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}.
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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
//