ID   DXR_CHRVO               Reviewed;         394 AA.
AC   Q7NVY8;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   16-JUN-2009, entry version 39.
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=CV_2202;
OS   Chromobacterium violaceum.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Chromobacterium.
OX   NCBI_TaxID=536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131;
RX   MEDLINE=22882880; PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA   Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA   Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA   Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA   Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M.,
RA   Batista J.S., Belo A., van den Berg C., Bogo M., Bonatto S.,
RA   Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A.,
RA   Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M.,
RA   Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O.,
RA   Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L.,
RA   Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A.,
RA   Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA   Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA   Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA   Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P.,
RA   Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S.,
RA   di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M.,
RA   Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C.,
RA   Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O.,
RA   Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P.,
RA   Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E.,
RA   Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N.,
RA   Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C.,
RA   Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L.,
RA   Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T.,
RA   Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT   "The complete genome sequence of Chromobacterium violaceum reveals
RT   remarkable and exploitable bacterial adaptability.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
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; AE016825; AAQ59875.1; -; Genomic_DNA.
DR   RefSeq; NP_901872.1; -.
DR   GeneID; 2549212; -.
DR   GenomeReviews; AE016825_GR; CV_2202.
DR   KEGG; cvi:CV_2202; -.
DR   NMPDR; fig|243365.1.peg.2202; -.
DR   HOGENOM; Q7NVY8; -.
DR   OMA; Q7NVY8; IHSMVEY.
DR   BioCyc; CVIO243365:CV_2202-MON; -.
DR   BRENDA; 1.1.1.267; 415.
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    394       1-deoxy-D-xylulose 5-phosphate
FT                                reductoisomerase.
FT                                /FTId=PRO_0000163635.
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       229    229       Divalent metal cation (By similarity).
FT   BINDING     128    128       Substrate (By similarity).
FT   BINDING     155    155       Substrate (By similarity).
FT   BINDING     184    184       Substrate (By similarity).
FT   BINDING     207    207       Substrate (By similarity).
FT   BINDING     229    229       Substrate (By similarity).
SQ   SEQUENCE   394 AA;  41674 MW;  482DEAA31A2275F0 CRC64;
     MTKPQGIAVL GATGSVGCNT LDVVARHPER YRVVALTAHR QLDKLFEQAR RFCPDYLVVA
     DADAAARLRA RLAEAGLRSE VLHGADALVQ VAALPEVDAV MASIVGAAGL PSALAAARAG
     KRILLANKES LVVAGRLFMD AVRASGSALL PVDSEHSAIF QSLPADYAGN PDGAGVRKII
     LTASGGPFRN RPAADLAHVT PDEACRHPNW SMGRKISVDS ATLMNKGLEV IEARWLFNVP
     PSRIEVAVHP QSVIHSMVQY RDGSVMAQLG SPDMRTPIAC ALAWPERIDA GVEPMDFFSL
     SDLTFEKPDL ERFPCLQLAF DALEMGGDAP AVLNAANEVA VAAFLAGRLR FVDIPRVVAA
     SLSGVSCAAS DSLEGLLARD EEARRFAEGG VAAC
//