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UniProtKB/Swiss-Prot entry P56216

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name VAOX_PENSI
Primary accession number P56216
Secondary accession number O60049
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on July 15, 1998 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 61)
Name and origin of the protein
Protein name Vanillyl-alcohol oxidase
Synonyms EC 1.1.3.38
Aryl-alcohol oxidase
4-allylphenol oxidase
Gene name
Name: VAOA
From
Penicillium simplicissimum [TaxID: 69488] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; Eurotiomycetidae; Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; Penicillium.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 6-30 AND 130-148.
STRAIN=ATCC 90172 / CBS 170.90 / PAZ 1;
DOI=10.1074/jbc.273.14.7865; PubMed=9525880 [NCBI, ExPASy, EBI, Israel, Japan]
Benen J.A.E., Sanchez-Torres P., Wagemaker M.J.M., Fraaije M.W., van Berkel W.J.H., Visser J.;
"Molecular cloning, sequencing, and heterologous expression of the vaoA gene from Penicillium simplicissimum CBS 170.90 encoding vanillyl-alcohol oxidase.";
J. Biol. Chem. 273:7865-7872(1998).
[2]
 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
STRAIN=ATCC 90172 / CBS 170.90 / PAZ 1;
DOI=10.1002/(SICI)1097-0134(199704)27:4<601::AID-PROT12>3.0.CO;2-O; PubMed=9141139 [NCBI, ExPASy, EBI, Israel, Japan]
Mattevi A., Fraaije M.W., Coda A., van Berkel W.J.H.;
"Crystallization and preliminary X-ray analysis of the flavoenzyme vanillyl-alcohol oxidase from Penicillium simplicissimum.";
Proteins 27:601-603(1997).
[3]
 X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANTS.
STRAIN=ATCC 90172 / CBS 170.90 / PAZ 1;
DOI=10.1074/jbc.274.50.35514; PubMed=10585424 [NCBI, ExPASy, EBI, Israel, Japan]
Fraaije M.W., van den Heuvel R.H.H., van Berkel W.J.H., Mattevi A.;
"Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase.";
J. Biol. Chem. 274:35514-35520(1999).
[4]
 X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF D170S MUTANT.
DOI=10.1074/jbc.275.20.14799; PubMed=10809721 [NCBI, ExPASy, EBI, Israel, Japan]
van den Heuvel R.H.H., Fraaije M.W., Mattevi A., van Berkel W.J.H.;
"Asp-170 is crucial for the redox properties of vanillyl-alcohol oxidase.";
J. Biol. Chem. 275:14799-14808(2000).
[5]
 X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF D170S/T457E MUTANT.
DOI=10.1073/pnas.160175897; PubMed=10920192 [NCBI, ExPASy, EBI, Israel, Japan]
van den Heuvel R.H.H., Fraaije M.W., Ferrer M., Mattevi A., van Berkel W.J.H.;
"Inversion of stereospecificity of vanillyl-alcohol oxidase.";
Proc. Natl. Acad. Sci. U.S.A. 97:9455-9460(2000).
[6]
 X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANTS.
STRAIN=ATCC 90172 / CBS 170.90 / PAZ 1;
DOI=10.1074/jbc.M004753200; PubMed=10984479 [NCBI, ExPASy, EBI, Israel, Japan]
Fraaije M.W., van den Heuvel R.H.H., van Berkel W.J.H., Mattevi A.;
"Structural analysis of flavinylation in vanillyl-alcohol oxidase.";
J. Biol. Chem. 275:38654-38658(2000).
[7]
 SUBCELLULAR LOCATION.
DOI=10.1016/S0014-5793(97)01605-0; PubMed=9475171 [NCBI, ExPASy, EBI, Israel, Japan]
Fraaije M.W., Sjollema K.A., Veenhuis M., van Berkel W.J.H.;
"Subcellular localization of vanillyl-alcohol oxidase in Penicillium simplicissimum.";
FEBS Lett. 422:65-68(1998).
[8]
 CHARACTERIZATION.
STRAIN=ATCC 90172 / CBS 170.90 / PAZ 1;
PubMed=1396672 [NCBI, ExPASy, EBI, Israel, Japan]
de Jong E., van Berkel W.J.H., van der Zwan R.P., de Bont J.A.M.;
"Purification and characterization of vanillyl-alcohol oxidase from Penicillium simplicissimum. A novel aromatic alcohol oxidase containing covalently bound FAD.";
Eur. J. Biochem. 208:651-657(1992).
[9]
 SUBSTRATE SPECIFICITY.
STRAIN=ATCC 90172 / CBS 170.90 / PAZ 1;
PubMed=8529652 [NCBI, ExPASy, EBI, Israel, Japan]
Fraaije M.W., Veeger C., van Berkel W.J.H.;
"Substrate specificity of flavin-dependent vanillyl-alcohol oxidase from Penicillium simplicissimum. Evidence for the production of 4-hydroxycinnamyl alcohols from 4-allylphenols.";
Eur. J. Biochem. 234:271-277(1995).
Comments
  • FUNCTION: 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 ACTIVITY: Vanillyl alcohol + O2 = vanillin + H2O2.
  • COFACTOR: Binds 1 FAD covalently per subunit.
  • ENZYME REGULATION: Competitively inhibited by cinnamyl and coniferyl alcohols and by isoeugenol.
  • BIOPHYSICOCHEMICAL PROPERTIES:
    pH dependence:   Optimum pH is about 10;
    Temperature dependence:   Optimum temperature is 38 degrees Celsius;
  • SUBUNIT: Homooctamer (tetramer of tightly interacting dimers).
