ID   DXR_BURTA               Reviewed;         398 AA.
AC   Q2SWZ2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase;
DE            Short=DXP reductoisomerase;
DE            EC=1.1.1.267;
DE   AltName: Full=1-deoxyxylulose-5-phosphate reductoisomerase;
DE   AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase;
GN   Name=dxr; OrderedLocusNames=BTH_I2033;
OS   Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 /
OS   CIP 106301).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R.,
RA   Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D.,
RA   Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P.,
RA   Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F.,
RA   Roberts K., Hatch B., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction
CC       of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol
CC       4-phosphate (MEP) (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2-C-methyl-D-erythritol 4-phosphate + NADP(+)
CC       = 1-deoxy-D-xylulose 5-phosphate + NADPH.
CC   -!- COFACTOR: Divalent cation (By similarity).
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl-PP biosynthesis via
CC       DXP pathway; isopentenyl-PP from 1-deoxy-D-xylulose 5-phosphate:
CC       step 1/6.
CC   -!- SIMILARITY: Belongs to the DXR family.
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DR   EMBL; CP000086; ABC36321.1; -; Genomic_DNA.
DR   RefSeq; YP_442557.1; -.
DR   GeneID; 3846968; -.
DR   GenomeReviews; CP000086_GR; BTH_I2033.
DR   KEGG; bte:BTH_I2033; -.
DR   TIGR; BTH_I2033; -.
DR   HOGENOM; Q2SWZ2; -.
DR   OMA; Q2SWZ2; IHSMVEY.
DR   BioCyc; BTHA271848:BTH_I2033-MON; -.
DR   GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisome...; IEA:HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00183; -; 1.
DR   InterPro; IPR003821; DXP_reductoisomerase.
DR   InterPro; IPR013644; DXP_reductoisomerase_C.
DR   InterPro; IPR013512; DXP_reductoisomerase_N.
DR   Pfam; PF08436; DXP_redisom_C; 1.
DR   Pfam; PF02670; DXP_reductoisom; 1.
DR   PIRSF; PIRSF006205; Dxp_reductismrs; 1.
DR   TIGRFAMs; TIGR00243; Dxr; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isoprene biosynthesis; Metal-binding; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    398       1-deoxy-D-xylulose 5-phosphate
FT                                reductoisomerase.
FT                                /FTId=PRO_1000020233.
FT   NP_BIND       8     37       NADP (By similarity).
FT   METAL       151    151       Divalent metal cation (By similarity).
FT   METAL       153    153       Divalent metal cation (By similarity).
FT   METAL       224    224       Divalent metal cation (By similarity).
FT   BINDING     126    126       Substrate (By similarity).
FT   BINDING     153    153       Substrate (By similarity).
FT   BINDING     179    179       Substrate (By similarity).
FT   BINDING     202    202       Substrate (By similarity).
FT   BINDING     224    224       Substrate (By similarity).
SQ   SEQUENCE   398 AA;  41724 MW;  128F3E70D3E00690 CRC64;
     MQKRLTLLGS TGSIGDSTLD VVTRHPERFA VHALTAHRNG DKLVAQCLRF APDVAVVGDA
     ETAARVEAQL RAAGSKTQVA YGKQALVDVS KSDGCDTVVA AIVGAAGLAP SLAAARAGKR
     ILLANKEALV MSGAIFMDAV RDHGAILLPV DSEHNAIFQC MPRDAAEHGG IAKIIVTASG
     GPFRTREPVT LASVTPDEAC KHPNWVMGRK ISVDSATMMN KGLEVIEAHW LFGLPSERID
     VLIHPQSVIH SLVSYCDGSV LAQLGNPDMR TPIAHALAFP ERVDAGVAQL DLAQIATLTF
     EKPDYARFPC LALAIDALEA GGVASAALNA ANEIAVDAFL SRRIRFTAIA QTVDAVLSGL
     SNRTPSGLDD VIGADADARR AATAFIDKLP APSVERAA
//