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Database: UniProt
Entry: K4KF65_EUCUL
LinkDB: K4KF65_EUCUL
Original site: K4KF65_EUCUL 
ID   K4KF65_EUCUL            Unreviewed;       478 AA.
AC   K4KF65;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=1-deoxy-D-xylulose-5-phosphate reductoisomerase {ECO:0000256|ARBA:ARBA00012366};
DE            EC=1.1.1.267 {ECO:0000256|ARBA:ARBA00012366};
GN   Name=DXR1 {ECO:0000313|EMBL:AFU93070.1};
OS   Eucommia ulmoides (Hardy rubber tree).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Garryales; Eucommiaceae; Eucommia.
OX   NCBI_TaxID=4392 {ECO:0000313|EMBL:AFU93070.1};
RN   [1] {ECO:0000313|EMBL:AFU93070.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Liu P.F., Du H.Y., Yun T.N.W., Huang H.Y.;
RT   "Cloning and Sequence Analysis of 1-deoxy-D-xylulose-5-phosphate reductase
RT   Gene cDNA from Eucommia ulmoides.";
RL   Lin Ye Ke Xue Yan Jiu 25:195-200(2012).
RN   [2] {ECO:0000313|EMBL:AQZ26748.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wuyun T., Wang L., Du H.;
RT   "Subcellular Localization and Expression Analysis of Genes from Eucommia
RT   ulmoides Involved in the MVA and MEP Pathway.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AFU93070.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00034272};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13719;
CC         Evidence={ECO:0000256|ARBA:ARBA00034272};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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:0000256|ARBA:ARBA00005094}.
CC   -!- SIMILARITY: Belongs to the DXR family. {ECO:0000256|ARBA:ARBA00006825}.
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DR   EMBL; JX458819; AFU93070.1; -; mRNA.
DR   EMBL; KX431565; AQZ26748.1; -; mRNA.
DR   AlphaFoldDB; K4KF65; -.
DR   UniPathway; UPA00056; UER00092.
DR   GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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   Gene3D; 1.10.1740.10; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   NCBIfam; TIGR00243; Dxr; 1.
DR   PANTHER; PTHR30525; 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE; 1.
DR   PANTHER; PTHR30525:SF0; 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE, CHLOROPLASTIC; 1.
DR   Pfam; PF08436; DXP_redisom_C; 1.
DR   Pfam; PF02670; DXP_reductoisom; 1.
DR   Pfam; PF13288; DXPR_C; 1.
DR   SUPFAM; SSF69055; 1-deoxy-D-xylulose-5-phosphate reductoisomerase, C-terminal domain; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   2: Evidence at transcript level;
KW   Isomerase {ECO:0000313|EMBL:AQZ26748.1};
KW   Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          84..212
FT                   /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02670"
FT   DOMAIN          226..309
FT                   /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08436"
FT   DOMAIN          341..463
FT                   /note="DXP reductoisomerase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13288"
SQ   SEQUENCE   478 AA;  51715 MW;  64E6979758B8EDD5 CRC64;
     MALNLLPRTE FNPVSFFHTS KSNRNLFNLQ GGFAFKRKDI GATNGLRVHC SAEEVGVAVA
     PPPAWPGRAV VEPGRKSWDG PKPISIVGST GSIGTQTLDI VAENPDKFKV VALAAGSNVT
     LLADQVKTFK PQLVAVRNES LVDELKEALA DAEYTPEIIP GEQGVIEVAR HPDAVTVVTG
     IVGCAGLKPT VAAIEAGKDI ALANKETLIA GGPFVLPLAH KHNVKILPAD SEHSAIFQCI
     QGLPEGALRR IILTASGGAF RDLPVDKLKD VKVADALKHP NWNMGKKITV DSATLFNKGL
     EVIEAHYLFG AEYDDIEIVI HPQSIIHSMI ETQDSSVLAQ LGWPDMRLPI LYTMSWPDRI
     FCSEITWPRL DLCKLGSLTF KMPDNVKYPS MDLAYAAGRA GGTMTGVLSA ANEKAVEMFI
     DEKIGYLDIF KVVELTCDKH RAELVSSPSL DEIVHYDLWA RKYAASLQPS SGLSPALV
//
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