VAOX_PENSI
ID VAOX_PENSI Reviewed; 560 AA.
AC P56216; O60049;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Vanillyl-alcohol oxidase;
DE EC=1.1.3.38;
DE AltName: Full=4-allylphenol oxidase;
DE AltName: Full=Aryl-alcohol oxidase;
GN Name=VAOA;
OS Penicillium simplicissimum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=69488;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 6-30 AND
RP 130-148.
RC STRAIN=ATCC 90172 / CBS 170.90 / PAZ 1;
RX PubMed=9525880; DOI=10.1074/jbc.273.14.7865;
RA Benen J.A.E., Sanchez-Torres P., Wagemaker M.J.M., Fraaije M.W.,
RA van Berkel W.J.H., Visser J.;
RT "Molecular cloning, sequencing, and heterologous expression of the vaoA
RT gene from Penicillium simplicissimum CBS 170.90 encoding vanillyl-alcohol
RT oxidase.";
RL J. Biol. Chem. 273:7865-7872(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RC STRAIN=ATCC 90172 / CBS 170.90 / PAZ 1;
RX PubMed=9141139;
RX DOI=10.1002/(sici)1097-0134(199704)27:4<601::aid-prot12>3.0.co;2-o;
RA Mattevi A., Fraaije M.W., Coda A., van Berkel W.J.H.;
RT "Crystallization and preliminary X-ray analysis of the flavoenzyme
RT vanillyl-alcohol oxidase from Penicillium simplicissimum.";
RL Proteins 27:601-603(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANTS.
RC STRAIN=ATCC 90172 / CBS 170.90 / PAZ 1;
RX PubMed=10585424; DOI=10.1074/jbc.274.50.35514;
RA Fraaije M.W., van den Heuvel R.H.H., van Berkel W.J.H., Mattevi A.;
RT "Covalent flavinylation is essential for efficient redox catalysis in
RT vanillyl-alcohol oxidase.";
RL J. Biol. Chem. 274:35514-35520(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF D170S MUTANT.
RX PubMed=10809721; DOI=10.1074/jbc.275.20.14799;
RA van den Heuvel R.H.H., Fraaije M.W., Mattevi A., van Berkel W.J.H.;
RT "Asp-170 is crucial for the redox properties of vanillyl-alcohol oxidase.";
RL J. Biol. Chem. 275:14799-14808(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF D170S/T457E MUTANT.
RX PubMed=10920192; DOI=10.1073/pnas.160175897;
RA van den Heuvel R.H.H., Fraaije M.W., Ferrer M., Mattevi A.,
RA van Berkel W.J.H.;
RT "Inversion of stereospecificity of vanillyl-alcohol oxidase.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9455-9460(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANTS.
RC STRAIN=ATCC 90172 / CBS 170.90 / PAZ 1;
RX PubMed=10984479; DOI=10.1074/jbc.m004753200;
RA Fraaije M.W., van den Heuvel R.H.H., van Berkel W.J.H., Mattevi A.;
RT "Structural analysis of flavinylation in vanillyl-alcohol oxidase.";
RL J. Biol. Chem. 275:38654-38658(2000).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=9475171; DOI=10.1016/s0014-5793(97)01605-0;
RA Fraaije M.W., Sjollema K.A., Veenhuis M., van Berkel W.J.H.;
RT "Subcellular localization of vanillyl-alcohol oxidase in Penicillium
RT simplicissimum.";
RL FEBS Lett. 422:65-68(1998).
RN [8]
RP CHARACTERIZATION.
RC STRAIN=ATCC 90172 / CBS 170.90 / PAZ 1;
RX PubMed=1396672; DOI=10.1111/j.1432-1033.1992.tb17231.x;
RA de Jong E., van Berkel W.J.H., van der Zwan R.P., de Bont J.A.M.;
RT "Purification and characterization of vanillyl-alcohol oxidase from
RT Penicillium simplicissimum. A novel aromatic alcohol oxidase containing
RT covalently bound FAD.";
RL Eur. J. Biochem. 208:651-657(1992).
