(data stored in ACNUC7421 zone)

SWISSPROT: DXR_ECO57

ID   DXR_ECO57               Reviewed;         398 AA.
AC   Q8X8Y1;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 99.
DE   RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183};
DE            Short=DXP reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183};
DE            EC=1.1.1.267 {ECO:0000255|HAMAP-Rule:MF_00183};
DE   AltName: Full=1-deoxyxylulose-5-phosphate reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183};
DE   AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00183};
GN   Name=dxr {ECO:0000255|HAMAP-Rule:MF_00183};
GN   OrderedLocusNames=Z0184, ECs0175;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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). {ECO:0000255|HAMAP-Rule:MF_00183}.
CC   -!- CATALYTIC ACTIVITY: 2-C-methyl-D-erythritol 4-phosphate + NADP(+)
CC       = 1-deoxy-D-xylulose 5-phosphate + NADPH. {ECO:0000255|HAMAP-
CC       Rule:MF_00183}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00183};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC       biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC       deoxy-D-xylulose 5-phosphate: step 1/6. {ECO:0000255|HAMAP-
CC       Rule:MF_00183}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00183}.
CC   -!- SIMILARITY: Belongs to the DXR family. {ECO:0000255|HAMAP-
CC       Rule:MF_00183}.
DR   EMBL; AE005174; AAG54475.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33598.1; -; Genomic_DNA.
DR   PIR; G85501; G85501.
DR   PIR; G90650; G90650.
DR   RefSeq; NP_308202.1; NC_002695.1.
DR   RefSeq; WP_000811924.1; NZ_MWVM01000012.1.
DR   ProteinModelPortal; Q8X8Y1; -.
DR   SMR; Q8X8Y1; -.
DR   STRING; 155864.Z0184; -.
DR   EnsemblBacteria; AAG54475; AAG54475; Z0184.
DR   EnsemblBacteria; BAB33598; BAB33598; BAB33598.
DR   GeneID; 913875; -.
DR   KEGG; ece:Z0184; -.
DR   KEGG; ecs:ECs0175; -.
DR   PATRIC; fig|386585.9.peg.277; -.
DR   eggNOG; ENOG4105CEA; Bacteria.
DR   eggNOG; COG0743; LUCA.
DR   HOGENOM; HOG000007221; -.
DR   KO; K00099; -.
DR   UniPathway; UPA00056; UER00092.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070402; F:NADPH binding; IEA:InterPro.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
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; IPR016040; NAD(P)-bd_dom.
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;
DR   PRODOM; Q8X8Y1.
DR   SWISS-2DPAGE; Q8X8Y1.
KW   Complete proteome; Isoprene biosynthesis; Metal-binding; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    398       1-deoxy-D-xylulose 5-phosphate
FT                                reductoisomerase.
FT                                /FTId=PRO_0000163652.
FT   NP_BIND       7     36       NADP. {ECO:0000255|HAMAP-Rule:MF_00183}.
FT   METAL       150    150       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00183}.
FT   METAL       152    152       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00183}.
FT   METAL       231    231       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00183}.
FT   BINDING     125    125       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00183}.
FT   BINDING     152    152       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00183}.
FT   BINDING     186    186       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00183}.
FT   BINDING     209    209       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00183}.
FT   BINDING     231    231       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00183}.
SQ   SEQUENCE   398 AA;  43361 MW;  8B532683A4FF082E CRC64;
     MKQLTILGST GSIGCSTLDV VRHNPEHFRV VALVAGKNVT RMVEQCLEFS PRYAVMDDEA
     SAKLLKTMLQ QQGSRTEVLS 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 VDASAREVAR KEVMRLAS
//

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