ID   DXR_CHLTA               Reviewed;         379 AA.
AC   Q3KMV0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-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=CTA_0076;
OS   Chlamydia trachomatis (strain A/HAR-13 / ATCC VR-571B).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=315277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16177312; DOI=10.1128/IAI.73.10.6407-6418.2005;
RA   Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT   "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT   genitotropic strains.";
RL   Infect. Immun. 73:6407-6418(2005).
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; CP000051; AAX50322.1; -; Genomic_DNA.
DR   RefSeq; YP_327870.1; -.
DR   GeneID; 3687563; -.
DR   GenomeReviews; CP000051_GR; CTA_0076.
DR   KEGG; cta:CTA_0076; -.
DR   HOGENOM; Q3KMV0; -.
DR   OMA; Q3KMV0; IHSMVEY.
DR   BioCyc; CTRA315277-1:CTA_0076-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    379       1-deoxy-D-xylulose 5-phosphate
FT                                reductoisomerase.
FT                                /FTId=PRO_1000020245.
FT   NP_BIND       7     36       NADP (By similarity).
FT   METAL       147    147       Divalent metal cation (By similarity).
FT   METAL       149    149       Divalent metal cation (By similarity).
FT   METAL       218    218       Divalent metal cation (By similarity).
FT   BINDING     122    122       Substrate (By similarity).
FT   BINDING     149    149       Substrate (By similarity).
FT   BINDING     173    173       Substrate (By similarity).
FT   BINDING     196    196       Substrate (By similarity).
FT   BINDING     218    218       Substrate (By similarity).
SQ   SEQUENCE   379 AA;  41762 MW;  3F00933320E54E4C CRC64;
     MKHLALIGST GSIGRQVLQV VRSIPDTFII ETLAAYGRNQ EALISQIREF NPRVVAVREE
     TTYKELRKLF PHIEILLGEE GLVSVATEPS VTMTIVASSG IDALPAVIAA IRQKKTIALA
     NKESLVAAGE LVTTLARENG VQILPIDSEH NALFQCLEGR DSSTIKKLLL TASGGPLRNK
     SKEELQKVSL QEVLRHPVWN MGPKITVDSS TLVNKGLEII EAFWLFGLEA VEIEAVIHPQ
     SLVHGMVEFC DGTILSVMNP PSMLFPIQHV LTFPERSPAI GPGFDFLSNR TLEFFPIDED
     RFPSVHLAKR VLLEKGSMGC FFNGANEALV HRFLAGEISW HQIVPKLQAL VDQHRVQSCL
     SLEEILSVDA EARARAQEC
//