ID A0A1D6FCR1_MAIZE Unreviewed; 573 AA.
AC A0A1D6FCR1;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=ZEAMMB73_Zm00001d008427 {ECO:0000313|EMBL:AQK89819.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK89819.1};
RN [1] {ECO:0000313|EMBL:AQK89819.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQK89819.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000784; AQK89819.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6FCR1; -.
DR SMR; A0A1D6FCR1; -.
DR IntAct; A0A1D6FCR1; 1.
DR STRING; 4577.A0A1D6FCR1; -.
DR InParanoid; A0A1D6FCR1; -.
DR UniPathway; UPA00056; UER00092.
DR ExpressionAtlas; A0A1D6FCR1; baseline and differential.
DR GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IBA:GO_Central.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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 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; 2.
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 Isomerase {ECO:0000313|EMBL:AQK89819.1};
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 116..232
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02670"
FT DOMAIN 323..374
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08436"
FT DOMAIN 406..488
FT /note="DXP reductoisomerase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13288"
SQ SEQUENCE 573 AA; 63091 MW; 129E016AC1C6BB4F CRC64;
MAAQPALKAS FRGELNAVSF LDSSRGPFGQ HKVDFTFQRK GKRAISLRRT CCSMQQAPPP
AWPGRAVAEP GRRSLDGPKP ISIVGSTGSI GTQIIRSSSM LLYSAALIFN LLHNAKTLDI
VAENPDKFRV VALSAGSNVT LLADQVKTFK PKLVAVRNET LVDELKEALA DCEEKPEIIP
GEQGVIEVAR HPDAITVVTG IVGCAGLKPT VAAIEAGKDI ALANKETLIA GGPFVLPLAH
KHKVKILPAD SEHSAIFQVS HKMFTCSAAN FFIIIHVWLH PRLVRRSTSS HYSNCIRWCF
QASPSICVIC TSVNMRIHLI SNAHDRDWPV DRLKDVKVAD ALKHPNWNMG KKITVDSATL
FNKGLEVIEA HYLFGAEYDD IEIVIHPQSI IHSMVETQDS SVLAQLGWPD MRIPILYTLS
WPDRIYCSEV TWPRLNLCKL GSLTFKAPDN VKYPSMDLAY AAGRAGGTMT GVLSAANEKA
VELFIDEKKE KEKENFGPTK VHGHLLMRMH VLKDIIPKIS YLDIFKVVEL TCDAHRNELV
ASPSLEEIIH YDLWARRHAA SLQPASGLSP VPA
//
