ID   PYRC5_PYRCO             Reviewed;         308 AA.
AC   O81355;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Phenylcoumaran benzylic ether reductase Pyrc5 {ECO:0000305};
DE            EC=1.23.1.- {ECO:0000269|PubMed:11606193};
DE   AltName: Full=Minor fruit allergen Pyr c 5 {ECO:0000303|PubMed:11606193};
DE   AltName: Allergen=Pyr c 5 {ECO:0000303|PubMed:11606193};
GN   Name=PYRC5 {ECO:0000312|EMBL:AAC24001.1};
OS   Pyrus communis (Pear) (Pyrus domestica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Pyrus.
OX   NCBI_TaxID=23211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND ALLERGEN.
RX   PubMed=11606193; DOI=10.1046/j.0014-2956.2001.02463.x;
RA   Karamloo F., Wangorsch A., Kasahara H., Davin L.B., Haustein D.,
RA   Lewis N.G., Vieths S.;
RT   "Phenylcoumaran benzylic ether and isoflavonoid reductases are a new class
RT   of cross-reactive allergens in birch pollen, fruits and vegetables.";
RL   Eur. J. Biochem. 268:5310-5320(2001).
CC   -!- FUNCTION: Oxidoreductase involved in lignan biosynthesis
CC       (PubMed:11606193). Catalyzes the NADPH-dependent reduction of
CC       phenylcoumaran benzylic ethers (PubMed:11606193). Converts
CC       dehydrodiconiferyl alcohol (DDC) to isodihydrodehydrodiconiferyl
CC       alcohol (IDDDC) (PubMed:11606193). {ECO:0000269|PubMed:11606193}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(-)-dehydrodiconiferyl alcohol + H(+) + NADPH = (S)-
CC         isodihydrodehydrodiconiferyl alcohol + NADP(+); Xref=Rhea:RHEA:59440,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:70467, ChEBI:CHEBI:143259;
CC         Evidence={ECO:0000269|PubMed:11606193};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(+)-dehydrodiconiferyl alcohol + H(+) + NADPH = (R)-
CC         isodihydrodehydrodiconiferyl alcohol + NADP(+); Xref=Rhea:RHEA:59844,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:143256, ChEBI:CHEBI:143260;
CC         Evidence={ECO:0000269|PubMed:11606193};
CC   -!- ALLERGEN: May cause an allergic reaction in human (PubMed:11606193).
CC       Binds to IgE from patients allergic to pear fruit (PubMed:11606193).
CC       Induces histamine release from basophils of patient allergic to the
CC       pear fruit protein Pyr c 5 (PubMed:11606193). Exhibits cross-reactivity
CC       with IgE from patients allergic to other fruits, vegetables and birch
CC       pollen (PubMed:11606193). May be a minor allergen of pear fruit
CC       (PubMed:11606193). {ECO:0000269|PubMed:11606193}.
CC   -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC       reductase subfamily. {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; AF071477; AAC24001.1; -; mRNA.
DR   AlphaFoldDB; O81355; -.
DR   SMR; O81355; -.
DR   Allergome; 3460; Pyr c 5.0101.
DR   Allergome; 609; Pyr c 5.
DR   GO; GO:0032442; F:phenylcoumaran benzylic ether reductase activity; IDA:UniProtKB.
DR   GO; GO:0009807; P:lignan biosynthetic process; IDA:UniProtKB.
DR   CDD; cd05259; PCBER_SDR_a; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR008030; NmrA-like.
DR   InterPro; IPR045312; PCBER-like.
DR   Pfam; PF05368; NmrA; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Allergen; NADP; Oxidoreductase.
FT   CHAIN           1..308
FT                   /note="Phenylcoumaran benzylic ether reductase Pyrc5"
FT                   /id="PRO_0000447191"
FT   ACT_SITE        133
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         11..17
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000305|PubMed:11606193"
FT   BINDING         36
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         45
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         137
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
SQ   SEQUENCE   308 AA;  33823 MW;  D7C630AD8BD65C32 CRC64;
     MASKSQILFI GGTGYIGKFI VEASAKAGYP TYVLVREASL SDPAKSKVIE NFKALGVNFV
     LGDLYDHESL VKAIKQVDVV ISTVGHGQLA DQGKIIAAIK EAGNVKRFFP SEFGNDVDRS
     HAVEPAKSAF ETKAKIRRAV EAEGIPYTYV SSNFFAGYFL PTLNQPGASS APRDKVVILG
     DGNPKAIFNK EDDIGTYTIR AVDDPRTLNK VLYIRPPANT ISFNELVSLW EKKIGKTLER
     IYVPEEQLLK NIQEAAVPLN VILSISHAVF VKGDHTNFEI EPSFGVEATA LYPDVKYTTV
     DEYLNQFV