HIDH_SOYBN
ID HIDH_SOYBN Reviewed; 319 AA.
AC Q5NUF3;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=2-hydroxyisoflavanone dehydratase;
DE EC=3.1.1.1;
DE EC=4.2.1.105;
DE AltName: Full=Carboxylesterase HIDH;
GN Name=HIDH; OrderedLocusNames=Glyma01g45020;
OS Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, MOTIF,
RP MUTAGENESIS OF GLY-78; GLY-79; THR-164; ASP-263 AND HIS-295, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Seedling;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cheung F., Xiao Y., Chan A., Moskal W., Town C.D.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82;
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
CC -!- FUNCTION: Dehydratase that mediates the biosynthesis of isoflavonoids.
CC Can use both 4'-hydroxylated and 4'-methoxylated 2-hydroxyisoflavanones
CC as substrates. Has also a slight carboxylesterase activity toward p-
CC nitrophenyl butyrate. {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=29 uM for 2,7-dihydroxy-4'-methoxyisoflavanone (at pH 7.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:15734910};
CC KM=114 uM for 2,7,4'-trihydroxyisoflavanone (at pH 7.5 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:15734910};
CC KM=170 uM for 2,5,7,4'-tetrahydroxyisoflavanone (at pH 7.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:15734910};
CC Note=kcat is 1.6 sec(-1) with 2,7-dihydroxy-4'-methoxyisoflavanone,
CC 5.3 sec(-1) with 2,7,4'-trihydroxyisoflavanone and 18.1 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; AB154415; BAD80840.1; -; mRNA.
DR EMBL; BT097440; ACU22699.1; -; mRNA.
DR EMBL; CM000834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001237228.1; NM_001250299.2.
DR AlphaFoldDB; Q5NUF3; -.
DR SMR; Q5NUF3; -.
DR STRING; 3847.GLYMA01G45020.1; -.
DR ESTHER; soybn-q5nuf3; Plant_carboxylesterase.
DR PRIDE; Q5NUF3; -.
DR EnsemblPlants; KRH77876; KRH77876; GLYMA_01G239600.
DR GeneID; 547489; -.
DR Gramene; KRH77876; KRH77876; GLYMA_01G239600.
DR KEGG; gmx:547489; -.
DR eggNOG; KOG1515; Eukaryota.
DR HOGENOM; CLU_012494_22_0_1; -.
DR InParanoid; Q5NUF3; -.
DR OMA; IDNPWIN; -.
DR OrthoDB; 1263520at2759; -.
DR SABIO-RK; Q5NUF3; -.
DR UniPathway; UPA00154; -.
DR Proteomes; UP000008827; Chromosome 1.
DR Genevisible; Q5NUF3; GM.
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:0016787; F:hydrolase activity; IBA:GO_Central.
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 InterPro; IPR002168; Lipase_GDXG_HIS_AS.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
PE 1: Evidence at protein level;
KW Flavonoid biosynthesis; Hydrolase; Lyase; Reference proteome.
FT CHAIN 1..319
FT /note="2-hydroxyisoflavanone dehydratase"
FT /id="PRO_0000424101"
FT MOTIF 77..79
FT /note="Involved in the stabilization of the negatively
FT charged intermediate by the formation of the oxyanion hole"
FT /evidence="ECO:0000305|PubMed:15734910"
FT ACT_SITE 164
FT /evidence="ECO:0000305|PubMed:15734910"
FT ACT_SITE 263
FT /evidence="ECO:0000305|PubMed:15734910"
FT ACT_SITE 295
FT /evidence="ECO:0000305|PubMed:15734910"
FT MUTAGEN 78
FT /note="G->A: Reduction of both dehydratase and
FT carboxylesterase activities."
FT /evidence="ECO:0000269|PubMed:15734910"
FT MUTAGEN 79
FT /note="G->A: Reduction of both dehydratase and
FT carboxylesterase activities."
FT /evidence="ECO:0000269|PubMed:15734910"
FT MUTAGEN 164
FT /note="T->A,S: Reduction of both dehydratase and
FT carboxylesterase activities."
FT /evidence="ECO:0000269|PubMed:15734910"
FT MUTAGEN 263
FT /note="D->N: Complete loss of both dehydratase and
FT carboxylesterase activities."
FT /evidence="ECO:0000269|PubMed:15734910"
FT MUTAGEN 295
FT /note="H->A: Complete loss of both dehydratase and
FT carboxylesterase activities."
FT /evidence="ECO:0000269|PubMed:15734910"
SQ SEQUENCE 319 AA; 35138 MW; E8333CF425FBA4A3 CRC64;
MAKEIVKELL PLIRVYKDGS VERLLSSENV AASPEDPQTG VSSKDIVIAD NPYVSARIFL
PKSHHTNNKL PIFLYFHGGA FCVESAFSFF VHRYLNILAS EANIIAISVD FRLLPHHPIP
AAYEDGWTTL KWIASHANNT NTTNPEPWLL NHADFTKVYV GGETSGANIA HNLLLRAGNE
SLPGDLKILG GLLCCPFFWG SKPIGSEAVE GHEQSLAMKV WNFACPDAPG GIDNPWINPC
VPGAPSLATL ACSKLLVTIT GKDEFRDRDI LYHHTVEQSG WQGELQLFDA GDEEHAFQLF
KPETHLAKAM IKRLASFLV
