(data stored in ACNUC7421 zone)

SWISSPROT: DXR_SALTY

ID   DXR_SALTY               Reviewed;         398 AA.
AC   Q8ZRP3;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   11-DEC-2019, entry version 103.
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}; OrderedLocusNames=STM0220;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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:0000255|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:0000255|HAMAP-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 biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 1/6. {ECO:0000255|HAMAP-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; AE006468; AAL19184.1; -; Genomic_DNA.
DR   RefSeq; NP_459225.1; NC_003197.2.
DR   RefSeq; WP_000811905.1; NC_003197.2.
DR   SMR; Q8ZRP3; -.
DR   PaxDb; Q8ZRP3; -.
DR   PRIDE; Q8ZRP3; -.
DR   EnsemblBacteria; AAL19184; AAL19184; STM0220.
DR   GeneID; 1251738; -.
DR   KEGG; stm:STM0220; -.
DR   PATRIC; fig|99287.12.peg.233; -.
DR   eggNOG; ENOG4105CEA; Bacteria.
DR   eggNOG; COG0743; LUCA.
DR   HOGENOM; HOG000007221; -.
DR   KO; K00099; -.
DR   OMA; AANEECV; -.
DR   PhylomeDB; Q8ZRP3; -.
DR   BioCyc; SENT99287:STM0220-MONOMER; -.
DR   UniPathway; UPA00056; UER00092.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IBA:GO_Central.
DR   GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR   GO; GO:0070402; F:NADPH binding; IBA:GO_Central.
DR   GO; GO:0051484; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process; IBA:GO_Central.
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;
DR   PRODOM; Q8ZRP3.
DR   SWISS-2DPAGE; Q8ZRP3.
KW   Isoprene biosynthesis; Metal-binding; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..398
FT                   /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase"
FT                   /id="PRO_0000163710"
FT   NP_BIND         7..36
FT                   /note="NADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   METAL           150
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   METAL           152
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   METAL           231
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         125
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         152
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         186
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         209
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         231
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
SQ   SEQUENCE   398 AA;  43353 MW;  CB720D959CDF8FCC CRC64;
     MKQLTILGST GSIGCSTLDV VRHNPDSFRV IALVAGKNVA RMAEQCLEFS PRYAVMDDTS
     SAEQLKIMLQ QHGSRTEVLS GQQAACEMAA LDEVGHVMAA IVGAAGLLPT LAAIRAGKTI
     LLANKESLVT CGRLFMDEVK RSNARLLPVD SEHNAIFQSL PQSIQHNLGY ADLEQNGVTS
     ILLTGSGGPF RETPMCDLAA MTPDQACRHP NWSMGRKISV DSATMMNKGL EYIEARWLFN
     ASARQMEVLI HPQSVIHSMV RYQDGSVLAQ LGEPDMRTPI AHTMAWPNRV TSGAQPLDFC
     KLSALTFSAP DYQRYPCLKL AMEAFEQGQA ATTALNAANE ITVAAFLAQQ IRFTDIAGLN
     LAVLERMDLQ EPASVEDVLQ VDAIAREVAR KQVIRLSR
//

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