ID   DXR_BLOPB               Reviewed;         397 AA.
AC   Q493C8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=BPEN_283;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the DXR family.
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DR   EMBL; CP000016; AAZ40914.1; -; Genomic_DNA.
DR   RefSeq; YP_277787.1; -.
DR   GeneID; 3562592; -.
DR   GenomeReviews; CP000016_GR; BPEN_283.
DR   KEGG; bpn:BPEN_283; -.
DR   HOGENOM; Q493C8; -.
DR   OMA; Q493C8; IHSMVEY.
DR   BioCyc; CBLO291272:BPEN_283-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    397       1-deoxy-D-xylulose 5-phosphate
FT                                reductoisomerase.
FT                                /FTId=PRO_1000020219.
FT   NP_BIND       7     36       NADP (By similarity).
FT   METAL       151    151       Divalent metal cation (By similarity).
FT   METAL       153    153       Divalent metal cation (By similarity).
FT   METAL       232    232       Divalent metal cation (By similarity).
FT   BINDING     126    126       Substrate (By similarity).
FT   BINDING     153    153       Substrate (By similarity).
FT   BINDING     187    187       Substrate (By similarity).
FT   BINDING     210    210       Substrate (By similarity).
FT   BINDING     232    232       Substrate (By similarity).
SQ   SEQUENCE   397 AA;  43728 MW;  CBB38A687381B052 CRC64;
     MQSLTILGST GSIGKATLSV IQQHTDKFFV HALVAKNNVA IMTEQCIAMS PKYACMISED
     AARILKKNLI TAGKYDIEVL SGVMHACELA STNDVDMVMS AIVGIAGLKP TFSALRAGKK
     ILLANKETLV TGGKLFMKEA NRYRACILPI DSEHNAIFQN LPEICQKSLG NTSLSECGIS
     RIVLTASGGI FFKTPQKQLT KITPEQACVH PNWSMGRKIS VDSATMMNKG LEYIEARHLF
     NAKPSEIEIL LHPQSIVHAM VYYSDGNVLA HLAPPDMRIP IAYAMAYPKR IGLKISSNID
     IYYLNKLHFD QLDNCSYPCF QLAIDADNCS QSATIILNAA NEIAVEAFLR KMISFTDIPD
     VIRRVLDAIN LNDPNDIEDI LYIDQKAREK AISICVI
//