ID   DXR_BUCAP               Reviewed;         398 AA.
AC   Q8K9S7;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 41.
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=BUsg_229;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67788.1; -; Genomic_DNA.
DR   RefSeq; NP_660577.1; -.
DR   HSSP; P45568; 1K5H.
DR   GeneID; 1005428; -.
DR   GenomeReviews; AE013218_GR; BUsg_229.
DR   KEGG; bas:BUsg229; -.
DR   HOGENOM; Q8K9S7; -.
DR   OMA; Q8K9S7; IHSMVEY.
DR   BioCyc; BAPH198804:BUSG229-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_0000163623.
FT   NP_BIND       7     36       NADP (By similarity).
FT   METAL       150    150       Divalent metal cation (By similarity).
FT   METAL       152    152       Divalent metal cation (By similarity).
FT   METAL       231    231       Divalent metal cation (By similarity).
FT   BINDING     125    125       Substrate (By similarity).
FT   BINDING     152    152       Substrate (By similarity).
FT   BINDING     186    186       Substrate (By similarity).
FT   BINDING     209    209       Substrate (By similarity).
FT   BINDING     231    231       Substrate (By similarity).
SQ   SEQUENCE   398 AA;  43727 MW;  386412F1393271B0 CRC64;
     MKKITVLGST GSIGISTLSI VKNNPSLFKV IVLVANKNSS MMLEQCEYFS PDWAIMKNKK
     SAHILKKRLK DKKIKTQVLS GNKAICQLAA LKESDLVISA IVGMAGLLPT LSAINAGKTI
     LLANKESLIV CGIIFMKALS SNKAKIFPID SEHNAIFQVL PKFVQKNLGK VNLKKNGVKS
     IILTASGGPF YNFKRENLSF VTPLEACSHP NWSMGRKISI DSATMINKGF EYAEARLLFN
     ASSSEIDILI HPQSIIHSMV EYIDGTILAQ LSVPDMKVAI SYAMSWPNRI SSGAKFLNFN
     KLSNLSFFKP DFIQFPCLKL AIDAFSQGQA AMTVLNAVNE VTVSAFLDSK ISFNKISEIN
     TDILMSSSFS EPVSVEEVLE IDKKTRIKSQ KKISSLIF
//