ID   DXR_BORA1               Reviewed;         399 AA.
AC   Q2L155;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, 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=BAV1740;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(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; AM167904; CAJ49348.1; -; Genomic_DNA.
DR   RefSeq; YP_786258.1; -.
DR   GeneID; 6266768; -.
DR   GenomeReviews; AM167904_GR; BAV1740.
DR   KEGG; bav:BAV1740; -.
DR   NMPDR; fig|521.1.peg.1680; -.
DR   HOGENOM; Q2L155; -.
DR   OMA; Q2L155; 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    399       1-deoxy-D-xylulose 5-phosphate
FT                                reductoisomerase.
FT                                /FTId=PRO_1000020220.
FT   NP_BIND      10     39       NADP (By similarity).
FT   METAL       153    153       Divalent metal cation (By similarity).
FT   METAL       155    155       Divalent metal cation (By similarity).
FT   METAL       232    232       Divalent metal cation (By similarity).
FT   BINDING     128    128       Substrate (By similarity).
FT   BINDING     155    155       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   399 AA;  42312 MW;  C5D2CFE3003299BE CRC64;
     MSGFQRIAVL GSTGSIGDST LDVIARYPER FGVYALSAFS RMDKLAAQAL ATGAAVVVVP
     DNNAATRFRQ AWSPSRALPE IRVGAQALAD TAADAGCDTV MAAIVGIAGL PAALAAAQSG
     KRVLLANKEA LVAAGSIFMS AVRQSGAELL PIDSEHNAIF QCLPQGERAG APSTPAKTVR
     KLILTASGGP FRRHSPEDLQ DVTPDQACAH PNWSMGRKIS VDSATMLNKG LEVIEAHWLF
     AMPADRIEVL IHPQSVVHSL VEYDDGSVLA QMGQPDMRTP ISYGLGFPER LDAGVSPLDL
     AKWGRLDFET PDLERFPCLR LSYEALRAGQ AACVALNAAN EIAVAAFLEG RLPYPWIARV
     IDAALEWQAG RPSVTLDHLT DVLALDAQVR AYAGNLGLA
//