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DXR_TROW8
ID   DXR_TROW8               Reviewed;         368 AA.
AC   Q83IC8;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=TW099;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(2003).
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; BX251410; CAD66783.1; -; Genomic_DNA.
DR   RefSeq; WP_011096064.1; NC_004551.1.
DR   AlphaFoldDB; Q83IC8; -.
DR   SMR; Q83IC8; -.
DR   GeneID; 67387872; -.
DR   KEGG; tws:TW099; -.
DR   HOGENOM; CLU_035714_4_0_11; -.
DR   OMA; PIDSEHF; -.
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; 2.
DR   Pfam; PF08436; DXP_redisom_C; 1.
DR   Pfam; PF02670; DXP_reductoisom; 2.
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..368
FT                   /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase"
FT                   /id="PRO_0000163728"
FT   BINDING         7..36
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         125
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         127
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         194
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
SQ   SEQUENCE   368 AA;  39894 MW;  06F9E8FDE3100DF9 CRC64;
     MQRVIIVGST GSIGTQAIDF ILKNRDSFLV VGLAASTQTS LLREQAQVFG TKNTAQGASE
     AAELIEATEA DVVLNAITGA AGLLSTYATL KTGKRLALAN KESLIMGGKY FLDMTSFKGQ
     ITPVDSEHSA IAQAMKSGKF SEVNKLILTA SGGPFYDRES LEGITLKDAL DHPTWNMGPM
     ISINSATMFN KGLEIIEAHL LFGIPYSQID VVIHPQSIVH SMVEYKDGSV IAQASVADMT
     LPIGYALSWP NRALNAVRPL EWGARQRWDF LPPTENSMRS INLARRAGEA GGVYPAVLNA
     SNECAVEAFM AGKISFARII HVTETVFNLY TKQHTNRESA KNPIEVILEE DARTRELAKT
     VIENMSAD
 
 
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