ID   DXR_MENPI               Reviewed;         470 AA.
AC   Q9XES0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase, chloroplastic;
DE            Short=1-deoxyxylulose-5-phosphate reductoisomerase;
DE            Short=DXP reductoisomerase;
DE            EC=1.1.1.267;
DE   AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase;
DE   Flags: Precursor;
GN   Name=DXR;
OS   Mentha piperita (Peppermint) (Mentha aquatica x Mentha spicata).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Menthinae;
OC   Mentha.
OX   NCBI_TaxID=34256;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Oil gland;
RX   PubMed=10222052; DOI=10.1006/abbi.1999.1168;
RA   Lange B.M., Croteau R.;
RT   "Isoprenoid biosynthesis via a mevalonate-independent pathway in plants:
RT   cloning and heterologous expression of 1-deoxy-D-xylulose-5-phosphate
RT   reductoisomerase from peppermint.";
RL   Arch. Biochem. Biophys. 365:170-174(1999).
RN   [2]
RP   SEQUENCE REVISION.
RA   Lange B.M., Croteau R.;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction of
CC       1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-
CC       phosphate (MEP). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-
CC         xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792,
CC         ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267;
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 1/6.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the DXR family. {ECO:0000305}.
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DR   EMBL; AF116825; AAD24768.2; -; mRNA.
DR   AlphaFoldDB; Q9XES0; -.
DR   SMR; Q9XES0; -.
DR   PRIDE; Q9XES0; -.
DR   UniPathway; UPA00056; UER00092.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070402; F:NADPH binding; IEA:InterPro.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00183; DXP_reductoisom; 1.
DR   InterPro; IPR003821; DXP_reductoisomerase.
DR   InterPro; IPR013644; DXP_reductoisomerase_C.
DR   InterPro; IPR013512; DXP_reductoisomerase_N.
DR   InterPro; IPR026877; DXPR_C.
DR   InterPro; IPR036169; DXPR_C_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR30525; PTHR30525; 1.
DR   Pfam; PF08436; DXP_redisom_C; 1.
DR   Pfam; PF02670; DXP_reductoisom; 1.
DR   Pfam; PF13288; DXPR_C; 1.
DR   PIRSF; PIRSF006205; Dxp_reductismrs; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF69055; SSF69055; 1.
DR   TIGRFAMs; TIGR00243; Dxr; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Isoprene biosynthesis; Metal-binding; NADP; Oxidoreductase;
KW   Plastid; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..470
FT                   /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase,
FT                   chloroplastic"
FT                   /id="PRO_0000007396"
FT   BINDING         80..109
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         272
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         294
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         294
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   470 AA;  51034 MW;  3C02B844923CD591 CRC64;
     MAPTEIKTLS FLDSSKSNYN LNPLKFQGGF AFKRKDSGCT AAKRVHCSAQ SQSPPPAWPG
     RAFPEPGRMT WEGPKPISVI GSTGSIGTQT LDIVAENPDK FRIVALAAGS NVTLLADQVK
     AFKPKLVSVK DESLISELKE ALAGFEDMPE IIPGEQGMIE VARHPDAVTV VTGIVGCAGL
     KPTVAAIEAG KDIALANKET LIAGGPFVLP LAKKHNVKIL PADSEHSAIF QCIQGLPEGA
     LRRIILTASG GAFRDLPVEK LKEVKVADAL KHPNWNMGKK ITVDSATLFN KGLEVIEAHY
     LFGAEYDDIE IVIHPQSIIH SMVETQDSSV LAQLGWPDMR LPILYTLSWP ERIYCSEITW
     PRLDLCKVDL TFKKPDNVKY PSMDLAYAAG RAGGTMTGVL SAANEKAVEM FIDEKIGYLD
     IFKVVELTCD KHRSEMAVSP SLEEIVHYDQ WARDYAATVL KSAGLSPALV