ID   DXR_ANAVT               Reviewed;         398 AA.
AC   Q3MDL2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-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=Ava_1300;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000117; ABA20924.1; -; Genomic_DNA.
DR   RefSeq; YP_321819.1; -.
DR   GeneID; 3683043; -.
DR   GenomeReviews; CP000117_GR; Ava_1300.
DR   KEGG; ava:Ava_1300; -.
DR   NMPDR; fig|240292.3.peg.2145; -.
DR   HOGENOM; Q3MDL2; -.
DR   OMA; Q3MDL2; IHSMVEY.
DR   BioCyc; AVAR240292:AVA_1300-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_1000020213.
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       221    221       Divalent metal cation (By similarity).
FT   BINDING     125    125       Substrate (By similarity).
FT   BINDING     152    152       Substrate (By similarity).
FT   BINDING     176    176       Substrate (By similarity).
FT   BINDING     199    199       Substrate (By similarity).
FT   BINDING     221    221       Substrate (By similarity).
SQ   SEQUENCE   398 AA;  43055 MW;  4AA74AB2321D3130 CRC64;
     MKSITLVGST GSIGTQTLDI VSQYPDQFRI VGLAAGSNVE MLAEQIRQFR PQIAAISAAE
     KLPALQAAIK DLDPQPILLG GEAGVIEVAR YGDAETVVTG IVGCAGLLPT IAAIEAGKDI
     ALANKETLIA GGPVVLPLVE KHGVKLLPAD SEHSAIFQCL QGVPKGGLRK ILLTASGGAF
     RDWDVERLAE VTVADALKHP NWSMGRKITV DSATLMNKGL EVIEAHFLFG LDYQDIEIVI
     HPQSIIHSLI ELQDTSVLAQ LGWPDMRLPL LYALSWPERI YTDWEPLNLV KAGNLTFREP
     DHQKYPCMQL AYAAGRAGGS MPAVLNAANE QVVALFLDEK IKFLDIPRCI ELVCDRHQND
     NCANPSLDDI LAADQWARQE VLTATKNLAS QPQIISVN
//