PAAS_ROSHC
ID PAAS_ROSHC Reviewed; 508 AA.
AC Q0ZS27; A6BM85;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Phenylacetaldehyde synthase {ECO:0000303|PubMed:16766535};
DE Short=RhPAAS {ECO:0000303|PubMed:16766535};
DE EC=4.1.1.109 {ECO:0000269|PubMed:16766535, ECO:0000269|PubMed:17928708};
DE AltName: Full=Aromatic L-amino acid decarboxylase {ECO:0000303|PubMed:17928708};
GN Name=PAAS {ECO:0000303|PubMed:16766535};
GN Synonyms=AADC {ECO:0000303|PubMed:17928708};
OS Rosa hybrid cultivar.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC Rosa.
OX NCBI_TaxID=128735;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC TISSUE=Petal;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=17928708; DOI=10.1271/bbb.70090;
RA Sakai M., Hirata H., Sayama H., Sekiguchi K., Itano H., Asai T., Dohra H.,
RA Hara M., Watanabe N.;
RT "Production of 2-phenylethanol in roses as the dominant floral scent
RT compound from L-phenylalanine by two key enzymes, a PLP-dependent
RT decarboxylase and a phenylacetaldehyde reductase.";
RL Biosci. Biotechnol. Biochem. 71:2408-2419(2007).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the decarboxylation of L-
CC phenylalanine to produce 2-phenylethylamine, which is then oxidized to
CC form 2-phenylacetaldehyde, a constituent of floral scent in petals
CC (PubMed:16766535, PubMed:17928708). 2-phenylacetaldehyde is a precursor
CC of 2-phenylethanol, another constituent of floral scent in petals
CC (PubMed:16766535, PubMed:17928708). {ECO:0000269|PubMed:16766535,
CC ECO:0000269|PubMed:17928708}.
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, ECO:0000269|PubMed:17928708};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55533;
CC Evidence={ECO:0000269|PubMed:16766535, ECO:0000269|PubMed:17928708};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:16766535, ECO:0000269|PubMed:17928708};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q0ZQX0}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; DQ192639; ABB04522.1; -; mRNA.
DR EMBL; AB305071; BAF64844.1; -; mRNA.
DR AlphaFoldDB; Q0ZS27; -.
DR SMR; Q0ZS27; -.
DR BioCyc; MetaCyc:MON-13646; -.
DR BRENDA; 4.1.1.109; 7163.
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 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..508
FT /note="Phenylacetaldehyde synthase"
FT /id="PRO_0000450476"
FT BINDING 203
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q8RY79"
FT BINDING 318
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q8RY79"
FT BINDING 348
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q8RY79"
FT MOD_RES 319
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000305|PubMed:16766535"
FT CONFLICT 65
FT /note="V -> E (in Ref. 2; BAF64844)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 56372 MW; E479A28F434F925B CRC64;
MGSFPFHRDL QEIASSQLTK ALDPEEFRKQ GHMVINFIAD YYQNIEKYPV LSRVEPGYLK
KCLPVSAPYD PEPISTILRD VQNHIVPGLT HWQSPNFFAY FSSTASTAGF LGEILTTGFN
VVGFNWVSSP AATELENIVM DWLGDMLQLP KSFHFSGNGG GVLHGSTCEA IVCTMVAARD
QMLRRIGSEN LGKLVVYGSD QTHSTLQKAT QIVGINTENF RAIKTTKSTG FALSPEMLRL
TISSDLEKGL VPLFLCATIG TTATTAIDPL EALCHVAKEY GVWVHVDAAY AGSACICPEF
RHFINGVEGA NSFSFNPHKW LFTGMDCCCL WVKNPSVLAS SLSTNPEFLR NKASDSKQVV
DYKDWQIALS RRFRALKLWL VLRSYGVANL RNFIRIHVKM AKTFEGLVRM DKRFEILVPR
NFSLVCFRIS PSALISSNED DEIGMVNEVN CKLLEAINAS GKAYMTHAVV GGLYVLRCAV
GATLTEEKHI VEAWNVVQDH AQAILSTY
