TRN2_DATST
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 03-AUG-2022, entry version 104.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Datureae; Datura.
OX NCBI_TaxID=4076;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Root;
RX PubMed=8415746; DOI=10.1073/pnas.90.20.9591;
RA Nakajima K., Hashimoto T., Yamada Y.;
RT "Two tropinone reductases with different stereospecificities are short-
RT 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 PubMed=9560196; DOI=10.1073/pnas.95.9.4876;
RA Nakajima K., Yamashita A., Akama H., Nakatsu T., Kato H., Hashimoto T.,
RA 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 SUBSTRATE.
RX PubMed=10387002; DOI=10.1021/bi9825044;
RA Yamashita A., Kato H., Wakatsuki S., Tomizaki T., Nakatsu T., Nakajima K.,
RA Hashimoto T., Yamada Y., Oda J.;
RT "Structure of tropinone reductase-II complexed with NADP+ and pseudotropine
RT at 1.9 A resolution: implication for stereospecific substrate binding and
RT catalysis.";
RL Biochemistry 38:7630-7637(1999).
CC -!- FUNCTION: Catalyzes the stereospecific reduction of tropinone to
CC pseudotropine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + pseudotropine = H(+) + NADPH + tropinone;
CC Xref=Rhea:RHEA:24244, ChEBI:CHEBI:15378, ChEBI:CHEBI:57493,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57851, ChEBI:CHEBI:58349;
CC EC=1.1.1.236;
CC -!- PATHWAY: Alkaloid biosynthesis; tropane alkaloid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10387002}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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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 AlphaFoldDB; P50163; -.
DR SMR; P50163; -.
DR KEGG; ag:AAA33282; -.
DR BioCyc; MetaCyc:MON-13851; -.
DR BRENDA; 1.1.1.236; 1839.
DR SABIO-RK; P50163; -.
DR UniPathway; UPA00330; -.
DR EvolutionaryTrace; P50163; -.
DR GO; GO:0050358; F:tropinone reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0009710; P:tropane alkaloid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR045000; TR.
DR PANTHER; PTHR42898; PTHR42898; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase.
FT CHAIN 1..260
FT /note="Tropinone reductase 2"
FT /id="PRO_0000054786"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT BINDING 18..41
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10387002"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10387002"
FT BINDING 192..196
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10387002"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:2AE2"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:2AE2"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:2AE2"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:2AE2"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:2AE2"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:2AE2"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:2AE2"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:2AE2"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:2AE2"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:2AE2"
FT HELIX 120..135
FT /evidence="ECO:0007829|PDB:2AE2"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:2AE2"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:2AE2"
FT HELIX 157..176
FT /evidence="ECO:0007829|PDB:2AE2"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:2AE2"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:2AE2"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:2AE2"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:2AE2"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2AE1"
FT HELIX 225..236
FT /evidence="ECO:0007829|PDB:2AE2"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2AE2"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:2AE2"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:2AE2"
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
