ID J9XH47_OLEEU Unreviewed; 199 AA.
AC J9XH47;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE RecName: Full=1-deoxy-D-xylulose-5-phosphate reductoisomerase {ECO:0000256|ARBA:ARBA00012366};
DE EC=1.1.1.267 {ECO:0000256|ARBA:ARBA00012366};
DE Flags: Fragment;
GN Name=DXR {ECO:0000313|EMBL:AFS28671.1};
OS Olea europaea (Common olive).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Oleaceae; Oleeae; Olea.
OX NCBI_TaxID=4146 {ECO:0000313|EMBL:AFS28671.1};
RN [1] {ECO:0000313|EMBL:AFS28671.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Fruit {ECO:0000313|EMBL:AFS28671.1};
RX PubMed=22963618; DOI=10.1186/1471-2229-12-162;
RA Alagna F., Mariotti R., Panara F., Caporali S., Urbani S., Veneziani G.,
RA Esposto S., Taticchi A., Rosati A., Rao R., Perrotta G., Servili M.,
RA Baldoni L.;
RT "Olive phenolic compounds: metabolic and transcriptional profiling during
RT fruit development.";
RL BMC Plant Biol. 12:162-162(2012).
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; JX266164; AFS28671.1; -; mRNA.
DR UniPathway; UPA00056; UER00092.
DR GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1740.10; -; 1.
DR InterPro; IPR003821; DXP_reductoisomerase.
DR InterPro; IPR013644; DXP_reductoisomerase_C.
DR InterPro; IPR026877; DXPR_C.
DR InterPro; IPR036169; DXPR_C_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; 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.
PE 2: Evidence at transcript level;
KW Isomerase {ECO:0000313|EMBL:AFS28671.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1..30
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08436"
FT DOMAIN 62..183
FT /note="DXP reductoisomerase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13288"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFS28671.1"
FT NON_TER 199
FT /evidence="ECO:0000313|EMBL:AFS28671.1"
SQ SEQUENCE 199 AA; 22303 MW; E72E1DE0039F2613 CRC64;
PNWNMGKKIT VDSATLFNKG LEVIEAHYLF GAEYDDIEIV IHPQSXIHSM IETQDSSVLA
QLGWPDMRLP ILYTLSWPDR ISCSEITWPR LDLCKLGSLT FKAPDNVKYP SMDLAYAAGR
AGGTMTGVLS AANEKAVELF IDEKISYLDI FKFVELTCDK HRSELVSXPS LEEIIHYDLW
ARDYAXSLQL SAGLSPVLV
//