PAR1_ROSHC
ID PAR1_ROSHC Reviewed; 322 AA.
AC A0A0B6VQ48; A0A0B6VNC0; B1B610;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Phenylacetaldehyde reductase {ECO:0000303|PubMed:20650544};
DE EC=1.1.1.- {ECO:0000269|PubMed:20650544};
DE AltName: Full=2-phenylethanol synthase {ECO:0000305};
GN Name=PAR {ECO:0000303|PubMed:20650544};
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], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=20650544; DOI=10.1016/j.jplph.2010.06.011;
RA Chen X.M., Kobayashi H., Sakai M., Hirata H., Asai T., Ohnishi T.,
RA Baldermann S., Watanabe N.;
RT "Functional characterization of rose phenylacetaldehyde reductase (PAR), an
RT enzyme involved in the biosynthesis of the scent compound 2-
RT phenylethanol.";
RL J. Plant Physiol. 168:88-95(2011).
CC -!- FUNCTION: Catalyzes the reduction of 2-phenylethylamine to produce 2-
CC phenylethanol, a constituent of floral scent in petals.
CC {ECO:0000269|PubMed:20650544}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-phenylacetaldehyde + H(+) + NADPH = 2-phenylethanol +
CC NADP(+); Xref=Rhea:RHEA:63736, ChEBI:CHEBI:15378, ChEBI:CHEBI:16424,
CC ChEBI:CHEBI:49000, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:20650544};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63737;
CC Evidence={ECO:0000269|PubMed:20650544};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-phenylacetaldehyde + H(+) + NADH = 2-phenylethanol + NAD(+);
CC Xref=Rhea:RHEA:63740, ChEBI:CHEBI:15378, ChEBI:CHEBI:16424,
CC ChEBI:CHEBI:49000, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:20650544};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63741;
CC Evidence={ECO:0000269|PubMed:20650544};
CC -!- TISSUE SPECIFICITY: Highly expressed in petals (PubMed:20650544).
CC Expressed in calyxes and leaves (PubMed:20650544).
CC {ECO:0000269|PubMed:20650544}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR EMBL; AB426519; BAG13450.2; -; mRNA.
DR EMBL; AB972811; BAQ20438.1; -; mRNA.
DR EMBL; AB972812; BAQ20439.1; -; mRNA.
DR AlphaFoldDB; A0A0B6VQ48; -.
DR SMR; A0A0B6VQ48; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase.
FT CHAIN 1..322
FT /note="Phenylacetaldehyde reductase"
FT /id="PRO_0000450479"
FT BINDING 42
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 161
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT CONFLICT 116
FT /note="P -> T (in Ref. 1; BAQ20438)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="I -> V (in Ref. 1; BAQ20438)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 35386 MW; 614F90377E923EB3 CRC64;
MSNKVVCVTG ASGYIASWLV KLLLQRGYTV KASVRNPNDP TKTEHLLALD GAKERLQLFK
ADLLEEGSFD SAVEGCEGVF HTASPFYHDV TDPKAELLDP AVKGTLNVLN SCSKSPSIKR
VVLTSSIAAV AYNGKPRTPD VVVDETWFTD PDVCKESKLW YVLSKTLAED AAWKFVKEKG
IDMVTINPAM VIGPLLQPTL NTSAAAILNI IKGARTYPNA SFGWINVKDV ANAHVQAFEI
PSASGRYCLV ERVAHFTEVL QIIHELYPDL QLPEKCSDDK PFVPTYQVSK EKAKSLGIEF
IPLDISLKET IESLKEKSIV SF
