined sources3
Beta strandi130 – 134Combined sources5
Turni135 – 138Combined sources4
Beta strandi139 – 142Combined sources4
Helixi148 – 157Combined sources10
Turni161 – 163Combined sources3
Beta strandi170 – 172Combined sources3
Helixi176 – 181Combined sources6
Helixi189 – 191Combined sources3
Helixi194 – 196Combined sources3
Beta strandi197 – 204Combined sources8
Beta strandi209 – 211Combined sources3
Helixi213 – 216Combined sources4
Helixi223 – 225Combined sources3
Helixi230 – 232Combined sources3
Turni237 – 241Combined sources5
Beta strandi246 – 248Combined sources3
Helixi251 – 254Combined sources4
Beta strandi255 – 268Combined sources14
Beta strandi276 – 283Combined sources8
Helixi286 – 288Combined sources3
Helixi289 – 301Combined sources13
Beta strandi310 – 313Combined sources4
Helixi314 – 321Combined sources8
Helixi324 – 326Combined sources3
Helixi336 – 346Combined sources11
Beta strandi350 – 359Combined sources10
Helixi361 – 375Combined sources15
Beta strandi382 – 384Combined sources3
Helixi386 – 388Combined sources3
Helixi394 – 401Combined sources8
Turni402 – 404Combined sources3
Helixi409 – 416Combined sources8
Beta strandi417 – 419Combined sources3
Beta strandi420 – 425Combined sources6
Beta strandi427 – 429Combined sources3
Helixi433 – 450Combined sources18
Beta strandi456 – 460Combined sources5
Beta strandi465 – 474Combined sources10
Helixi478 – 497Combined sources20
Beta strandi502 – 504Combined sources3
Helixi507 – 509Combined sources3
Helixi510 – 516Combined sources7
Helixi519 – 535Combined sources17
Helixi545 – 547Combined sources3
Helixi555 – 558Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56216.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini67 – 272FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST206

Sequence similaritiesi

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

Phylogenomic databases

KOiK20153.

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

        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)DescriptionActionsGraphical viewLength
Sequence conflicti274R → G in CAA75722 (PubMed:9525880).Curated1
Sequence conflicti330R → K in CAA75722 (PubMed:9525880).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y15627 Genomic DNA. Translation: CAA75722.1.

Genome annotation databases

KEGGiag:CAA75722.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y15627 Genomic DNA. Translation: CAA75722.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA4. Auxiliary Activities 4.

Proteomic databases

PRIDEiP56216.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA75722.

Phylogenomic databases

KOiK20153.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17583.
BRENDAi1.1.3.38. 4640.
SABIO-RKP56216.

Miscellaneous databases

EvolutionaryTraceiP56216.

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]
ProtoNetiSearch...

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 2, 2016
This is version 99 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.