DXR_PSEMY
ID DXR_PSEMY Reviewed; 394 AA.
AC A4XWT5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183};
DE Short=DXP reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183};
DE EC=1.1.1.267 {ECO:0000255|HAMAP-Rule:MF_00183};
DE AltName: Full=1-deoxyxylulose-5-phosphate reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183};
DE AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00183};
GN Name=dxr {ECO:0000255|HAMAP-Rule:MF_00183}; OrderedLocusNames=Pmen_3047;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) 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:0000255|HAMAP-Rule:MF_00183}.
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:0000255|HAMAP-Rule:MF_00183};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00183};
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:0000255|HAMAP-Rule:MF_00183}.
CC -!- SIMILARITY: Belongs to the DXR family. {ECO:0000255|HAMAP-
CC Rule:MF_00183}.
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DR EMBL; CP000680; ABP85801.1; -; Genomic_DNA.
DR RefSeq; WP_012019183.1; NC_009439.1.
DR AlphaFoldDB; A4XWT5; -.
DR SMR; A4XWT5; -.
DR STRING; 399739.Pmen_3047; -.
DR EnsemblBacteria; ABP85801; ABP85801; Pmen_3047.
DR KEGG; pmy:Pmen_3047; -.
DR PATRIC; fig|399739.8.peg.3093; -.
DR eggNOG; COG0743; Bacteria.
DR HOGENOM; CLU_035714_0_1_6; -.
DR OMA; PIDSEHF; -.
DR OrthoDB; 1200722at2; -.
DR UniPathway; UPA00056; UER00092.
DR GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:UniProtKB-UniRule.
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 GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Isoprene biosynthesis; Metal-binding; NADP; Oxidoreductase.
FT CHAIN 1..394
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase"
FT /id="PRO_1000020291"
FT BINDING 10..39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 153
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 155
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 229
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
SQ SEQUENCE 394 AA; 42330 MW; 1DFEB36292A5BD64 CRC64;
MSTVQQITVL GATGSIGLST LDVIARHPER YAVFALSGFS RLAELETLCV QHRPRYVVVP
DAAAAHALQG SLRAAALPTE VLVGEEGLCA VAGHGEVDCV MAAIVGAAGL RPTLAAVQAG
KKVLLANKEA LVMSGALFMQ AVRESGATLL PIDSEHNAIF QCLPGDYGRG LQAVGVRRVL
LTASGGPFRE TPLAELERVT PEQACAHPNW SMGRKISVDS ASMMNKGLEL IEACWLFDAR
PEQIEVVIHR QSVIHSLVDY VDGSVLAQLG NPDMRTPIAH ALAWPQRIDS GVSPLDLFAI
GRLDFERPDE QRFPCLRLAR EAAQVGGSAP AMLNAANEVA VDAFLQRRIR FSDIARMIEF
VLNAESARAV EALDAVFEAD RRARALAGEW LARH
