SILD_FORIN
ID SILD_FORIN Reviewed; 277 AA.
AC Q94KL7;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Secoisolariciresinol dehydrogenase;
DE EC=1.1.1.331;
DE Flags: Fragment;
OS Forsythia intermedia (Border forsythia) (Forsythia suspensa x Forsythia
OS viridissima).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Oleaceae; Forsythieae; Forsythia.
OX NCBI_TaxID=55183;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC TISSUE=Stem;
RX PubMed=11278426; DOI=10.1074/jbc.m008622200;
RA Xia Z.Q., Costa M.A., Pelissier H.C., Davin L.B., Lewis N.G.;
RT "Secoisolariciresinol dehydrogenase purification, cloning, and functional
RT expression. Implications for human health protection.";
RL J. Biol. Chem. 276:12614-12623(2001).
CC -!- FUNCTION: Oxidoreductase involved in lignan biosynthesis. Catalyzes the
CC stereospecific conversion of (-)-secoisolariciresinol to (-)-
CC matairesinol via a lactol intermediate. {ECO:0000269|PubMed:11278426}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(-)-secoisolariciresinol + 2 NAD(+) = (-)-matairesinol + 2
CC H(+) + 2 NADH; Xref=Rhea:RHEA:33887, ChEBI:CHEBI:6698,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:65004; EC=1.1.1.331;
CC Evidence={ECO:0000269|PubMed:11278426};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF352735; AAK38665.1; -; mRNA.
DR AlphaFoldDB; Q94KL7; -.
DR SMR; Q94KL7; -.
DR BRENDA; 1.1.1.331; 13002.
DR GO; GO:0102911; F:(-)-secoisolariciresinol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0009807; P:lignan biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NAD; Oxidoreductase.
FT CHAIN 1..>277
FT /note="Secoisolariciresinol dehydrogenase"
FT /id="PRO_0000424208"
FT ACT_SITE 166
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 24..29
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT NON_TER 277
SQ SEQUENCE 277 AA; 29256 MW; 98885C210CAFE2EB CRC64;
MAATSQVLTA IARRLEGKVA LITGGASGIG ETTAKLFSQH GAKVAIADVQ DELGHSVVEA
IGTSNSTYIH CDVTNEDGVK NAVDNTVSTY GKLDIMFSNA GISDPNRPRI IDNEKADFER
VFSVNVTGVF LCMKHAARVM IPARSGNIIS TASLSSTMGG GSSHAYCGSK HAVLGLTRNL
AVELGQFGIR VNCLSPFGLP TALGKKFSGI KNEEEFENVI NFAGNLKGPK FNVEDVANAA
LYLASDEAKY VSGHNLFIDG GFSVCNSVIK VFQYPDS
