ID TRN2_DATST Reviewed; 260 AA. AC P50163; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 16-JUN-2009, entry version 59. DE RecName: Full=Tropinone reductase 2; DE EC=1.1.1.236; DE AltName: Full=Tropinone reductase II; DE Short=TR-II; GN Name=TR2; OS Datura stramonium (Jimsonweed) (Common thornapple). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Datureae; OC Datura. OX NCBI_TaxID=4076; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Root; RX MEDLINE=94022421; PubMed=8415746; DOI=10.1073/pnas.90.20.9591; RA Nakajima K., Hashimoto T., Yamada Y.; RT "Two tropinone reductases with different stereospecificities are RT short-chain dehydrogenases evolved from a common ancestor."; RL Proc. Natl. Acad. Sci. U.S.A. 90:9591-9595(1993). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX MEDLINE=98226735; PubMed=9560196; DOI=10.1073/pnas.95.9.4876; RA Nakajima K., Yamashita A., Akama H., Nakatsu T., Kato H., RA Hashimoto T., Oda J., Yamada Y.; RT "Crystal structures of two tropinone reductases: different reaction RT stereospecificities in the same protein fold."; RL Proc. Natl. Acad. Sci. U.S.A. 95:4876-4881(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NADP AND RP SUBSTRATE. RX MEDLINE=99316165; PubMed=10387002; DOI=10.1021/bi9825044; RA Yamashita A., Kato H., Wakatsuki S., Tomizaki T., Nakatsu T., RA Nakajima K., Hashimoto T., Yamada Y., Oda J.; RT "Structure of tropinone reductase-II complexed with NADP+ and RT pseudotropine at 1.9 A resolution: implication for stereospecific RT substrate binding and catalysis."; RL Biochemistry 38:7630-7637(1999). CC -!- FUNCTION: Catalyzes the stereospecific reduction of tropinone to CC pseudotropine. CC -!- CATALYTIC ACTIVITY: Pseudotropine + NADP(+) = tropinone + NADPH. CC -!- PATHWAY: Alkaloid biosynthesis; tropane alkaloid biosynthesis. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L20474; AAA33282.1; -; mRNA. DR PIR; B48674; B48674. DR PDB; 1IPE; X-ray; 2.50 A; A/B=2-260. DR PDB; 1IPF; X-ray; 2.50 A; A/B=2-260. DR PDB; 2AE1; X-ray; 2.30 A; A=1-260. DR PDB; 2AE2; X-ray; 1.90 A; A/B=1-260. DR PDBsum; 1IPE; -. DR PDBsum; 1IPF; -. DR PDBsum; 2AE1; -. DR PDBsum; 2AE2; -. DR BioCyc; MetaCyc:MON-13851; -. DR BRENDA; 1.1.1.236; 20628. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0050358; F:tropinone reductase activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR19410; ADH_short_C2; 1. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW 3D-structure; NADP; Oxidoreductase. FT CHAIN 1 260 Tropinone reductase 2. FT /FTId=PRO_0000054786. FT NP_BIND 18 41 NADP. FT NP_BIND 192 196 NADP. FT ACT_SITE 159 159 Proton acceptor. FT BINDING 146 146 Substrate. FT STRAND 11 15 FT HELIX 20 30 FT TURN 31 33 FT STRAND 35 41 FT HELIX 43 55 FT STRAND 60 64 FT HELIX 70 83 FT TURN 84 86 FT STRAND 90 93 FT HELIX 103 105 FT HELIX 108 118 FT HELIX 120 134 FT STRAND 137 144 FT HELIX 147 149 FT HELIX 157 176 FT HELIX 178 180 FT STRAND 182 189 FT HELIX 204 215 FT STRAND 217 219 FT HELIX 225 236 FT HELIX 238 240 FT STRAND 247 251 FT HELIX 254 256 SQ SEQUENCE 260 AA; 28311 MW; 2DBF4963B2CCA303 CRC64; MAGRWNLEGC TALVTGGSRG IGYGIVEELA SLGASVYTCS RNQKELNDCL TQWRSKGFKV EASVCDLSSR SERQELMNTV ANHFHGKLNI LVNNAGIVIY KEAKDYTVED YSLIMSINFE AAYHLSVLAH PFLKASERGN VVFISSVSGA LAVPYEAVYG ATKGAMDQLT RCLAFEWAKD NIRVNGVGPG VIATSLVEMT IQDPEQKENL NKLIDRCALR RMGEPKELAA MVAFLCFPAA SYVTGQIIYV DGGLMANCGF //