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P50163 (TRN2_DATST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tropinone reductase 2

EC=1.1.1.236
Alternative name(s):
Tropinone reductase II
Short name=TR-II
Gene names
Name:TR2
OrganismDatura stramonium (Jimsonweed) (Common thornapple)
Taxonomic identifier4076 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeDatureaeDatura

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the stereospecific reduction of tropinone to pseudotropine.

Catalytic activity

Pseudotropine + NADP+ = tropinone + NADPH.

Pathway

Alkaloid biosynthesis; tropane alkaloid biosynthesis.

Subunit structure

Homodimer.

Sequence similarities

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

Ontologies

Keywords
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processtropane alkaloid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functiontropinone reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 260260Tropinone reductase 2
PRO_0000054786

Regions

Nucleotide binding18 – 4124NADP
Nucleotide binding192 – 1965NADP

Sites

Active site1591Proton acceptor
Binding site1461Substrate

Secondary structure

.............................................. 260
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50163 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 2DBF4963B2CCA303

FASTA26028,311
        10         20         30         40         50         60 
MAGRWNLEGC TALVTGGSRG IGYGIVEELA SLGASVYTCS RNQKELNDCL TQWRSKGFKV 

        70         80         90        100        110        120 
EASVCDLSSR SERQELMNTV ANHFHGKLNI LVNNAGIVIY KEAKDYTVED YSLIMSINFE 

       130        140        150        160        170        180 
AAYHLSVLAH PFLKASERGN VVFISSVSGA LAVPYEAVYG ATKGAMDQLT RCLAFEWAKD 

       190        200        210        220        230        240 
NIRVNGVGPG VIATSLVEMT IQDPEQKENL NKLIDRCALR RMGEPKELAA MVAFLCFPAA 

       250        260 
SYVTGQIIYV DGGLMANCGF 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[3]"Structure of tropinone reductase-II complexed with NADP+ and pseudotropine at 1.9 A resolution: implication for stereospecific substrate binding and catalysis."
Yamashita A., Kato H., Wakatsuki S., Tomizaki T., Nakatsu T., Nakajima K., Hashimoto T., Yamada Y., Oda J.
Biochemistry 38:7630-7637(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L20474 mRNA. Translation: AAA33282.1.
PIRB48674.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IPEX-ray2.50A/B2-260[»]
1IPFX-ray2.50A/B2-260[»]
2AE1X-ray2.30A1-260[»]
2AE2X-ray1.90A/B1-260[»]
ProteinModelPortalP50163.
SMRP50163. Positions 2-260.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13851.
BRENDA1.1.1.236. 1839.
SABIO-RKP50163.
UniPathwayUPA00330.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP50163.

Entry information

Entry nameTRN2_DATST
AccessionPrimary (citable) accession number: P50163
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 19, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways