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Protein

Vanillyl-alcohol oxidase

Gene

VAOA

Organism
Penicillium simplicissimum
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FADNote: Binds 1 FAD covalently per subunit.

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Competitively inhibited by cinnamyl and coniferyl alcohols and by isoeugenol.

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Optimum pH is about 10.

Temperature dependencei

Optimum temperature is 38 degrees Celsius.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1081
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei170Important for the catalytic mechanism; Involved in substrate deprotonation1
Active sitei5031
Active sitei5041

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processMethanol utilization
LigandFAD, Flavoprotein

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-17583

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.3.38 4640

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P56216

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
AA4 Auxiliary Activities 4

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Vanillyl-alcohol oxidase (EC:1.1.3.38)
Alternative name(s):
4-allylphenol oxidase
Aryl-alcohol oxidase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:VAOA
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPenicillium simplicissimum
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri69488 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Peroxisome

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000657631 – 560Vanillyl-alcohol oxidaseAdd BLAST560

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei422Tele-8alpha-FAD histidine1

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P56216

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homooctamer (tetramer of tightly interacting dimers).

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1560
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P56216

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P56216

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P56216

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini67 – 272FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST206

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

To bacterial flavocytochrome p-cresol methyl hydroxylase.Curated

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K20153

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
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

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016170 Cytok_DH_C_sf
IPR016166 FAD-bd_PCMH
IPR036318 FAD-bd_PCMH-like_sf
IPR016167 FAD-bd_PCMH_sub1
IPR016169 FAD-bd_PCMH_sub2
IPR016164 FAD-linked_Oxase-like_C
IPR004113 FAD-linked_oxidase_C
IPR006094 Oxid_FAD_bind_N
IPR016171 Vanillyl_alc_oxidase_C-sub2

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02913 FAD-oxidase_C, 1 hit
PF01565 FAD_binding_4, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF55103 SSF55103, 1 hit
SSF56176 SSF56176, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51387 FAD_PCMH, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC3B4E4A966C1BCEE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti274R → G in CAA75722 (PubMed:9525880).Curated1
Sequence conflicti330R → K in CAA75722 (PubMed:9525880).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Y15627 Genomic DNA Translation: CAA75722.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:CAA75722

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]
5MXJX-ray2.80A/B1-560[»]
5MXUX-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-RKiP56216

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
InterProiView protein in InterPro
IPR016170 Cytok_DH_C_sf
IPR016166 FAD-bd_PCMH
IPR036318 FAD-bd_PCMH-like_sf
IPR016167 FAD-bd_PCMH_sub1
IPR016169 FAD-bd_PCMH_sub2
IPR016164 FAD-linked_Oxase-like_C
IPR004113 FAD-linked_oxidase_C
IPR006094 Oxid_FAD_bind_N
IPR016171 Vanillyl_alc_oxidase_C-sub2
PfamiView protein in Pfam
PF02913 FAD-oxidase_C, 1 hit
PF01565 FAD_binding_4, 1 hit
SUPFAMiSSF55103 SSF55103, 1 hit
SSF56176 SSF56176, 1 hit
PROSITEiView protein in PROSITE
PS51387 FAD_PCMH, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiVAOX_PENSI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P56216
Secondary accession number(s): O60049
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: December 5, 2018
This is version 108 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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