ID   DXR_ORIVU               Reviewed;         106 AA.
AC   H8ZW44;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase {ECO:0000303|PubMed:22387534};
DE            EC=1.1.1.267 {ECO:0000250|UniProtKB:P45568};
DE   Flags: Fragment;
GN   Name=DXR {ECO:0000303|PubMed:22387534};
OS   Origanum vulgare (Wild marjoram).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Origanum.
OX   NCBI_TaxID=39352;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. LNIV008;
RX   PubMed=22387534; DOI=10.1016/j.ympev.2012.02.010;
RA   Curto M.A., Puppo P., Ferreira D., Nogueira M., Meimberg H.;
RT   "Development of phylogenetic markers from single-copy nuclear genes for
RT   multi locus, species level analyses in the mint family (Lamiaceae).";
RL   Mol. Phylogenet. Evol. 63:758-767(2012).
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   -!- SIMILARITY: Belongs to the DXR family. {ECO:0000305}.
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DR   EMBL; JN587739; AFD50369.1; -; Genomic_DNA.
DR   SMR; H8ZW44; -.
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:InterPro.
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   InterPro; IPR003821; DXP_reductoisomerase.
DR   InterPro; IPR013644; DXP_reductoisomerase_C.
DR   PANTHER; PTHR30525; PTHR30525; 1.
DR   Pfam; PF08436; DXP_redisom_C; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Isomerase; Metal-binding; Oxidoreductase; Plastid.
FT   CHAIN           <1..>106
FT                   /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase"
FT                   /id="PRO_0000453305"
FT   REGION          65..71
FT                   /note="Binding to substrate phosphate group"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         3
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         5
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         5
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         29
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         74
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:AFD50369.1"
FT   NON_TER         106
FT                   /evidence="ECO:0000312|EMBL:AFD50369.1"
SQ   SEQUENCE   106 AA;  11723 MW;  EEB7307518AF1A80 CRC64;
     PADSEHSAIF QCIQGLPEGA LRRIILTASG GAFRDLPVEK LKEVKVADAL KHPNWNMGKK
     ITVDSATLFN KGLEVIEAHY LFGAEYDDIE IVIHPQSIIH SMVETQ