ID   ALL12_OLEEU             Reviewed;         308 AA.
AC   E1U332;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Isoflavone reductase-like protein {ECO:0000305};
DE   AltName: Full=Pollen allergen Ole e 12 {ECO:0000303|PubMed:22385802};
DE   AltName: Allergen=Ole e 12 {ECO:0000303|PubMed:22385802};
OS   Olea europaea (Common olive).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Oleaceae; Oleeae; Olea.
OX   NCBI_TaxID=4146;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Castro L., Rodriguez R., Villalba M.;
RT   "Ole e 12, an allergen from olive pollen, is an isoflavone reductase.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   REVIEW, AND NOMENCLATURE.
RX   PubMed=22385802; DOI=10.1016/j.talanta.2012.01.016;
RA   Esteve C., Montealegre C., Marina M.L., Garcia M.C.;
RT   "Analysis of olive allergens.";
RL   Talanta 92:1-14(2012).
RN   [3]
RP   3D-STRUCTURE MODELING, AND SUBUNIT.
RX   PubMed=24154826; DOI=10.1007/s10822-013-9686-y;
RA   Jimenez-Lopez J.C., Kotchoni S.O., Hernandez-Soriano M.C., Gachomo E.W.,
RA   Alche J.D.;
RT   "Structural functionality, catalytic mechanism modeling and molecular
RT   allergenicity of phenylcoumaran benzylic ether reductase, an olive pollen
RT   (Ole e 12) allergen.";
RL   J. Comput. Aided Mol. Des. 27:873-895(2013).
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24154826}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALLERGEN: Protein found in olive tree pollen that may cause an allergic
CC       reaction in human. {ECO:0000305}.
CC   -!- MISCELLANEOUS: The catalytic tetrad is probably composed of Lys-133,
CC       Tyr-158, Ser-159 and Asn-153. {ECO:0000305|PubMed:24154826}.
CC   -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC       reductase subfamily. {ECO:0000305}.
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DR   EMBL; EU927297; ACL13551.1; -; mRNA.
DR   AlphaFoldDB; E1U332; -.
DR   SMR; E1U332; -.
DR   Allergome; 12134; Ole e 12.0101.
DR   Allergome; 9073; Ole e 12.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; Cytoplasm; NADP; Oxidoreductase.
FT   CHAIN           1..308
FT                   /note="Isoflavone reductase-like protein"
FT                   /id="PRO_0000421084"
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:0000250|UniProtKB:Q9LD14"
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;  34068 MW;  4B8FCC442FE93F0D CRC64;
     MADKTKILII GGTGYIGKFI VEASAKSEHP TFALARESTI SDPVKGKIIQ GFKNSGVTIL
     TGDLYDHESL VKAIKQVDVV ISTVGQLQLA DQVKIIAAIK EAGNVKRFFP SDFGTDVDRC
     HAVEPAKSSF EIKSQIRRAI EAEGIPYTFV SANYFAGYSL PTLVQPEVTA PPRDKVIILG
     DGNAKAVFNE ENDIGTYTIK AVDDARTLNK ILYIKPPKNI YSFNELVALW EKKIGKTLEK
     IYVPEEQVLK QIQESPFPIN IVMAINHSAF VKGDLTNFKI EPSFGVEASE LYPDVKYTTV
     EEYLDQFV