SILD_PODPE
ID SILD_PODPE Reviewed; 278 AA.
AC Q94KL8;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Secoisolariciresinol dehydrogenase {ECO:0000303|PubMed:11278426};
DE EC=1.1.1.331 {ECO:0000269|PubMed:11278426, ECO:0000269|PubMed:15653677, ECO:0000269|PubMed:16493463};
DE Flags: Fragment;
OS Podophyllum peltatum (American mandrake).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Berberidaceae; Podophylloideae;
OC Podophyllum.
OX NCBI_TaxID=35933;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Rhizome;
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).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF SER-153;
RP TYR-167 AND LYS-171.
RX PubMed=16493463; DOI=10.1039/b516563f;
RA Moinuddin S.G., Youn B., Bedgar D.L., Costa M.A., Helms G.L., Kang C.,
RA Davin L.B., Lewis N.G.;
RT "Secoisolariciresinol dehydrogenase: mode of catalysis and
RT stereospecificity of hydride transfer in Podophyllum peltatum.";
RL Org. Biomol. Chem. 4:808-816(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEXES WITH NAD AND
RP MATAIRESINOL, CATALYTIC ACTIVITY, ACTIVE SITE, AND SUBUNIT.
RX PubMed=15653677; DOI=10.1074/jbc.m413266200;
RA Youn B., Moinuddin S.G., Davin L.B., Lewis N.G., Kang C.;
RT "Crystal structures of apo-form and binary/ternary complexes of Podophyllum
RT secoisolariciresinol dehydrogenase, an enzyme involved in formation of
RT health-protecting and plant defense lignans.";
RL J. Biol. Chem. 280:12917-12926(2005).
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 ECO:0000269|PubMed:16493463}.
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, ECO:0000269|PubMed:15653677,
CC ECO:0000269|PubMed:16493463};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15653677}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF352734; AAK38664.1; -; mRNA.
DR PDB; 2BGK; X-ray; 1.60 A; A/B=1-278.
DR PDB; 2BGL; X-ray; 2.80 A; A=1-278.
DR PDB; 2BGM; X-ray; 2.00 A; A=1-278.
DR PDBsum; 2BGK; -.
DR PDBsum; 2BGL; -.
DR PDBsum; 2BGM; -.
DR AlphaFoldDB; Q94KL8; -.
DR SMR; Q94KL8; -.
DR KEGG; ag:AAK38664; -.
DR BRENDA; 1.1.1.331; 4929.
DR EvolutionaryTrace; Q94KL8; -.
DR GO; GO:0102911; F:(-)-secoisolariciresinol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009807; P:lignan biosynthetic process; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IPI: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 3D-structure; NAD; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..>278
FT /note="Secoisolariciresinol dehydrogenase"
FT /id="PRO_0000424207"
FT ACT_SITE 167
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:15653677,
FT ECO:0000269|PubMed:16493463, ECO:0007744|PDB:2BGL,
FT ECO:0007744|PDB:2BGM"
FT BINDING 23..28
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15653677,
FT ECO:0007744|PDB:2BGL, ECO:0007744|PDB:2BGM"
FT BINDING 47
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15653677,
FT ECO:0007744|PDB:2BGL, ECO:0007744|PDB:2BGM"
FT BINDING 73
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15653677,
FT ECO:0007744|PDB:2BGL, ECO:0007744|PDB:2BGM"
FT BINDING 99
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15653677,
FT ECO:0007744|PDB:2BGL, ECO:0007744|PDB:2BGM"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15653677,
FT ECO:0007744|PDB:2BGL, ECO:0007744|PDB:2BGM"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15653677,
FT ECO:0007744|PDB:2BGL, ECO:0007744|PDB:2BGM"
FT BINDING 171
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15653677,
FT ECO:0007744|PDB:2BGL, ECO:0007744|PDB:2BGM"
FT BINDING 200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007744|PDB:2BGL, ECO:0007744|PDB:2BGM"
FT MUTAGEN 153
FT /note="S->A: Strongly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:16493463"
FT MUTAGEN 167
FT /note="Y->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:16493463"
FT MUTAGEN 171
FT /note="K->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:16493463"
FT NON_TER 278
FT TURN 13..16
FT /evidence="ECO:0007829|PDB:2BGK"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:2BGK"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:2BGK"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:2BGK"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:2BGK"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2BGK"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:2BGK"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:2BGK"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:2BGK"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:2BGK"
FT HELIX 115..125
FT /evidence="ECO:0007829|PDB:2BGK"
FT HELIX 127..140
FT /evidence="ECO:0007829|PDB:2BGK"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:2BGK"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:2BGK"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:2BGK"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2BGL"
FT HELIX 165..185
FT /evidence="ECO:0007829|PDB:2BGK"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:2BGK"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:2BGK"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:2BGK"
FT HELIX 213..222
FT /evidence="ECO:0007829|PDB:2BGK"
FT HELIX 233..244
FT /evidence="ECO:0007829|PDB:2BGK"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:2BGK"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:2BGK"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:2BGK"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:2BGK"
SQ SEQUENCE 278 AA; 29253 MW; DB735A376E112375 CRC64;
MGSTSTPDSS TNRLQDKVAI ITGGAGGIGE TTAKLFVRYG AKVVIADIAD DHGQKVCNNI
GSPDVISFVH CDVTKDEDVR NLVDTTIAKH GKLDIMFGNV GVLSTTPYSI LEAGNEDFKR
VMDINVYGAF LVAKHAARVM IPAKKGSIVF TASISSFTAG EGVSHVYTAT KHAVLGLTTS
LCTELGEYGI RVNCVSPYIV ASPLLTDVFG VDSSRVEELA HQAANLKGTL LRAEDVADAV
AYLAGDESKY VSGLNLVIDG GYTRTNPAFP TALKHGLA
