SDH_SINHE
ID SDH_SINHE Reviewed; 278 AA.
AC A3F5F0;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Secoisolariciresinol dehydrogenase {ECO:0000303|PubMed:23653238, ECO:0000303|Ref.1};
DE Short=PhSDH {ECO:0000303|PubMed:23653238};
DE EC=1.1.1.331 {ECO:0000269|PubMed:26359402};
GN Name=SDH {ECO:0000303|PubMed:23653238, ECO:0000303|Ref.1};
GN Synonyms=Phex30828 {ECO:0000303|PubMed:26359402};
OS Sinopodophyllum hexandrum (Himalayan may apple) (Podophyllum hexandrum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Berberidaceae; Podophylloideae;
OC Sinopodophyllum.
OX NCBI_TaxID=93608;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wankhade D.P., Sen J., Sinha A.K.;
RT "Secoisolariciresinol dehydrogenase from Podophyllum hexandrum Royle.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY, AND INDUCTION BY WOUNDING; UV-LIGHT AND JASMONIC ACID.
RX PubMed=23653238; DOI=10.1007/s00709-013-0505-z;
RA Wankhede D.P., Biswas D.K., Rajkumar S., Sinha A.K.;
RT "Expressed sequence tags and molecular cloning and characterization of gene
RT encoding pinoresinol/lariciresinol reductase from Podophyllum hexandrum.";
RL Protoplasma 250:1239-1249(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOTECHNOLOGY, TISSUE SPECIFICITY, INDUCTION
RP BY WOUNDING, AND PATHWAY.
RX PubMed=26359402; DOI=10.1126/science.aac7202;
RA Lau W., Sattely E.S.;
RT "Six enzymes from mayapple that complete the biosynthetic pathway to the
RT etoposide aglycone.";
RL Science 349:1224-1228(2015).
CC -!- FUNCTION: Oxidoreductase involved in lignan biosynthesis
CC (PubMed:26359402). Also involved in the biosynthesis of etoposide, a
CC chemotherapeutic compound of the topoisomerase inhibitor family
CC (PubMed:26359402). Catalyzes the stereospecific conversion of (-)-
CC secoisolariciresinol to (-)-matairesinol via a lactol intermediate
CC (PubMed:26359402). {ECO:0000269|PubMed:26359402}.
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:26359402};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33888;
CC Evidence={ECO:0000269|PubMed:26359402};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC {ECO:0000269|PubMed:26359402}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q94KL8}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in stems and rhizomes, and, to a
CC lower extent, in leaves. {ECO:0000269|PubMed:23653238,
CC ECO:0000269|PubMed:26359402}.
CC -!- INDUCTION: Transiently induced after wounding and by jasmonic acid
CC (MeJA) (PubMed:26359402, PubMed:23653238). After an exposition to UV-
CC light, first transiently induced before fading out (PubMed:23653238).
CC {ECO:0000269|PubMed:23653238, ECO:0000269|PubMed:26359402}.
CC -!- BIOTECHNOLOGY: Combinatorially expression of Sinopodophyllum hexandrum
CC (mayapple) genes of the podophyllotoxin pathway (e.g. DIR, PLR, SDH,
CC CYP719A23, OMT3, CYP71CU1, OMT1, 2-ODD, CYP71BE54 and CYP82D61) in
CC Nicotiana benthamiana (tobacco) results in the production of the
CC chemotherapeutic compound etoposide. {ECO:0000305|PubMed:26359402}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; EF205022; ABN14311.1; -; mRNA.
DR AlphaFoldDB; A3F5F0; -.
DR SMR; A3F5F0; -.
DR KEGG; ag:ABN14311; -.
DR BRENDA; 1.1.1.331; 4928.
DR UniPathway; UPA00711; -.
DR GO; GO:0102911; F:(-)-secoisolariciresinol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0019438; P:aromatic compound biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009807; P:lignan biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0009411; P:response to UV; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR CDD; cd05326; secoisolariciresinol-DH_like_SDR_c; 1.
DR InterPro; IPR045309; ABA2-like.
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 NAD; Oxidoreductase.
FT CHAIN 1..278
FT /note="Secoisolariciresinol dehydrogenase"
FT /id="PRO_0000451900"
FT ACT_SITE 167
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q94KL8"
FT BINDING 23..28
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q94KL8"
FT BINDING 47
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q94KL8"
FT BINDING 73
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q94KL8"
FT BINDING 99
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q94KL8"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q94KL8"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q94KL8"
FT BINDING 171
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q94KL8"
FT BINDING 200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q94KL8"
SQ SEQUENCE 278 AA; 29196 MW; FBB3EDF643D7F1FE CRC64;
MGSTSTPASS TNRLQDKVAI ITGGAGGIGE TTAKLFVRYG AKVVIADISD DHGQKVCNNI
GSPDVISFVH CDVTKDEDVR NLVDTTIAKH GKLDIMFGNV GVLSTTPYSI LEAGNEDFKR
VMDINVYGAF LVAKHAARVM IPAKKGSIVF TASISSFTAG EGVSHVYTAT KHAVLGLTTS
LCTELGQHGI RVNCVSPYVV ASPLLTDVFG VDSSRVEELA HQAANLKGIL LRAEDVADAV
AYLAGDESKY VSGLNLVIDG GYTRTNPAFP TALKHGLA
