ID   6DCS_SOYBN              Reviewed;         315 AA.
AC   P26690;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=NAD(P)H-dependent 6'-deoxychalcone synthase;
DE            EC=2.3.1.170;
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], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Harosoy 63;
RX   PubMed=1840523; DOI=10.1111/j.1432-1033.1991.tb15833.x;
RA   Welle R., Schroeder G., Schiltz E., Grisebach H., Schroeder J.;
RT   "Induced plant responses to pathogen attack. Analysis and heterologous
RT   expression of the key enzyme in the biosynthesis of phytoalexins in soybean
RT   (Glycine max L. Merr. cv. Harosoy 63).";
RL   Eur. J. Biochem. 196:423-430(1991).
CC   -!- FUNCTION: Co-acts with chalcone synthase in formation of 4,2',4'-
CC       trihydroxychalcone, involved in the biosynthesis of glyceollin type
CC       phytoalexins.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-coumaroyl-CoA + 3 H(+) + 3 malonyl-CoA + NADPH = 3 CO2 + 4
CC         CoA + H2O + isoliquiritigenin + NADP(+); Xref=Rhea:RHEA:10584,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57355, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77948;
CC         EC=2.3.1.170;
CC   -!- PATHWAY: Phytoalexin biosynthesis; glyceollin biosynthesis.
CC   -!- SUBUNIT: Monomer.
CC   -!- INDUCTION: By pathogen infection.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; X55730; CAA39261.1; -; mRNA.
DR   PIR; S14222; S14222.
DR   RefSeq; NP_001235973.1; NM_001249044.1.
DR   AlphaFoldDB; P26690; -.
DR   SMR; P26690; -.
DR   STRING; 3847.GLYMA02G47750.1; -.
DR   PRIDE; P26690; -.
DR   ProMEX; P26690; -.
DR   GeneID; 547911; -.
DR   KEGG; gmx:547911; -.
DR   eggNOG; KOG1577; Eukaryota.
DR   OrthoDB; 1016440at2759; -.
DR   UniPathway; UPA00898; -.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0033808; F:6'-deoxychalcone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd19124; AKR_AKR4A_4B; 1.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR044497; AKR4A/B.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; SSF51430; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Flavonoid biosynthesis; NADP;
KW   Reference proteome; Transferase.
FT   CHAIN           1..315
FT                   /note="NAD(P)H-dependent 6'-deoxychalcone synthase"
FT                   /id="PRO_0000124609"
FT   ACT_SITE        59
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         216..274
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            88
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   315 AA;  35490 MW;  C3A6BE07EF330F47 CRC64;
     MAAAIEIPTI VFPNSSAQQR MPVVGMGSAP DFTCKKDTKE AIIEAVKQGY RHFDTAAAYG
     SEQALGEALK EAIHLGLVSR QDLFVTSKLW VTENHPHLVL PALRKSLKTL QLEYLDLYLI
     HWPLSSQPGK FSFPIEVEDL LPFDVKGVWE SMEECQKLGL TKAIGVSNFS VKKLQNLLSV
     ATIRPVVDQV EMNLAWQQKK LREFCKENGI IVTAFSPLRK GASRGPNEVM ENDVLKEIAE
     AHGKSIAQVS LRWLYEQGVT FVPKSYDKER MNQNLHIFDW ALTEQDHHKI SQISQSRLIS
     GPTKPQLADL WDDQI