ID   DXR_THYVU               Reviewed;         211 AA.
AC   A0A1U9X9N3;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase {ECO:0000303|PubMed:28365519};
DE            EC=1.1.1.267 {ECO:0000250|UniProtKB:P45568};
DE   Flags: Fragment;
GN   Name=DXR {ECO:0000303|PubMed:28365519};
OS   Thymus vulgaris (Thyme).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Thymus.
OX   NCBI_TaxID=49992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY JASMONIC
RP   ACID; SALICYLIC ACID AND UV-C.
RX   PubMed=28365519; DOI=10.1016/j.plaphy.2017.03.016;
RA   Majdi M., Malekzadeh-Mashhady A., Maroufi A., Crocoll C.;
RT   "Tissue-specific gene-expression patterns of genes associated with
RT   thymol/carvacrol biosynthesis in thyme (Thymus vulgaris L.) and their
RT   differential changes upon treatment with abiotic elicitors.";
RL   Plant Physiol. Biochem. 115:152-162(2017).
CC   -!- FUNCTION: Enzyme of the plastid non-mevalonate pathway for isoprenoid
CC       biosynthesis that catalyzes the NADP-dependent rearrangement and
CC       reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-
CC       erythritol 4-phosphate (MEP). Required for chloroplast development.
CC       {ECO:0000250|UniProtKB:Q9XFS9}.
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         Evidence={ECO:0000250|UniProtKB:P45568};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13719;
CC         Evidence={ECO:0000250|UniProtKB:P45568};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:P45568};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 1/6. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000250|UniProtKB:Q9XFS9}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in flowers and, to a lower extent,
CC       in leaves. {ECO:0000269|PubMed:28365519}.
CC   -!- INDUCTION: Induced by jasmonic acid (MeJA), salicylic acid (SA) and UV-
CC       C irradiation. {ECO:0000269|PubMed:28365519}.
CC   -!- SIMILARITY: Belongs to the DXR family. {ECO:0000305}.
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DR   EMBL; KY621335; AQY77498.1; -; mRNA.
DR   SMR; A0A1U9X9N3; -.
DR   UniPathway; UPA00056; UER00092.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR   GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR   GO; GO:0010225; P:response to UV-C; IEP:UniProtKB.
DR   InterPro; IPR003821; DXP_reductoisomerase.
DR   InterPro; IPR013644; DXP_reductoisomerase_C.
DR   InterPro; IPR026877; DXPR_C.
DR   InterPro; IPR036169; DXPR_C_sf.
DR   PANTHER; PTHR30525; PTHR30525; 1.
DR   Pfam; PF08436; DXP_redisom_C; 1.
DR   Pfam; PF13288; DXPR_C; 1.
DR   SUPFAM; SSF69055; SSF69055; 1.
DR   TIGRFAMs; TIGR00243; Dxr; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Isomerase; Metal-binding; Oxidoreductase; Plastid.
FT   CHAIN           <1..>211
FT                   /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase"
FT                   /id="PRO_0000453304"
FT   REGION          76..82
FT                   /note="Binding to substrate phosphate group"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         14
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         16
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         85
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:AQY77498.1"
FT   NON_TER         211
FT                   /evidence="ECO:0000312|EMBL:AQY77498.1"
SQ   SEQUENCE   211 AA;  23535 MW;  7285A7EEDE280489 CRC64;
     PLAKKHNVKI LPADSEHSAI FQCIQGLPEG ALRRIILTAS GGAFRDLPVE KLKEVKVADA
     LKHPNWNMGK KITVDSATLF NKGLEVIEAH YLFGAEYDDI EIVIHPQSII HSMVETQDSS
     VLAQLGWPDM RLPILYTLSW PERVYCSEIT WPRLDLCNVD LTFKKPDHVK YPSMDLAYAA
     GRAGGTMTGV LSAANEKAVE MFIDEKISYL D