ID   PAAS_PETHY              Reviewed;         506 AA.
AC   Q0ZQX0;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Phenylacetaldehyde synthase {ECO:0000303|PubMed:16766535};
DE            Short=PhPAAS {ECO:0000303|PubMed:16766535};
DE            EC=4.1.1.109 {ECO:0000269|PubMed:16766535};
GN   Name=PAAS {ECO:0000303|PubMed:16766535};
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Mitchell;
RX   PubMed=16766535; DOI=10.1074/jbc.m602708200;
RA   Kaminaga Y., Schnepp J., Peel G., Kish C.M., Ben-Nissan G., Weiss D.,
RA   Orlova I., Lavie O., Rhodes D., Wood K., Porterfield D.M., Cooper A.J.,
RA   Schloss J.V., Pichersky E., Vainstein A., Dudareva N.;
RT   "Plant phenylacetaldehyde synthase is a bifunctional homotetrameric enzyme
RT   that catalyzes phenylalanine decarboxylation and oxidation.";
RL   J. Biol. Chem. 281:23357-23366(2006).
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes the decarboxylation of L-
CC       phenylalanine to 2-phenylethylamine, which is then oxidized to form 2-
CC       phenylacetaldehyde, a constituent of floral scent (PubMed:16766535). 2-
CC       phenylacetaldehyde is a precursor of 2-phenylethanol, another
CC       constituent of floral scent (PubMed:16766535).
CC       {ECO:0000269|PubMed:16766535}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + H2O + L-phenylalanine + O2 = 2-phenylacetaldehyde + CO2
CC         + H2O2 + NH4(+); Xref=Rhea:RHEA:55532, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:16424, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58095; EC=4.1.1.109;
CC         Evidence={ECO:0000269|PubMed:16766535};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55533;
CC         Evidence={ECO:0000269|PubMed:16766535};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:16766535};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.18 mM for L-phenylalanine {ECO:0000269|PubMed:16766535};
CC       pH dependence:
CC         Optimum pH is 8.5. {ECO:0000269|PubMed:16766535};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16766535}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in corolla limbs and at lower
CC       levels in corolla tubes and ovaries. {ECO:0000269|PubMed:16766535}.
CC   -!- INDUCTION: Follows a circadian-oscillation with the highest expression
CC       in the middle of the light phase and the lowest expression in the
CC       middle of the dark phase. {ECO:0000269|PubMed:16766535}.
CC   -!- MISCELLANEOUS: Flowers of plants silencing PAAS, neither produce 2-
CC       phenylacetaldehyde nor 2-phenylethanol. {ECO:0000269|PubMed:16766535}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; DQ243784; ABB72475.1; -; mRNA.
DR   AlphaFoldDB; Q0ZQX0; -.
DR   SMR; Q0ZQX0; -.
DR   KEGG; ag:ABB72475; -.
DR   BioCyc; MetaCyc:MONOMER-13645; -.
DR   BRENDA; 4.1.1.109; 4700.
DR   GO; GO:1990055; F:phenylacetaldehyde synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd06450; DOPA_deC_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010977; Aromatic_deC.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR11999:SF156; TYROSINE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   1: Evidence at protein level;
KW   Decarboxylase; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..506
FT                   /note="Phenylacetaldehyde synthase"
FT                   /id="PRO_0000450475"
FT   BINDING         101
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q8RY79"
FT   BINDING         202
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q8RY79"
FT   BINDING         317
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q8RY79"
FT   MOD_RES         318
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000305|PubMed:16766535"
SQ   SEQUENCE   506 AA;  57078 MW;  605547DFA358C870 CRC64;
     MDTIKINPEF DGQFCKTTSL LDPEEFRRNG HMMVDFLADY FHNIEKYPVR SQVEPGYLER
     LLPDSAPIQP EPIEKILKDV RSDIFPGLTH WQSPNFFAYF PCSSSTAGIL GEMLSAGLNV
     VGFSWIASPA ATELESIVMD WLGKLINLPK TYLFSGGGGG VMQGTTCEVM LCTIVAARDK
     MLEKFGRENI DKLVVYASDQ THFSFQKAVK ISGIKPENFR AIPTTKATEF SLNPESLRRA
     IQEDKKAGLI PLFLCTSIGT TSTTAVDPLK PLCEIAEEYG IWVHVDAAYA GSACICPEFQ
     HFLDGVEHAN SFSFNAHKWL FTTLDCCCLW LKDPSSLTKA LSTNPEVLRN DATDSEQVVD
     YKDWQITLSR RFRSLKLWLV LKSYGVANLR NFIRSHIEMA KHFEELVAMD ERFEIMAPRN
     FSLVCFRVSL LALEKKFNFV DETQVNEFNA KLLESIISSG NVYMTHTVVE GVYMIRFAVG
     APLTDYPHID MAWNVVRNHA TMMLNA
//