DIR_GLYEC
ID DIR_GLYEC Reviewed; 188 AA.
AC A0A1V1FH01;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Pterocarpan synthase 1 {ECO:0000303|PubMed:28394400};
DE Short=GePTS1 {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};
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, AND CATALYTIC ACTIVITY.
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=(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)-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=(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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=200 uM for (3R,4R)-7,2'-dihydroxy-4'-methoxyisoflavanol
CC {ECO:0000269|PubMed:28394400};
CC pH dependence:
CC Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:28394400};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9SUQ8}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the plant dirigent protein family.
CC {ECO:0000250|UniProtKB:Q9SUQ8}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LC121822; BAX03553.1; -; mRNA.
DR PDB; 6OOC; X-ray; 2.60 A; A/B/C/D/E/F=1-188.
DR PDBsum; 6OOC; -.
DR AlphaFoldDB; A0A1V1FH01; -.
DR SMR; A0A1V1FH01; -.
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 1: Evidence at protein level;
KW 3D-structure; Apoplast; Glycoprotein; Lyase; Plant defense; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..188
FT /note="Pterocarpan synthase 1"
FT /id="PRO_5010603000"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:6OOC"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:6OOC"
FT STRAND 37..50
FT /evidence="ECO:0007829|PDB:6OOC"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:6OOC"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:6OOC"
FT STRAND 78..90
FT /evidence="ECO:0007829|PDB:6OOC"
FT STRAND 95..105
FT /evidence="ECO:0007829|PDB:6OOC"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6OOC"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:6OOC"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:6OOC"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:6OOC"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:6OOC"
FT STRAND 143..153
FT /evidence="ECO:0007829|PDB:6OOC"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:6OOC"
FT STRAND 160..170
FT /evidence="ECO:0007829|PDB:6OOC"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:6OOC"
FT STRAND 177..188
FT /evidence="ECO:0007829|PDB:6OOC"
SQ SEQUENCE 188 AA; 20698 MW; 8B4218C0EDB45E3C CRC64;
MAKSTTFFIS LTLPFLLLSV VTATYYQSMS PTVLGFQEEK FTHLHFYFHD VVTGPKPSMV
IVAEPNGKAK NSLPFGTVVA MDDPLTVGPE SDSKLVGKAQ GIYTSISQEE MGLMMVMTMA
FSDGEFNGST LSILARNMIM SEPVREMAIV GGTGAFRFAR GYAQAKFYSV DFTKGDAIVE
YDIFVFHY