RN [9]
RP SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 90172 / CBS 170.90 / PAZ 1;
RX PubMed=8529652; DOI=10.1111/j.1432-1033.1995.271_c.x;
RA Fraaije M.W., Veeger C., van Berkel W.J.H.;
RT "Substrate specificity of flavin-dependent vanillyl-alcohol oxidase from
RT Penicillium simplicissimum. Evidence for the production of 4-
RT hydroxycinnamyl alcohols from 4-allylphenols.";
RL Eur. J. Biochem. 234:271-277(1995).
CC -!- FUNCTION: Catalyzes the conversion of vanillin alcohol to vanillin, and
CC also the conversion of a wide range of phenolic compounds bearing side
CC chains of variable size at the para position of the aromatic ring.
CC Crucial for the degradation of the secondary metabolites derived from
CC the degradation of the lignin. Catalyzes besides the oxidation of 4-
CC hydroxybenzyl alcohols, the oxidative deamination of 4-
CC hydroxybenzylamines, the oxidative demethylation of 4-(methoxy-
CC methyl)phenols and the oxidative hydration of 4-allylphenols. Most
CC active with 4-allylphenols.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxy-3-methoxy-benzenemethanol + O2 = H2O2 + vanillin;
CC Xref=Rhea:RHEA:10036, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:18346, ChEBI:CHEBI:18353; EC=1.1.3.38;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD covalently per subunit.;
CC -!- ACTIVITY REGULATION: Competitively inhibited by cinnamyl and coniferyl
CC alcohols and by isoeugenol.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is about 10.;
CC Temperature dependence:
CC Optimum temperature is 38 degrees Celsius.;
CC -!- SUBUNIT: Homooctamer (tetramer of tightly interacting dimers).
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:9475171}.
CC Cytoplasm {ECO:0000269|PubMed:9475171}.
CC -!- INDUCTION: By 4-methoxybenzyl alcohols, anisyl and veratryl alcohols.
CC Repressed by carbon catabolite.
CC -!- SIMILARITY: To bacterial flavocytochrome p-cresol methyl hydroxylase.
CC {ECO:0000305}.
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DR EMBL; Y15627; CAA75722.1; -; Genomic_DNA.
DR PDB; 1AHU; X-ray; 2.70 A; A/B=1-560.
DR PDB; 1AHV; X-ray; 3.10 A; A/B=1-560.
DR PDB; 1AHZ; X-ray; 3.30 A; A/B=1-560.
DR PDB; 1DZN; X-ray; 2.80 A; A/B=1-560.
DR PDB; 1E0Y; X-ray; 2.75 A; A/B=1-560.
DR PDB; 1E8F; X-ray; 2.90 A; A/B=1-560.
DR PDB; 1E8G; X-ray; 2.10 A; A/B=1-560.
DR PDB; 1E8H; X-ray; 2.60 A; A/B=1-560.
DR PDB; 1QLT; X-ray; 2.20 A; A/B=1-560.
DR PDB; 1QLU; X-ray; 2.40 A; A/B=1-560.
DR PDB; 1VAO; X-ray; 2.50 A; A/B=1-560.
DR PDB; 1W1J; X-ray; 2.70 A; A/B=1-560.
DR PDB; 1W1K; X-ray; 2.55 A; A/B=1-560.
DR PDB; 1W1L; X-ray; 2.70 A; A/B=1-560.
DR PDB; 1W1M; X-ray; 3.00 A; A/B=1-560.
DR PDB; 2VAO; X-ray; 2.80 A; A/B=1-560.
DR PDB; 5MXJ; X-ray; 2.80 A; A/B=1-560.
DR PDB; 5MXU; X-ray; 2.80 A; A/B=1-560.
DR PDBsum; 1AHU; -.
DR PDBsum; 1AHV; -.
DR PDBsum; 1AHZ; -.
DR PDBsum; 1DZN; -.
DR PDBsum; 1E0Y; -.
DR PDBsum; 1E8F; -.
DR PDBsum; 1E8G; -.
DR PDBsum; 1E8H; -.
DR PDBsum; 1QLT; -.
