ID   TRN1_DATST              Reviewed;         273 AA.
AC   P50162;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Tropinone reductase 1;
DE            EC=1.1.1.206;
DE   AltName: Full=Tropinone reductase I;
DE            Short=TR-I;
DE   AltName: Full=Tropine dehydrogenase;
GN   Name=TR1;
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], AND PARTIAL PROTEIN SEQUENCE.
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 (2.4 ANGSTROMS) IN COMPLEX WITH NADP.
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).
CC   -!- FUNCTION: Catalyzes the stereospecific reduction of tropinone to
CC       tropine.
CC   -!- CATALYTIC ACTIVITY: Tropine + 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.
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DR   EMBL; L20473; AAA33281.1; -; mRNA.
DR   PIR; A48674; A48674.
DR   PDB; 1AE1; X-ray; 2.40 A; A/B=1-273.
DR   PDBsum; 1AE1; -.
DR   BioCyc; MetaCyc:MON-13848; -.
DR   BRENDA; 1.1.1.206; 20628.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0050356; F:tropine dehydrogenase 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; Direct protein sequencing; NADP; Oxidoreductase.
FT   CHAIN         1    273       Tropinone reductase 1.
FT                                /FTId=PRO_0000054785.
FT   NP_BIND      25     49       NADP.
FT   ACT_SITE    171    171       Proton acceptor.
FT   BINDING     158    158       Substrate.
FT   STRAND       23     28
FT   HELIX        32     43
FT   STRAND       47     53
FT   HELIX        55     67
FT   STRAND       72     76
FT   HELIX        82     95
FT   STRAND      102    105
FT   TURN        115    117
FT   HELIX       120    130
FT   HELIX       132    148
FT   STRAND      150    156
FT   HELIX       159    161
FT   HELIX       169    189
FT   HELIX       190    192
FT   STRAND      194    201
FT   HELIX       220    229
FT   HELIX       238    249
FT   HELIX       251    253
FT   STRAND      260    264
FT   HELIX       267    269
SQ   SEQUENCE   273 AA;  29617 MW;  39A523EF04EA81F1 CRC64;
     MEESKVSMMN CNNEGRWSLK GTTALVTGGS KGIGYAIVEE LAGLGARVYT CSRNEKELDE
     CLEIWREKGL NVEGSVCDLL SRTERDKLMQ TVAHVFDGKL NILVNNAGVV IHKEAKDFTE
     KDYNIIMGTN FEAAYHLSQI AYPLLKASQN GNVIFLSSIA GFSALPSVSL YSASKGAINQ
     MTKSLACEWA KDNIRVNSVA PGVILTPLVE TAIKKNPHQK EEIDNFIVKT PMGRAGKPQE
     VSALIAFLCF PAASYITGQI IWADGGFTAN GGF
//