ID A0A0A0LNW9_CUCSA Unreviewed; 469 AA.
AC A0A0A0LNW9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ORFNames=Csa_1G004930 {ECO:0000313|EMBL:KGN63580.1};
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN63580.1, ECO:0000313|Proteomes:UP000029981};
RN [1] {ECO:0000313|EMBL:KGN63580.1, ECO:0000313|Proteomes:UP000029981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX PubMed=19881527; DOI=10.1038/ng.475;
RA Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT "The genome of the cucumber, Cucumis sativus L.";
RL Nat. Genet. 41:1275-1281(2009).
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; CM002922; KGN63580.1; -; Genomic_DNA.
DR RefSeq; XP_004138108.1; XM_004138060.2.
DR RefSeq; XP_011657140.1; XM_011658838.1.
DR AlphaFoldDB; A0A0A0LNW9; -.
DR STRING; 3659.A0A0A0LNW9; -.
DR EnsemblPlants; KGN63580; KGN63580; Csa_1G004930.
DR GeneID; 101207716; -.
DR Gramene; KGN63580; KGN63580; Csa_1G004930.
DR KEGG; csv:101207716; -.
DR eggNOG; ENOG502QPJ7; Eukaryota.
DR OMA; MMNKGFE; -.
DR OrthoDB; 275538at2759; -.
DR UniPathway; UPA00056; UER00092.
DR Proteomes; UP000029981; Chromosome 1.
DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
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 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 PIRSF; PIRSF006205; Dxp_reductismrs; 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 3: Inferred from homology;
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000029981}.
FT DOMAIN 75..203
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02670"
FT DOMAIN 217..300
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08436"
FT DOMAIN 332..453
FT /note="DXP reductoisomerase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13288"
SQ SEQUENCE 469 AA; 50960 MW; E849D544765E324B CRC64;
MALNVLAPPE IKALSFLESS RSRHFTKLQG GSSIKECRTI VHKRIHCSSQ PPPPAWPGQA
VVPPGYKKWD GRKPISILGS TGSIGTQTLD IVAENPEKFK VVGLAAGSNI TLLADQVKTF
KPQLVAVRNE SLIDELKEAL ADLDEKPEII PGEQGVIEVA RHPDAVTVVT GIVGCAGLKP
TVAAIEAGKD IALANKETLI AGGPFVLPLA HKHNVKILPA DSEHSAIFQC IQGLPEGALR
RIILTASGGA FRDLPVEKLK DVKVADALKH PNWSMGKKIT VDSATLFNKG LEVIEAHYLF
GAEYDDIEIV IHPQSIIHSM IETQDSSVLA QLGWPDMRLP IAYTITWPER LYCSEVTWPR
LDLCKLGSLT FKTPDNVKYP SMDLAYAAGR AGGTMTGVLS AANEKAVEMF IDEKISYLDI
FKVVELTCDK HQNELITAPS LEEIVHYDLW ARDYAANLQS SSSFSPVAA
//
