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DXR_BIFLS
ID   DXR_BIFLS               Reviewed;         396 AA.
AC   B7GQ02; E8MQW1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Blon_0779, BLIJ_0794;
OS   Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS   1222 / NCTC 11817 / S12).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=391904;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX   PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA   Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA   Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA   Richardson P.M., Mills D.A.;
RT   "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT   adaptations for milk utilization within the infant microbiome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX   PubMed=21270894; DOI=10.1038/nature09646;
RA   Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA   Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA   Morita H., Hattori M., Ohno H.;
RT   "Bifidobacteria can protect from enteropathogenic infection through
RT   production of acetate.";
RL   Nature 469:543-547(2011).
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   -!- SIMILARITY: Belongs to the DXR family. {ECO:0000255|HAMAP-
CC       Rule:MF_00183}.
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DR   EMBL; CP001095; ACJ51882.1; -; Genomic_DNA.
DR   EMBL; AP010889; BAJ68386.1; -; Genomic_DNA.
DR   RefSeq; WP_012577163.1; NZ_JDTT01000007.1.
DR   AlphaFoldDB; B7GQ02; -.
DR   SMR; B7GQ02; -.
DR   PRIDE; B7GQ02; -.
DR   EnsemblBacteria; ACJ51882; ACJ51882; Blon_0779.
DR   KEGG; bln:Blon_0779; -.
DR   KEGG; blon:BLIJ_0794; -.
DR   PATRIC; fig|391904.8.peg.800; -.
DR   HOGENOM; CLU_035714_4_0_11; -.
DR   OMA; PIDSEHF; -.
DR   UniPathway; UPA00056; UER00092.
DR   Proteomes; UP000001360; 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;
KW   Isoprene biosynthesis; Metal-binding; NADP; Oxidoreductase.
FT   CHAIN           1..396
FT                   /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase"
FT                   /id="PRO_1000189857"
FT   BINDING         12..41
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         155
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         157
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         226
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
SQ   SEQUENCE   396 AA;  41983 MW;  208FA0FD032A13D1 CRC64;
     MSIASNSTVI ILGSTGSIGT QGLDVIARHP ERFTVTGLAA GGAHIELLAQ QAAQFHVSEV
     AVFDETKIPA LQAALAQAGA QGVRVTGGPD SVIAMAGSGA NVVLNGITGS IGLEPSIAAL
     KAGSQLALAN KESVVAGGHL LFSAQVRENQ INPVDSEHSA IWQSLRSGTH AEVAKLVVTA
     SGGPFRGWKR ADMENITPEQ ALHHPTWNMG PVVTINSSTL MNKGLEVIEA SRLFDVPPER
     IDVTVHPQSI VHSMVEFVDG ATICQASPPD MRLPIALGLS APDRMANVAA ACDWTKAATW
     TFEPLDDEAF PAVQLARHCL AASEKHTAVL NAANEQAVHA FLEHRLPYLG IVDTVKAVLD
     QMDAELRGNP LFTDVEEMNQ LELEARRRAD DLINKQ
 
 
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