DIR_SOYBN
ID DIR_SOYBN Reviewed; 186 AA.
AC I1JNN8; C6T2A3;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Pterocarpan synthase 1 {ECO:0000303|PubMed:28394400};
DE Short=GmPTS1 {ECO:0000303|PubMed:28394400};
DE EC=4.2.1.139 {ECO:0000269|PubMed:28394400};
DE AltName: Full=Dirigent protein {ECO:0000305};
DE Flags: Precursor;
GN Name=PTS1 {ECO:0000303|PubMed:28394400};
GN ORFNames=GLYMA_03G147700 {ECO:0000312|EMBL:KRH67111.1};
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].
RA Cheung F., Xiao Y., Chan A., Moskal W., Town C.D.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=28394400; DOI=10.1093/pcp/pcw213;
RA Uchida K., Akashi T., Aoki T.;
RT "The missing link in leguminous pterocarpan biosynthesis is a dirigent
RT domain-containing protein with isoflavanol dehydratase activity.";
RL Plant Cell Physiol. 58:398-408(2017).
CC -!- FUNCTION: Involved in pterocarpan phytoalexin biosynthesis
CC (PubMed:28394400). Catalyzes the last step in the biosynthesis of the
CC phytoalexin medicarpin, and thereby contributes to plant defense
CC reactions (PubMed:28394400). Dirigent proteins impart stereoselectivity
CC on the phenoxy radical-coupling reaction, yielding optically active
CC lignans from two molecules of coniferyl alcohol in the biosynthesis of
CC lignans, flavonolignans, and alkaloids and thus plays a central role in
CC plant secondary metabolism (By similarity).
CC {ECO:0000250|UniProtKB:Q9SUQ8, ECO:0000269|PubMed:28394400}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (4R)-4,2'-dihydroxyisoflavan = a pterocarpan + H2O.;
CC EC=4.2.1.139; Evidence={ECO:0000269|PubMed:28394400};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R,4R)-7,2'-dihydroxy-4'-methoxyisoflavanol = (-)-medicarpin
CC + H2O; Xref=Rhea:RHEA:35811, ChEBI:CHEBI:100, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:72646; EC=4.2.1.139;
CC Evidence={ECO:0000269|PubMed:28394400};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35812;
CC Evidence={ECO:0000269|PubMed:28394400};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R,4R)-3-(6-hydroxy-1,3-benzodioxol-5-yl)-3,4-dihydro-2H-
CC chromene-4,7-diol = (-)-maackiain + H2O; Xref=Rhea:RHEA:58924,
CC ChEBI:CHEBI:99, ChEBI:CHEBI:15377, ChEBI:CHEBI:142868; EC=4.2.1.139;
CC Evidence={ECO:0000269|PubMed:28394400};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58925;
CC Evidence={ECO:0000269|PubMed:28394400};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S,4R)-7,2'-dihydroxy-4'-methoxyisoflavanol = (+)-medicarpin
CC + H2O; Xref=Rhea:RHEA:58920, ChEBI:CHEBI:6714, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:142866; EC=4.2.1.139;
CC Evidence={ECO:0000269|PubMed:28394400};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58921;
CC Evidence={ECO:0000269|PubMed:28394400};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R,4R)-7,2',4'-trihydroxyisoflavanol = (6aR,11aR)-3,9-
CC dihydroxypterocarpan + H2O; Xref=Rhea:RHEA:58928, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15648, ChEBI:CHEBI:142869; EC=4.2.1.139;
CC Evidence={ECO:0000269|PubMed:28394400};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58929;
CC Evidence={ECO:0000269|PubMed:28394400};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9SUQ8}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000305}.
CC -!- INDUCTION: Induced in cell culture by yeast extract, an elicitor for
CC medicarpin induction. {ECO:0000269|PubMed:28394400}.
CC -!- SIMILARITY: Belongs to the plant dirigent protein family.
CC {ECO:0000250|UniProtKB:Q9SUQ8}.
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DR EMBL; BT091561; ACU15747.1; -; mRNA.
DR EMBL; CM000836; KRH67111.1; -; Genomic_DNA.
DR RefSeq; NP_001236934.1; NM_001250005.2.
DR AlphaFoldDB; I1JNN8; -.
DR SMR; I1JNN8; -.
DR PRIDE; I1JNN8; -.
DR EnsemblPlants; KRH67111; KRH67111; GLYMA_03G147700.
DR GeneID; 100500621; -.
DR Gramene; KRH67111; KRH67111; GLYMA_03G147700.
DR KEGG; gmx:100500621; -.
DR eggNOG; ENOG502RXST; Eukaryota.
DR HOGENOM; CLU_087111_2_0_1; -.
DR InParanoid; I1JNN8; -.
DR OMA; HEYREMS; -.
DR OrthoDB; 1307715at2759; -.
DR Proteomes; UP000008827; Chromosome 3.
DR ExpressionAtlas; I1JNN8; baseline and differential.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IEA:UniProt.
DR Gene3D; 2.40.480.10; -; 1.
DR InterPro; IPR044859; Allene_oxi_cyc_Dirigent.
DR InterPro; IPR004265; Dirigent.
DR PANTHER; PTHR21495; PTHR21495; 1.
DR Pfam; PF03018; Dirigent; 1.
PE 2: Evidence at transcript level;
KW Apoplast; Glycoprotein; Lyase; Plant defense; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..186
FT /note="Pterocarpan synthase 1"
FT /id="PRO_5014485865"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 51
FT /note="T -> A (in Ref. 1; ACU15747)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 186 AA; 20511 MW; 025C988E69E251E3 CRC64;
MAKSTFFVCL NLSLLFSLVT ATYYSSLTPT LLGFREEQFT HLHFFFHDVV TGPKPSMVFI
AEPNGKAKDA LPFGTVVAMD DPLTVGPEQD SKLVGKAQGI YTSISQEEMG LMMVMTMAFT
DGDFNGSTIS VLGRNMIMSE PVREMAIVGG TGAFRFARGY AQARFYSVDF TKGDAIVEYD
VFVNHY
