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UniProtKB/Swiss-Prot entry P50162

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TRN1_DATST
Primary accession number P50162
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 59)
Name and origin of the protein
Protein name Tropinone reductase 1
Synonyms EC 1.1.1.206
Tropinone reductase I
TR-I
Tropine dehydrogenase
Gene name
Name: TR1
From
Datura stramonium (Jimsonweed) (Common thornapple) [TaxID: 4076] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; asterids; lamiids; Solanales; Solanaceae; Solanoideae; Datureae; Datura.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Root;
PubMed=8415746 [NCBI, ExPASy, EBI, Israel, Japan]
Nakajima K., Hashimoto T., Yamada Y.;
"Two tropinone reductases with different stereospecificities are short-chain dehydrogenases evolved from a common ancestor.";
Proc. Natl. Acad. Sci. U.S.A. 90:9591-9595(1993).
[2]
 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NADP.
DOI=10.1073/pnas.95.9.4876; PubMed=9560196 [NCBI, ExPASy, EBI, Israel, Japan]
Nakajima K., Yamashita A., Akama H., Nakatsu T., Kato H., Hashimoto T., Oda J., Yamada Y.;
"Crystal structures of two tropinone reductases: different reaction stereospecificities in the same protein fold.";
Proc. Natl. Acad. Sci. U.S.A. 95:4876-4881(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L20473; AAA33281.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A48674; A48674.
3D structure databases
PDB
1AE1; X-ray; 2.40 A; A/B=1-273.[ExPASy / RCSB / EBI]
PDBsum 1AE1; -.
ModBase P50162.
Enzyme and pathway databases
BioCyc MetaCyc:MON-13848; -.
Ontologies
GO
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0050356; Molecular function: tropine dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR19410; ADH_short_C2; 1.
Pfam PF00106; adh_short; 1.
Pfam graphical view of domain structure.
PRINTS PR00081; GDHRDH.
PR00080; SDRFAMILY.
PROSITE PS00061; ADH_SHORT; 1.
Other
ProtoNet P50162.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   273  273     Tropinone reductase 1. PRO_0000054785
NP_BIND   25    49  25     NADP. 
ACT_SITE   171   171        Proton acceptor. 
BINDING   158   158        Substrate. 
STRAND   23    28  6      
HELIX   32    43  12      
STRAND   47    53  7      
HELIX   55    67  13      
STRAND   72    76  5      
HELIX   82    95  14      
STRAND   102   105  4      
TURN   115   117  3      
HELIX   120   130  11      
HELIX   132   148  17      
STRAND   150   156  7      
HELIX   159   161  3      
HELIX   169   189  21      
HELIX   190   192  3      
STRAND   194   201  8      
HELIX   220   229  10      
HELIX   238   249  12      
HELIX   251   253  3      
STRAND   260   264  5      
HELIX   267   269  3      
Sequence information
Length: 273 AA [This is the length of the unprocessed precursor] Molecular weight: 29617 Da [This is the MW of the unprocessed precursor] CRC64: 39A523EF04EA81F1 [This is a checksum on the sequence] 
        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
P50162 in FASTA format

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