(data stored in ACNUC9543 zone)

SWISSPROT: DXR_YERPA

ID   DXR_YERPA               Reviewed;         398 AA.
AC   Q1CAN0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   11-DEC-2019, entry version 85.
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=YPA_0524;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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; CP000308; ABG12492.1; -; Genomic_DNA.
DR   RefSeq; WP_002212135.1; NZ_CP009906.1.
DR   SMR; Q1CAN0; -.
DR   EnsemblBacteria; ABG12492; ABG12492; YPA_0524.
DR   KEGG; ypa:YPA_0524; -.
DR   HOGENOM; HOG000007221; -.
DR   KO; K00099; -.
DR   OMA; AANEECV; -.
DR   UniPathway; UPA00056; UER00092.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:UniProtKB-UniRule.
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   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
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; Q1CAN0.
DR   SWISS-2DPAGE; Q1CAN0.
KW   Isoprene biosynthesis; Metal-binding; NADP; Oxidoreductase.
FT   CHAIN           1..398
FT                   /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase"
FT                   /id="PRO_1000020326"
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;  43115 MW;  C9B1FC9E0166D057 CRC64;
     MKQLTILGST GSIGNSTLSV VRANPELFKV TALVAGRNVR EMAQQCLEFS PRYAAMSDEH
     SAKSLRLLLA EQGSDTEVYS GETAACELAA LDDVDQVMAA IVGIAGLPST LAAIRAGKQV
     LLANKESLIT CGKLFMDEVK RSRAQLLPID SEHNAIFQSL PERIQRQLGY SSLNENGVSR
     IILTGSGGPF RETPLSQFSD VTPDQACAHP NWSMGRKISV DSATMMNKGL EYIEARWLFN
     ASAEQIEVVL HPQSVIHSMV RYHDGSILAQ MGTPDMRTPI AHAMAYPMRV SSGVAPLDFC
     KVGALTFTTP DYQRYPCLKL AIDACNAGQA ATTALNAANE ISVMAFLDSK IRFTDIEVIN
     RTVVEGLLLS EPTSVEEVLV IDRKARDVAA QVIAKLNN
//

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