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Protein

Secoisolariciresinol dehydrogenase

Gene
N/A
Organism
Podophyllum peltatum (Mayapple)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Oxidoreductase involved in lignan biosynthesis. Catalyzes the stereospecific conversion of (-)-secoisolariciresinol to (-)-matairesinol via a lactol intermediate.2 Publications

Catalytic activityi

--secoisolariciresinol + 2 NAD+ = (-)-matairesinol + 2 NADH.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei47NAD1
Binding sitei73NAD; via amide nitrogen1
Binding sitei99NAD; via carbonyl oxygen1
Binding sitei104Substrate; via carbonyl oxygen1
Binding sitei164Substrate; via amide nitrogen1
Active sitei167Proton donor/acceptor2 Publications1
Binding sitei171NAD1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi23 – 28NAD6

GO - Molecular functioni

GO - Biological processi

  • lignan biosynthetic process Source: UniProtKB
  • protein homotetramerization Source: UniProtKB

Keywordsi

Molecular functionOxidoreductase
LigandNAD, Nucleotide-binding

Enzyme and pathway databases

BRENDAi1.1.1.331 4929

Names & Taxonomyi

Protein namesi
Recommended name:
Secoisolariciresinol dehydrogenase (EC:1.1.1.331)
OrganismiPodophyllum peltatum (Mayapple)
Taxonomic identifieri35933 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsRanunculalesBerberidaceaePodophylloideaePodophyllum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi153S → A: Strongly reduces enzyme activity. 1 Publication1
Mutagenesisi167Y → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi171K → A: Abolishes enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004242071 – ›278Secoisolariciresinol dehydrogenaseAdd BLAST›278

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1278
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni13 – 16Combined sources4
Beta strandi18 – 23Combined sources6
Helixi27 – 38Combined sources12
Beta strandi42 – 48Combined sources7
Helixi50 – 60Combined sources11
Turni63 – 65Combined sources3
Beta strandi66 – 70Combined sources5
Helixi76 – 90Combined sources15
Beta strandi95 – 98Combined sources4
Turni110 – 112Combined sources3
Helixi115 – 125Combined sources11
Helixi127 – 140Combined sources14
Turni141 – 144Combined sources4
Beta strandi146 – 151Combined sources6
Helixi154 – 156Combined sources3
Beta strandi161 – 163Combined sources3
Helixi165 – 185Combined sources21
Helixi186 – 188Combined sources3
Beta strandi190 – 198Combined sources9
Beta strandi208 – 210Combined sources3
Helixi213 – 222Combined sources10
Helixi233 – 244Combined sources12
Helixi246 – 248Combined sources3
Beta strandi255 – 259Combined sources5
Helixi262 – 264Combined sources3
Helixi268 – 272Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BGKX-ray1.60A/B1-278[»]
2BGLX-ray2.80A1-278[»]
2BGMX-ray2.00A1-278[»]
ProteinModelPortaliQ94KL8
SMRiQ94KL8
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ94KL8

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK19650

Family and domain databases

InterProiView protein in InterPro
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam
PRINTSiPR00081 GDHRDH
PR00080 SDRFAMILY
SUPFAMiSSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00061 ADH_SHORT, 1 hit

Sequencei

Sequence statusi: Fragment.

Q94KL8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSTSTPDSS TNRLQDKVAI ITGGAGGIGE TTAKLFVRYG AKVVIADIAD
60 70 80 90 100
DHGQKVCNNI GSPDVISFVH CDVTKDEDVR NLVDTTIAKH GKLDIMFGNV
110 120 130 140 150
GVLSTTPYSI LEAGNEDFKR VMDINVYGAF LVAKHAARVM IPAKKGSIVF
160 170 180 190 200
TASISSFTAG EGVSHVYTAT KHAVLGLTTS LCTELGEYGI RVNCVSPYIV
210 220 230 240 250
ASPLLTDVFG VDSSRVEELA HQAANLKGTL LRAEDVADAV AYLAGDESKY
260 270
VSGLNLVIDG GYTRTNPAFP TALKHGLA
Length:278
Mass (Da):29,253
Last modified:December 1, 2001 - v1
Checksum:iDB735A376E112375
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei2781

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF352734 mRNA Translation: AAK38664.1

Genome annotation databases

KEGGiag:AAK38664

Similar proteinsi

Entry informationi

Entry nameiSILD_PODPE
AccessioniPrimary (citable) accession number: Q94KL8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: December 1, 2001
Last modified: May 23, 2018
This is version 73 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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