  • SUBCELLULAR LOCATION: Peroxisome. Cytoplasm.
  • INDUCTION: By 4-methoxybenzyl alcohols, anisyl and veratryl alcohols. Repressed by carbon catabolite.
  • SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
  • SIMILARITY: To bacterial flavocytochrome p-cresol methyl hydroxylase.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y15627; CAA75722.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
PDB
1AHU; X-ray; 2.70 A; A/B=1-560.[ExPASy / RCSB / EBI]
1AHV; X-ray; 3.10 A; A/B=1-560.[ExPASy / RCSB / EBI]
1AHZ; X-ray; 3.30 A; A/B=1-560.[ExPASy / RCSB / EBI]
1DZN; X-ray; 2.80 A; A/B=1-560.[ExPASy / RCSB / EBI]
1E0Y; X-ray; 2.75 A; A/B=1-560.[ExPASy / RCSB / EBI]
1E8F; X-ray; 2.90 A; A/B=1-560.[ExPASy / RCSB / EBI]
1E8G; X-ray; 2.10 A; A/B=1-560.[ExPASy / RCSB / EBI]
1E8H; X-ray; 2.60 A; A/B=1-560.[ExPASy / RCSB / EBI]
1QLT; X-ray; 2.20 A; A/B=1-560.[ExPASy / RCSB / EBI]
1QLU; X-ray; 2.40 A; A/B=1-560.[ExPASy / RCSB / EBI]
1VAO; X-ray; 2.50 A; A/B=1-560.[ExPASy / RCSB / EBI]
1W1J; X-ray; 2.70 A; A/B=1-560.[ExPASy / RCSB / EBI]
1W1K; X-ray; 2.55 A; A/B=1-560.[ExPASy / RCSB / EBI]
1W1L; X-ray; 2.70 A; A/B=1-560.[ExPASy / RCSB / EBI]
1W1M; X-ray; 3.00 A; A/B=1-560.[ExPASy / RCSB / EBI]
2VAO; X-ray; 2.80 A; A/B=1-560.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AHU; -.
1AHV; -.
1AHZ; -.
1DZN; -.
1E0Y; -.
1E8F; -.
1E8G; -.
1E8H; -.
1QLT; -.
1QLU; -.
1VAO; -.
1W1J; -.
1W1K; -.
1W1L; -.
1W1M; -.
2VAO; -.
ModBase P56216.
Family and domain databases
InterPro IPR016167; FAD-bd_2_sub1.
IPR016168; FAD-linked_Oxase_FAD-bd_sub2.
IPR004113; FAD-linked_oxidase_C.
IPR006094; Oxid_FAD_bind_N.
IPR016170; Vanillyl_alc_oxidase_C-sub1.
IPR016171; Vanillyl_alc_oxidase_C-sub2.
Graphical view of domain structure.
Gene3D G3DSA:3.30.43.10; FAD-binding_2_sub1; 1.
G3DSA:3.30.465.20; FAD-linked_oxidase_FAD-bd_sub2; 1.
G3DSA:3.40.462.10; Vanillyl_alc_oxidase_C-sub1; 1.
G3DSA:1.10.45.10; Vanillyl_alc_oxidase_C-sub2; 1.
Pfam PF02913; FAD-oxidase_C; 1.
PF01565; FAD_binding_4; 1.
Pfam graphical view of domain structure.
PROSITE PS51387; FAD_PCMH; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P56216.
Other
LinkHub P56216; -.
ProtoNet P56216.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Methanol utilization; Oxidoreductase; Peroxisome.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   560  560     Vanillyl-alcohol oxidase. PRO_0000065763
DOMAIN   67   272  206     FAD-binding PCMH-type. 
ACT_SITE   108   108         
ACT_SITE   503   503         
ACT_SITE   504   504         
SITE   170   170  1     Important for the catalytic mechanism; Involved in substrate deprotonation. 
MOD_RES   422   422        Tele-8alpha-FAD histidine. 
CONFLICT   274   274        R -> G (in Ref. 1; CAA75722). 
CONFLICT   330   330        R -> K (in Ref. 1; CAA75722). 
HELIX   18    32  15      
HELIX   34    36  3      
STRAND   37    39  3      
STRAND   51    54  4      
STRAND   56    58  3      
STRAND   72    75  4      
HELIX   80    93  14      
STRAND   97   102  6      
TURN   106   111  6      
STRAND   119   122  4      
TURN   124   126  3      
STRAND   130   134  5      
TURN   135   138  4      
STRAND   139   142  4      
HELIX   148   157  10      
TURN   161   163  3      
HELIX   176   181  6      
HELIX   194   196  3      
STRAND   197   204  8      
STRAND   209   211  3      
HELIX   213   216  4      
HELIX   223   225  3      
HELIX   230   232  3      
TURN   237   241  5      
HELIX   251   254  4      
STRAND   255   268  14      
STRAND   276   283  8      
HELIX   286   288  3      
HELIX   289   301  13      
STRAND   310   313  4      
HELIX   314   321  8      
HELIX   324   326  3      
HELIX   336   346  11      
STRAND   350   359  10      
HELIX   361   375  15      
STRAND   382   384  3      
HELIX   386   388  3      
HELIX   394   401  8      
TURN   402   404  3      
HELIX   409   416  8      
STRAND   420   425  6      
STRAND   427   429  3      
HELIX   433   450  18      
STRAND   456   460  5      
STRAND   465   474  10      
HELIX   478   497  20      
HELIX   507   509  3      
HELIX   510   516  7      
HELIX   519   535  17      
HELIX   545   547  3      
HELIX   555   558  4      
Sequence information
Length: 560 AA [This is the length of the unprocessed precursor] Molecular weight: 63035 Da [This is the MW of the unprocessed precursor] CRC64: C3B4E4A966C1BCEE [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSKTQEFRPL TLPPKLSLSD FNEFIQDIIR IVGSENVEVI SSKDQIVDGS YMKPTHTHDP 

