P50163 (TRN2_DATST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tropinone reductase 2
EC=1.1.1.236

Alternative name(s):
Tropinone reductase II
Short name=TR-II

Gene names

Name:

TR2

Organism

Datura stramonium (Jimsonweed) (Common thornapple)

Taxonomic identifier

4076 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Datureae › Datura

Protein attributes

Sequence length	260 AA.
Sequence status	Complete.
Protein existence	Evidence 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
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	tropane alkaloid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro tropinone reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 260

260

Tropinone reductase 2

PRO_0000054786

Regions

Nucleotide binding

18 – 41

24

NADP

Nucleotide binding

192 – 196

5

NADP

Sites

Active site

159

1

Proton acceptor

Binding site

146

1

Substrate

Secondary structure

1

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260

Helix Strand Turn

Details...

Beta strand

11 – 16

6

Helix

20 – 31

12

Beta strand

35 – 41

7

Helix

43 – 55

13

Beta strand

59 – 64

6

Helix

70 – 83

14

Turn

84 – 86

3

Beta strand

90 – 93

4

Helix

103 – 105

3

Helix

108 – 118

11

Helix

120 – 135

16

Beta strand

137 – 144

8

Helix

147 – 149

3

Helix

157 – 176

20

Helix

178 – 180

3

Beta strand

182 – 189

8

Helix

195 – 200

6

Helix

204 – 215

12

Beta strand

217 – 219

3

Helix

225 – 236

12

Helix

238 – 240

3

Beta strand

247 – 251

5

Helix

254 – 256

3

Sequences

	Sequence		Length	Mass (Da)
	P50163 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 2DBF4963B2CCA303	FASTA	260	28,311
	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

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.

PIR

B48674.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IPE	X-ray	2.50	A/B	2-260	[»]
1IPF	X-ray	2.50	A/B	2-260	[»]
2AE1	X-ray	2.30	A	1-260	[»]
2AE2	X-ray	1.90	A/B	1-260	[»]

ProteinModelPortal

P50163.

SMR

P50163. Positions 2-260.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-13851.

BRENDA

1.1.1.236. 1839.

SABIO-RK

P50163.

UniPathway

UPA00330.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.
PR00080. SDRFAMILY.

PROSITE

PS00061. ADH_SHORT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P50163.

Entry information

Entry name

TRN2_DATST

Accession

Primary (citable) accession number: P50163

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program