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 24-JAN-2024, entry version 126. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 KEGG; ag:CAA75722; -. DR BioCyc; MetaCyc:MONOMER-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; 3.30.465.10; -; 1. DR Gene3D; 3.40.462.10; FAD-linked oxidases, C-terminal domain; 1. DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1. DR InterPro; IPR016170; Cytok_DH_C_sf. DR InterPro; IPR004113; FAD-bd_oxidored_4_C. 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; IPR006094; Oxid_FAD_bind_N. DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2. DR PANTHER; PTHR11748:SF114; ARYL-ALCOHOL OXIDASE VANILLYL-ALCOHOL OXIDASE (AFU_ORTHOLOGUE AFUA_3G09500)-RELATED; 1. DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1. DR Pfam; PF02913; FAD-oxidase_C; 1. DR Pfam; PF01565; FAD_binding_4; 1. DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1. DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 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 //