PAAS_PETHY
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 03-AUG-2022, entry version 58.
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: Higly 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:MON-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:cellular amino acid metabolic process; IEA:InterPro.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; SSF53383; 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
