ID DXR_CHLTE Reviewed; 382 AA. AC Q8KG43; DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, 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=CT0125; OS Chlorobium tepidum. OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobaculum. OX NCBI_TaxID=1097; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49652 / DSM 12025 / TLS; RX MEDLINE=22103685; PubMed=12093901; DOI=10.1073/pnas.132181499; RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., RA Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., RA Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., RA Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P., RA Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., RA Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., RA Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.; RT "The complete genome sequence of Chlorobium tepidum TLS, a RT photosynthetic, anaerobic, green-sulfur bacterium."; RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002). 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE006470; AAM71373.1; -; Genomic_DNA. DR RefSeq; NP_661031.1; -. DR HSSP; P45568; 1K5H. DR GeneID; 1006807; -. DR GenomeReviews; AE006470_GR; CT0125. DR KEGG; cte:CT0125; -. DR NMPDR; fig|194439.1.peg.125; -. DR TIGR; CT0125; -. DR HOGENOM; Q8KG43; -. DR OMA; Q8KG43; IHSMVEY. DR BioCyc; CTEP194439:CT_0125-MON; -. DR BRENDA; 1.1.1.267; 189605. 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 1 382 1-deoxy-D-xylulose 5-phosphate FT reductoisomerase. FT /FTId=PRO_0000163634. 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 219 219 Divalent metal cation (By similarity). FT BINDING 123 123 Substrate (By similarity). FT BINDING 150 150 Substrate (By similarity). FT BINDING 174 174 Substrate (By similarity). FT BINDING 197 197 Substrate (By similarity). FT BINDING 219 219 Substrate (By similarity). SQ SEQUENCE 382 AA; 41344 MW; 4B42A8B6F36368CA CRC64; MKSLSILGST GSIGLSTLDV VRRHPERFSI AALAEGHDVE MLLKQIDEFR PSLVSVRDEA SRERLKGMLG DHKPEILCGL EGAAEVAAVD GADMVVSAIV GAAGLVPTVR AIEAGKDIAL ANKETLVVAG QLVSDLVKKH DVKLLPVDSE HSAIFQSLVG HRTEDIERII LTASGGPFRK TPAEELKNVG PEQALKHPQW SMGAKITIDS ATLMNKGLEV IEAHWLFDMP AEKIGVVVHP QSIIHSMVEY IDGCVIAQLG VPDMRAPIAY ALAWPERCET GIGKLDLTKV ATLTFEEPDM ERFPALRLAF DALKAGQTYP AVLNAANEIA VAAFLDKKIG FTDIAGTVDK TMQAHEAWTP ITLEEYLQAD KWARETARQL IG //