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Protein

Secoisolariciresinol dehydrogenase

Gene
N/A
Organism
Podophyllum peltatum (Mayapple)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei47 – 471NAD
Binding sitei73 – 731NAD; via amide nitrogen
Binding sitei99 – 991NAD; via carbonyl oxygen
Binding sitei104 – 1041Substrate; via carbonyl oxygen
Binding sitei164 – 1641Substrate; via amide nitrogen
Active sitei167 – 1671Proton donor/acceptor2 Publications
Binding sitei171 – 1711NAD

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi23 – 286NAD

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi153 – 1531S → A: Strongly reduces enzyme activity. 1 Publication
Mutagenesisi167 – 1671Y → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi171 – 1711K → A: Abolishes enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›278›278Secoisolariciresinol dehydrogenasePRO_0000424207Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1
278
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni13 – 164Combined sources
Beta strandi18 – 236Combined sources
Helixi27 – 3812Combined sources
Beta strandi42 – 487Combined sources
Helixi50 – 6011Combined sources
Turni63 – 653Combined sources
Beta strandi66 – 705Combined sources
Helixi76 – 9015Combined sources
Beta strandi95 – 984Combined sources
Turni110 – 1123Combined sources
Helixi115 – 12511Combined sources
Helixi127 – 14014Combined sources
Turni141 – 1444Combined sources
Beta strandi146 – 1516Combined sources
Helixi154 – 1563Combined sources
Beta strandi161 – 1633Combined sources
Helixi165 – 18521Combined sources
Helixi186 – 1883Combined sources
Beta strandi190 – 1989Combined sources
Beta strandi208 – 2103Combined sources
Helixi213 – 22210Combined sources
Helixi233 – 24412Combined sources
Helixi246 – 2483Combined sources
Beta strandi255 – 2595Combined sources
Helixi262 – 2643Combined sources
Helixi268 – 2725Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ94KL8.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK19650.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei278 – 2781

Sequence databases

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

Genome annotation databases

KEGGiag:AAK38664.

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAK38664.

Phylogenomic databases

KOiK19650.

Enzyme and pathway databases

BRENDAi1.1.1.331. 4929.

Miscellaneous databases

EvolutionaryTraceiQ94KL8.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSILD_PODPE
AccessioniPrimary (citable) accession number: Q94KL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.