ID   HIDM_GLYEC              Reviewed;         328 AA.
AC   Q5NUF4;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=2-hydroxyisoflavanone dehydratase;
DE            EC=3.1.1.1;
DE            EC=4.2.1.105;
DE   AltName: Full=Carboxylesterase HIDM;
GN   Name=HIDM;
OS   Glycyrrhiza echinata (Licorice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Galegeae; Glycyrrhiza.
OX   NCBI_TaxID=46348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Protoplast;
RX   PubMed=15734910; DOI=10.1104/pp.104.056747;
RA   Akashi T., Aoki T., Ayabe S.;
RT   "Molecular and biochemical characterization of 2-hydroxyisoflavanone
RT   dehydratase. Involvement of carboxylesterase-like proteins in leguminous
RT   isoflavone biosynthesis.";
RL   Plant Physiol. 137:882-891(2005).
CC   -!- FUNCTION: Dehydratase that mediates the biosynthesis of isoflavonoids.
CC       Can better use 2,7-dihydroxy-4'-methoxyisoflavanone as substrate. Has
CC       also a slight carboxylesterase activity toward p-nitrophenyl butyrate.
CC       {ECO:0000269|PubMed:15734910}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-2,4',7-trihydroxyisoflavanone = daidzein + H(+) + H2O;
CC         Xref=Rhea:RHEA:16445, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:63325, ChEBI:CHEBI:77764; EC=4.2.1.105;
CC         Evidence={ECO:0000269|PubMed:15734910};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hydroxy-2,3-dihydrogenistein = genistein + H(+) + H2O;
CC         Xref=Rhea:RHEA:36803, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:31080, ChEBI:CHEBI:74224; EC=4.2.1.105;
CC         Evidence={ECO:0000269|PubMed:15734910};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC         Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC         Evidence={ECO:0000269|PubMed:15734910};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=58 uM for 2,7-dihydroxy-4'-methoxyisoflavanone (at pH 7.5 and 30
CC         degrees Celsius) {ECO:0000269|PubMed:15734910};
CC         KM=210 uM for 2,7,4'-trihydroxyisoflavanone (at pH 7.5 and 30 degrees
CC         Celsius) {ECO:0000269|PubMed:15734910};
CC         KM=304 uM for 2,5,7,4'-tetrahydroxyisoflavanone (at pH 7.5 and 30
CC         degrees Celsius) {ECO:0000269|PubMed:15734910};
CC         Note=kcat is 9.8 sec(-1) with 2,7-dihydroxy-4'-methoxyisoflavanone,
CC         0.12 sec(-1) with 2,7,4'-trihydroxyisoflavanone and 0.19 sec(-1) with
CC         2,5,7,4'-tetrahydroxyisoflavanone as substrates, respectively (at pH
CC         7.5 and 30 degrees Celsius).;
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AB154414; BAD80839.1; -; mRNA.
DR   AlphaFoldDB; Q5NUF4; -.
DR   SMR; Q5NUF4; -.
DR   ESTHER; glyec-q5nuf4; Plant_carboxylesterase.
DR   BRENDA; 4.2.1.105; 2486.
DR   SABIO-RK; Q5NUF4; -.
DR   UniPathway; UPA00154; -.
DR   GO; GO:0033987; F:2-hydroxyisoflavanone dehydratase activity; IDA:UniProtKB.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009717; P:isoflavonoid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0046287; P:isoflavonoid metabolic process; IDA:UniProtKB.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Flavonoid biosynthesis; Hydrolase; Lyase.
FT   CHAIN           1..328
FT                   /note="2-hydroxyisoflavanone dehydratase"
FT                   /id="PRO_0000424102"
FT   MOTIF           85..87
FT                   /note="Involved in the stabilization of the negatively
FT                   charged intermediate by the formation of the oxyanion hole"
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        272
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        304
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
SQ   SEQUENCE   328 AA;  36061 MW;  4694C7E46C2202D4 CRC64;
     MASSTSTTTS KEIDRELPPL LRVYKDGTVE RFLGSSFVPP SPEDPETGVS TKDIVISENP
     TISARVYLPK LNNTTEKLPI LVYYHGGAFC LESAFSFLHQ RYLNIVASKA NVLVVSIEYR
     LAPEHPLPAA YEDGWYALKW VTSHSTNNNK PTNADPWLIK HGDFNRFYIG GDTSGANIAH
     NAALRVGAEA LPGGLRIAGV LSAFPLFWGS KPVLSEPVEG HEKSSPMQVW NFVYPDAPGG
     IDNPLINPLA PGAPNLATLG CPKMLVFVAG KDDLRDRGIW YYEAVKESGW KGDVELAQYE
     GEEHCFQIYH PETENSKDLI GRIASFLV