DR PDBsum; 1QLU; -.
DR PDBsum; 1VAO; -.
DR PDBsum; 1W1J; -.
DR PDBsum; 1W1K; -.
DR PDBsum; 1W1L; -.
DR PDBsum; 1W1M; -.
DR PDBsum; 2VAO; -.
DR PDBsum; 5MXJ; -.
DR PDBsum; 5MXU; -.
DR AlphaFoldDB; P56216; -.
DR SMR; P56216; -.
DR CAZy; AA4; Auxiliary Activities 4.
DR PRIDE; P56216; -.
DR KEGG; ag:CAA75722; -.
DR BioCyc; MetaCyc:MON-17583; -.
DR BRENDA; 1.1.3.38; 4640.
DR SABIO-RK; P56216; -.
DR EvolutionaryTrace; P56216; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0018465; F:vanillyl-alcohol oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0015945; P:methanol metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.45.10; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.10; -; 1.
DR InterPro; IPR016170; Cytok_DH_C_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR004113; FAD-linked_oxidase_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF55103; SSF55103; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein;
KW Methanol utilization; Oxidoreductase; Peroxisome.
FT CHAIN 1..560
FT /note="Vanillyl-alcohol oxidase"
FT /id="PRO_0000065763"
FT DOMAIN 67..272
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT ACT_SITE 108
FT ACT_SITE 503
FT ACT_SITE 504
FT SITE 170
FT /note="Important for the catalytic mechanism; Involved in
FT substrate deprotonation"
FT MOD_RES 422
FT /note="Tele-8alpha-FAD histidine"
FT CONFLICT 274
FT /note="R -> G (in Ref. 1; CAA75722)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="R -> K (in Ref. 1; CAA75722)"
FT /evidence="ECO:0000305"
FT HELIX 18..32
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1AHU"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1QLU"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 80..93
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:1E8G"
FT TURN 106..111
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:1E8G"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:1E8G"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:1E8G"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1QLT"
FT HELIX 176..181
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:2VAO"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:1E8G"
FT TURN 237..241
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:1VAO"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 255..268
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 289..301
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 314..321
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 336..346
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 350..359
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 361..375
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 394..401
FT /evidence="ECO:0007829|PDB:1E8G"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 409..416
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:1AHV"
FT STRAND 420..425
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 433..450
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 465..474
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 478..497
FT /evidence="ECO:0007829|PDB:1E8G"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:1QLU"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 510..516
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 519..535
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:1E8G"
FT HELIX 555..558
FT /evidence="ECO:0007829|PDB:1E8G"
SQ SEQUENCE 560 AA; 63035 MW; C3B4E4A966C1BCEE CRC64;
MSKTQEFRPL TLPPKLSLSD FNEFIQDIIR IVGSENVEVI SSKDQIVDGS YMKPTHTHDP
HHVMDQDYFL ASAIVAPRNV ADVQSIVGLA NKFSFPLWPI SIGRNSGYGG AAPRVSGSVV
LDMGKNMNRV LEVNVEGAYC VVEPGVTYHD LHNYLEANNL RDKLWLDVPD LGGGSVLGNA
VERGVGYTPY GDHWMMHSGM EVVLANGELL RTGMGALPDP KRPETMGLKP EDQPWSKIAH
LFPYGFGPYI DGLFSQSNMG IVTKIGIWLM PNPRGYQSYL ITLPKDGDLK QAVDIIRPLR
LGMALQNVPT IRHILLDAAV LGDKRSYSSR TEPLSDEELD KIAKQLNLGR WNFYGALYGP
EPIRRVLWET IKDAFSAIPG VKFYFPEDTP ENSVLRVRDK TMQGIPTYDE LKWIDWLPNG
AHLFFSPIAK VSGEDAMMQY AVTKKRCQEA GLDFIGTFTV GMREMHHIVC IVFNKKDLIQ
KRKVQWLMRT LIDDCAANGW GEYRTHLAFM DQIMETYNWN NSSFLRFNEV LKNAVDPNGI
IAPGKSGVWP SQYSHVTWKL
