ID   DXR_ANAPZ               Reviewed;         385 AA.
AC   Q2GKQ8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=APH_0440;
OS   Anaplasma phagocytophilum (strain HZ).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma; phagocytophilum group.
OX   NCBI_TaxID=212042;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S.,
RA   Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N.,
RA   Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P.,
RA   Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F.,
RA   Forberger H., Halpin R., Mulligan S., Robinson J., White O.,
RA   Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(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; CP000235; ABD44127.1; -; Genomic_DNA.
DR   RefSeq; YP_505043.1; -.
DR   GeneID; 3930540; -.
DR   GenomeReviews; CP000235_GR; APH_0440.
DR   KEGG; aph:APH_0440; -.
DR   NMPDR; fig|212042.5.peg.429; -.
DR   TIGR; APH_0440; -.
DR   HOGENOM; Q2GKQ8; -.
DR   OMA; Q2GKQ8; IHSMVEY.
DR   BioCyc; APHA212042:APH_0440-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    385       1-deoxy-D-xylulose 5-phosphate
FT                                reductoisomerase.
FT                                /FTId=PRO_1000077331.
FT   NP_BIND       7     36       NADP (By similarity).
FT   METAL       148    148       Divalent metal cation (By similarity).
FT   METAL       150    150       Divalent metal cation (By similarity).
FT   METAL       217    217       Divalent metal cation (By similarity).
FT   BINDING     123    123       Substrate (By similarity).
FT   BINDING     150    150       Substrate (By similarity).
FT   BINDING     172    172       Substrate (By similarity).
FT   BINDING     195    195       Substrate (By similarity).
FT   BINDING     217    217       Substrate (By similarity).
SQ   SEQUENCE   385 AA;  41579 MW;  253AE0A7AF9BEB47 CRC64;
     MKKVSVFGST GFIGKTTVGI LSGNTEDFKV IALVAGSNVS LLAQQAKLLN AEMAVIADDA
     QYEELKRSLH GSGIRVAAGK EAVLEAAALS VDTAVMAITG IVALSAVMRL IESGVGTIAL
     ASKESVVCGG VLLRDAACKS GTRIVPVDSE HNAVFRLLSQ GDNPYKITIT ASGGPFLHWS
     HDQLKSVTIE DALVHPVWKM GKKISVDSAT MMNKALEVLE ASYLFELGYR KIDVVIHPES
     IVHALAFYQD GTSTALMSLP DMSIPILHAL YWPHRKEVSV REVDLIAYGK LTFIRPDFER
     FPALKAAFDI LQSSERDVAS IVFNAANEVA VESFLNSEIT FLEIVNIVLH VMNKVPYGKV
     SSLADIMEYD LLGRCIAREV ISDAS
//