        70         80         90        100        110        120 
HHVMDQDYFL ASAIVAPRNV ADVQSIVGLA NKFSFPLWPI SIGRNSGYGG AAPRVSGSVV 

       130        140        150        160        170        180 
LDMGKNMNRV LEVNVEGAYC VVEPGVTYHD LHNYLEANNL RDKLWLDVPD LGGGSVLGNA 

       190        200        210        220        230        240 
VERGVGYTPY GDHWMMHSGM EVVLANGELL RTGMGALPDP KRPETMGLKP EDQPWSKIAH 

       250        260        270        280        290        300 
LFPYGFGPYI DGLFSQSNMG IVTKIGIWLM PNPRGYQSYL ITLPKDGDLK QAVDIIRPLR 

       310        320        330        340        350        360 
LGMALQNVPT IRHILLDAAV LGDKRSYSSR TEPLSDEELD KIAKQLNLGR WNFYGALYGP 

       370        380        390        400        410        420 
EPIRRVLWET IKDAFSAIPG VKFYFPEDTP ENSVLRVRDK TMQGIPTYDE LKWIDWLPNG 

       430        440        450        460        470        480 
AHLFFSPIAK VSGEDAMMQY AVTKKRCQEA GLDFIGTFTV GMREMHHIVC IVFNKKDLIQ 

       490        500        510        520        530        540 
KRKVQWLMRT LIDDCAANGW GEYRTHLAFM DQIMETYNWN NSSFLRFNEV LKNAVDPNGI 

       550        560 
IAPGKSGVWP SQYSHVTWKL
P56216 in FASTA format

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