Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P50162 (TRN1_DATST)

Last modified June 16, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Tropinone reductase 1
    EC=1.1.1.206
Alternative name(s):
    Tropinone reductase I
      Short name=TR-I
    Tropine dehydrogenase
Gene names
Name: TR1
OrganismDatura stramonium (Jimsonweed) (Common thornapple)
Taxonomic identifier4076 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Datureae › Datura

Hide | Top

Protein attributes

Sequence length273 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Catalyzes the stereospecific reduction of tropinone to tropine.

Catalytic activity

Tropine + NADP+ = tropinone + NADPH.

Pathway

Alkaloid biosynthesis; tropane alkaloid biosynthesis.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Hide | Top

Ontologies

Keywords
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

tropine dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 273273Tropinone reductase 1
PRO_0000054785

Regions

Nucleotide binding25 – 4925NADP

Sites

Active site1711Proton acceptor
Binding site1581Substrate

Secondary structure

1 ........................................ 273
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P50162-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 39A523EF04EA81F1

FASTA27329,617
        10         20         30         40         50         60 
MEESKVSMMN CNNEGRWSLK GTTALVTGGS KGIGYAIVEE LAGLGARVYT CSRNEKELDE 

        70         80         90        100        110        120 
CLEIWREKGL NVEGSVCDLL SRTERDKLMQ TVAHVFDGKL NILVNNAGVV IHKEAKDFTE 

       130        140        150        160        170        180 
KDYNIIMGTN FEAAYHLSQI AYPLLKASQN GNVIFLSSIA GFSALPSVSL YSASKGAINQ 

       190        200        210        220        230        240 
MTKSLACEWA KDNIRVNSVA PGVILTPLVE TAIKKNPHQK EEIDNFIVKT PMGRAGKPQE 

       250        260        270 
VSALIAFLCF PAASYITGQI IWADGGFTAN GGF

« Hide

Hide | Top

References

[1]"Two tropinone reductases with different stereospecificities are short-chain dehydrogenases evolved from a common ancestor."
Nakajima K., Hashimoto T., Yamada Y.
Proc. Natl. Acad. Sci. U.S.A. 90:9591-9595(1993) [PubMed: 8415746] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Root.
[2]"Crystal structures of two tropinone reductases: different reaction stereospecificities in the same protein fold."
Nakajima K., Yamashita A., Akama H., Nakatsu T., Kato H., Hashimoto T., Oda J., Yamada Y.
Proc. Natl. Acad. Sci. U.S.A. 95:4876-4881(1998) [PubMed: 9560196] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NADP.

Hide | Top

Cross-references

Sequence databases

L20473 mRNA. Translation: AAA33281.1.
PIRA48674.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1AE1X-ray2.40A/B1-273[»]
ModBaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MON-13848.
BRENDA1.1.1.206. 20628.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameTRN1_DATST
AccessionPrimary (citable) accession number: P50162
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents