Reviewed, UniProtKB/Swiss-Prot P50163 (TRN2_DATST)

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

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

Protein attributes

Sequence length	260 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	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 – 15

5

Helix

20 – 30

11

Turn

31 – 33

3

Beta strand

35 – 41

7

Helix

43 – 55

13

Beta strand

60 – 64

5

Helix

70 – 83

14

Turn

84 – 86

3

Beta strand

90 – 93

4

Helix

103 – 105

3

Helix

108 – 118

11

Helix

120 – 134

15

Beta strand

137 – 144

8

Helix

147 – 149

3

Helix

157 – 176

20

Helix

178 – 180

3

Beta strand

182 – 189

8

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)
	P50163-1 [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: 8415746] [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: 9560196] [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: 10387002] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L20474 mRNA. Translation: AAA33282.1.

PIR

B48674.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13851.

BRENDA

1.1.1.236. 20628.

Family and domain databases

InterPro

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

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR19410. ADH_short_C2. 1 hit.

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.
PR00080. SDRFAMILY.

PROSITE

PS00061. ADH_SHORT. 1 hit.
[Graphical view]

ProtoNet

Search...

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:	June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)