ID   DXR_BAUCH               Reviewed;         398 AA.
AC   Q1LSV3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
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=BCI_0531;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
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; CP000238; ABF14058.1; -; Genomic_DNA.
DR   RefSeq; YP_588961.1; -.
DR   GeneID; 4056432; -.
DR   GenomeReviews; CP000238_GR; BCI_0531.
DR   KEGG; bci:BCI_0531; -.
DR   HOGENOM; Q1LSV3; -.
DR   OMA; Q1LSV3; IHSMVEY.
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_1000020218.
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;  43611 MW;  EA2B63D193C903CC CRC64;
     MKYLTILGST GSIGTSTLTV IKQNPDKFTV RALVAKNNFT LMTKQCLDFR PSWVGMVDKR
     AARELKANLA QLGIAINIIS GNQAACELAA LKEIDTVMAA IAGVDGLLST LSALRAGKRV
     LLANKESLVS CGRLFMNEVH QHNAQLLPVD SEHNAIFQIL PEPIQRQLGC LSLSKYGVSQ
     IILTGSGGPF RQTPLDALAT ITSDQACIHP NWSMGRKISV DSATMMNKGL EYIEARCLFN
     ASTDQIEVLL HPQSIFHSMV RYVDGSVLAQ LAYPDMRIPI TYALSYPTRV PIKVTPLNFL
     QLGTLSFDQP DNKRYPCLQL AIEASKLGQA ATTTLNAANE VAVAAFLQRK IRFTDIASVN
     QMVLDKINLE EPSSIEEVLC IDRQARINAH LSIRYLAL
//