BETV6_BETPN
ID BETV6_BETPN Reviewed; 308 AA.
AC Q9FUW6; O65002;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Phenylcoumaran benzylic ether reductase Betv6 {ECO:0000305};
DE EC=1.23.1.- {ECO:0000269|PubMed:11606193};
DE AltName: Full=Minor pollen allergen Bet v 6 {ECO:0000303|PubMed:11606193};
DE AltName: Allergen=Bet v 6 {ECO:0000303|PubMed:11606193};
GN Name=BETV6 {ECO:0000303|PubMed:11606193};
OS Betula pendula (European white birch) (Betula verrucosa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Betulaceae; Betula.
OX NCBI_TaxID=3505;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RC TISSUE=Pollen;
RX PubMed=10550744; DOI=10.1016/s0091-6749(99)70080-1;
RA Karamloo F., Schmitz N., Scheurer S., Foetisch K., Hoffmann A.,
RA Haustein D., Vieths S.;
RT "Molecular cloning and characterization of a birch pollen minor allergen,
RT Bet v 5, belonging to a family of isoflavone reductase-related proteins.";
RL J. Allergy Clin. Immunol. 104:991-999(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND ALLERGEN.
RC TISSUE=Pollen;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-300, PROTEIN SEQUENCE OF 176-200, AND
RP ALLERGEN.
RC TISSUE=Pollen;
RX PubMed=9519865; DOI=10.1046/j.1365-3083.1998.00294.x;
RA Vieths S., Frank E., Scheurer S., Meyer H.E., Hrazdina G., Haustein D.;
RT "Characterization of a new IgE-binding 35-kDa protein from birch pollen
RT with cross-reacting homologues in various plant foods.";
RL Scand. J. Immunol. 47:263-272(1998).
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:9519865,
CC PubMed:11606193, PubMed:10550744). Binds to IgE from patients allergic
CC to birch pollen (PubMed:9519865, PubMed:11606193, PubMed:10550744).
CC Induces histamine release from basophils of patient allergic to the
CC birch pollen protein Bet v 6 (PubMed:10550744). Exhibits cross-
CC reactivity with IgE from patients allergic to fruits and vegetables
CC (PubMed:9519865, PubMed:11606193, PubMed:10550744). May be a minor
CC allergen of birch pollen (PubMed:9519865, PubMed:11606193,
CC PubMed:10550744). {ECO:0000269|PubMed:10550744,
CC ECO:0000269|PubMed:11606193, ECO:0000269|PubMed:9519865}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; AF282850; AAG22740.1; -; mRNA.
DR EMBL; AF135127; AAC05116.2; -; mRNA.
DR PIR; T08106; T08106.
DR AlphaFoldDB; Q9FUW6; -.
DR SMR; Q9FUW6; -.
DR Allergome; 131; Bet v 6.
DR Allergome; 132; Bet v 6.0101.
DR Allergome; 133; Bet v 6.0102.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009807; P:lignan biosynthetic process; IEA:UniProt.
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; Direct protein sequencing; NADP; Oxidoreductase.
FT CHAIN 1..308
FT /note="Phenylcoumaran benzylic ether reductase Betv6"
FT /id="PRO_0000447190"
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; 34190 MW; C14AB150751542BC CRC64;
MAHKSKILII GGTGYIGKFI VEASAKSGHP TFALVRESTV SDPVKGKLVE KFKGLGVTLL
HGDLYDHESL VKAFKQVDVV ISTVGHLQLA DQVKIIAAIK EAGNIKRFFP SEFGNDVDRV
HAVEPAKTAF ATKAEIRRKT EAEGIPYTYV SSNFFAGYFL PTLAQPGLTS PPREKVVIFG
DGNARAVFNK EDDIGTYTIR AVDDPRTLNK IVYIKPAKNI YSFNEIVALW EKKIGKTLEK
IYVPEEKLLK DIQESPIPIN VILAINHSVF VKGDHTNFEI EASFGVEASE LYPDVKYTTV
EEYLQQFV
