TRN1_DATST
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 03-AUG-2022, entry version 110.
DE RecName: Full=Tropinone reductase 1 {ECO:0000303|PubMed:8415746};
DE EC=1.1.1.206 {ECO:0000269|PubMed:8415746};
DE AltName: Full=Tropine dehydrogenase;
DE AltName: Full=Tropinone reductase I;
DE Short=TR-I;
GN Name=TR1 {ECO:0000303|PubMed:8415746};
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], PARTIAL PROTEIN SEQUENCE, AND CATALYTIC
RP ACTIVITY.
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19027726; DOI=10.1016/j.cbi.2008.10.040;
RA Persson B., Kallberg Y., Bray J.E., Bruford E., Dellaporta S.L.,
RA Favia A.D., Duarte R.G., Joernvall H., Kavanagh K.L., Kedishvili N.,
RA Kisiela M., Maser E., Mindnich R., Orchard S., Penning T.M., Thornton J.M.,
RA Adamski J., Oppermann U.;
RT "The SDR (short-chain dehydrogenase/reductase and related enzymes)
RT nomenclature initiative.";
RL Chem. Biol. Interact. 178:94-98(2009).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NADP, AND ACTIVE
RP SITE.
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).
CC -!- FUNCTION: Catalyzes the stereospecific reduction of tropinone to
CC tropine. {ECO:0000269|PubMed:8415746}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + tropine = H(+) + NADPH + tropinone;
CC Xref=Rhea:RHEA:18357, ChEBI:CHEBI:15378, ChEBI:CHEBI:57554,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57851, ChEBI:CHEBI:58349;
CC EC=1.1.1.206; Evidence={ECO:0000269|PubMed:8415746};
CC -!- PATHWAY: Alkaloid biosynthesis; tropane alkaloid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9560196}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. SDR65C subfamily. {ECO:0000305}.
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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 AlphaFoldDB; P50162; -.
DR SMR; P50162; -.
DR KEGG; ag:AAA33281; -.
DR BioCyc; MetaCyc:MON-13848; -.
DR BRENDA; 1.1.1.206; 1839.
DR SABIO-RK; P50162; -.
DR UniPathway; UPA00330; -.
DR EvolutionaryTrace; P50162; -.
DR GO; GO:0050356; F:tropine dehydrogenase 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; Direct protein sequencing; NADP; Oxidoreductase.
FT CHAIN 1..273
FT /note="Tropinone reductase 1"
FT /id="PRO_0000054785"
FT ACT_SITE 171
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:9560196"
FT BINDING 25..49
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:9560196"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9560196"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:1AE1"
FT HELIX 32..43
FT /evidence="ECO:0007829|PDB:1AE1"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:1AE1"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:1AE1"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1AE1"
FT HELIX 82..95
FT /evidence="ECO:0007829|PDB:1AE1"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:1AE1"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1AE1"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:1AE1"
FT HELIX 132..148
FT /evidence="ECO:0007829|PDB:1AE1"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:1AE1"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1AE1"
FT HELIX 169..189
FT /evidence="ECO:0007829|PDB:1AE1"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1AE1"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:1AE1"
FT HELIX 207..215
FT /evidence="ECO:0007829|PDB:1AE1"
FT HELIX 220..229
FT /evidence="ECO:0007829|PDB:1AE1"
FT HELIX 238..249
FT /evidence="ECO:0007829|PDB:1AE1"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:1AE1"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:1AE1"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:1AE1"
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
