(data stored in ACNUC1104 zone)

SWISSPROT: DXR_BORPA

ID   DXR_BORPA               Reviewed;         399 AA.
AC   Q7WA54;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAY-2019, entry version 92.
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=BPP1533;
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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:
CC       Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-
CC         D-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
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   -!- SIMILARITY: Belongs to the DXR family. {ECO:0000255|HAMAP-
CC       Rule:MF_00183}.
DR   EMBL; BX640427; CAE36835.1; -; Genomic_DNA.
DR   RefSeq; WP_010928081.1; NC_002928.3.
DR   SMR; Q7WA54; -.
DR   EnsemblBacteria; CAE36835; CAE36835; BPP1533.
DR   KEGG; bpa:BPP1533; -.
DR   HOGENOM; HOG000007221; -.
DR   KO; K00099; -.
DR   OMA; AHPNWVM; -.
DR   BioCyc; BPAR257311:G1GSY-1573-MONOMER; -.
DR   UniPathway; UPA00056; UER00092.
DR   Proteomes; UP000001421; 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; Q7WA54.
DR   SWISS-2DPAGE; Q7WA54.
KW   Complete proteome; Isoprene biosynthesis; Metal-binding; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    399       1-deoxy-D-xylulose 5-phosphate
FT                                reductoisomerase.
FT                                /FTId=PRO_0000163619.
FT   NP_BIND      10     39       NADP. {ECO:0000255|HAMAP-Rule:MF_00183}.
FT   METAL       153    153       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00183}.
FT   METAL       155    155       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00183}.
FT   METAL       232    232       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00183}.
FT   BINDING     128    128       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00183}.
FT   BINDING     155    155       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00183}.
FT   BINDING     187    187       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00183}.
FT   BINDING     210    210       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00183}.
FT   BINDING     232    232       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00183}.
SQ   SEQUENCE   399 AA;  42113 MW;  CB6CD0C8169FF761 CRC64;
     MTRFQRVAVL GSTGSIGDST LDVIARHPDR LGVYALSAYS RMDKLAAQAA ACGAAVVVVP
     DDAAAARFRA AWRGKAAMPE VRVGPRTLAE TAAAPECTTV MAAIVGAAGL PAALAAAQAG
     KRVLLANKEA LVAAGSLFMA AVRENGAELL PIDSEHNAIF QCMPQGARAA APTAPAPGVR
     RLLLTASGGP FRRQDPADLH EVTPAQACAH PNWSMGRKIS VDSATMLNKG LEVIEAHWLF
     AMPSERIDVL IHPQSVVHSM VEYDDGSVLA QLGQPDMRTP IAYGLGFPER LASGVGLLDL
     TRWGRLDFEQ PDLQRFPCLA LSFAALRAGQ PACVALNAAN EVAVAAFLEG RLRYTWVARV
     IEAVLEWQAK QASVTLTSLD DVLDLDARAR SFAGNLGLA
//

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