ID A0A7R7TN08_THETH Unreviewed; 367 AA. AC A0A7R7TN08; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 29-SEP-2021, entry version 2. DE RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00183}; DE Short=DXP reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00183}; DE EC=1.1.1.267 {ECO:0000256|HAMAP-Rule:MF_00183}; DE AltName: Full=1-deoxyxylulose-5-phosphate reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00183}; DE AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00183}; GN Name=dxr {ECO:0000256|HAMAP-Rule:MF_00183, GN ECO:0000313|EMBL:BCQ00098.1}; GN ORFNames=TthHB5002_08700 {ECO:0000313|EMBL:BCP97767.1}, GN TthHB5008_08680 {ECO:0000313|EMBL:BCQ00098.1}; OS Thermus thermophilus. OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=274 {ECO:0000313|EMBL:BCQ00098.1}; RN [1] {ECO:0000313|EMBL:BCQ00098.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HB5002 {ECO:0000313|EMBL:BCP97767.1}, and HB5008 RC {ECO:0000313|EMBL:BCQ00098.1}; RA Miyazaki K., Moriya T., Oshima T., Yura K., Bessho Y.; RT "Complete genome sequences of twin Thermus thermophilus strains HB5002 and RT HB5008 isolated from Mine Onsen hot spring in Japan."; RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction of CC 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4- CC phosphate (MEP). {ECO:0000256|HAMAP-Rule:MF_00183}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D- CC xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792, CC ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267; CC Evidence={ECO:0000256|ARBA:ARBA00000539, ECO:0000256|HAMAP- CC Rule:MF_00183}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00183}; CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5- CC phosphate: step 1/6. {ECO:0000256|ARBA:ARBA00005094, ECO:0000256|HAMAP- CC Rule:MF_00183}. CC -!- SIMILARITY: Belongs to the DXR family. {ECO:0000256|ARBA:ARBA00006825, CC ECO:0000256|HAMAP-Rule:MF_00183}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00183}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP024301; BCP97767.1; -; Genomic_DNA. DR EMBL; AP024305; BCQ00098.1; -; Genomic_DNA. DR UniPathway; UPA00056; UER00092. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR HAMAP; MF_00183; DXP_reductoisom; 1. DR InterPro; IPR003821; DXP_reductoisomerase. DR InterPro; IPR013644; DXP_reductoisomerase_C. DR InterPro; IPR013512; DXP_reductoisomerase_N. DR InterPro; IPR026877; DXPR_C. DR InterPro; IPR036169; DXPR_C_sf. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR30525; PTHR30525; 1. DR Pfam; PF08436; DXP_redisom_C; 1. DR Pfam; PF02670; DXP_reductoisom; 1. DR Pfam; PF13288; DXPR_C; 1. DR PIRSF; PIRSF006205; Dxp_reductismrs; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF69055; SSF69055; 1. DR TIGRFAMs; TIGR00243; Dxr; 1. PE 3: Inferred from homology; KW Isomerase {ECO:0000313|EMBL:BCQ00098.1}; KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP- KW Rule:MF_00183}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00183}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00183}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00183}. FT DOMAIN 4..120 FT /note="DXP_reductoisom" FT /evidence="ECO:0000259|Pfam:PF02670" FT DOMAIN 134..216 FT /note="DXP_redisom_C" FT /evidence="ECO:0000259|Pfam:PF08436" FT DOMAIN 248..361 FT /note="DXPR_C" FT /evidence="ECO:0000259|Pfam:PF13288" FT METAL 138 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183" FT METAL 140 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183" FT METAL 208 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183" FT BINDING 113 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183" FT BINDING 140 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183" FT BINDING 164 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183" FT BINDING 186 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183" FT BINDING 208 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183" SQ SEQUENCE 367 AA; 40162 MW; A8F89A83EA9290D6 CRC64; MKRVVVLGST GSIGQQALEV CRLRGYEVVG LAAGKNLEAL SRQIALWKPR LVAAEESLHK ELKARFPGLR LATAEEVAAL EAEVAVAAIP GLAGLAPTRM AVRTGKRVAL ANKEAMVAAG PLLWREAEAH GAEILPVDSE HSALFQALLG ERREDVAELI LTASGGPFLR EPEDLAQVTP EMALRHPRWR MGPKVTVDSA TLFNKGLEVL EAKELFRFPL ERIKVLIHPQ AYVHGLVRFV DGSLKAQLGP TDMRLFIQYA LTYPERAETP LKDLPIPGVL EFLEPDLKRF PALALAYEAG RRGGLAQVAV SAADEVAVEA FLQGKIPFPR IPEILARVLE ATPIEPLTWE SLFAVDAWAR EEAKRWA //