ID A0A826NPK5_ECOLX Unreviewed; 398 AA. AC A0A826NPK5; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 19-JAN-2022, 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=ispC {ECO:0000313|EMBL:EFA8351117.1}; GN Synonyms=dxr {ECO:0000256|HAMAP-Rule:MF_00183}; GN ORFNames=C1073_002004 {ECO:0000313|EMBL:EFA8351117.1}; OS Escherichia coli O157. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1045010 {ECO:0000313|EMBL:EFA8351117.1, ECO:0000313|Proteomes:UP000525392}; RN [1] {ECO:0000313|EMBL:EFA8351117.1, ECO:0000313|Proteomes:UP000525392} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFSAN074462 {ECO:0000313|EMBL:EFA8351117.1, RC ECO:0000313|Proteomes:UP000525392}; RG GenomeTrakr network: Whole genome sequencing for foodborne pathogen traceback; RL Submitted (AUG-2018) 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 -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00183}. CC -!- SIMILARITY: Belongs to the DXR family. {ECO:0000256|ARBA:ARBA00006825, CC ECO:0000256|HAMAP-Rule:MF_00183}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EFA8351117.1}. 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; AASBYM010000018; EFA8351117.1; -; Genomic_DNA. DR UniPathway; UPA00056; UER00092. DR Proteomes; UP000525392; Unassembled WGS sequence. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase 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:EFA8351117.1}; 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..132 FT /note="DXP_reductoisom" FT /evidence="ECO:0000259|Pfam:PF02670" FT DOMAIN 146..239 FT /note="DXP_redisom_C" FT /evidence="ECO:0000259|Pfam:PF08436" FT DOMAIN 271..387 FT /note="DXPR_C" FT /evidence="ECO:0000259|Pfam:PF13288" FT NP_BIND 7..36 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183" FT METAL 150 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183" FT METAL 152 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183" FT METAL 231 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183" FT BINDING 125 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183" FT BINDING 152 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 209 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183" FT BINDING 231 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183" SQ SEQUENCE 398 AA; 43335 MW; 8E5B5FF5772364D2 CRC64; MKQLTILGST GSIGCSTLDV VRHNPEHFRV VALVAGKNVT RMVEQCLEFS PRYAVMDDEA SAKLLKTMLQ QQGSCTEVLS GQQAACDMAA LEDVDQVMAA IVGAAGLLPT LAAIRAGKTI LLANKESLVT CGRLFMDAVK QSKAQLLPVD SEHNAIFQSL PQPIQHNLGY ADLEQNGVVS ILLTGSGGPF RETPLRDLAT MTPDQACRHP NWSMGRKISV DSATMMNKGL EYIEARWLFN ASASQMEVLI HPQSVIHSMV RYQDGSVLAQ LGEPDMRTPI AHTMAWPNRV NSGVKPLDFC KLSALTFAAP DYDRYPCLKL AMEAFEQGQA ATTALNAANE ITVAAFLAQQ IRFTDIAALN LSVLEKMDMR EPQCVDDVLS VDANAREVAR KEVMRLAS //