ID A0A1H9NYN2_9CORY Unreviewed; 387 AA.
AC A0A1H9NYN2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00183};
DE Short=DXP reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00183};
DE EC=1.1.1.267 {ECO:0000256|HAMAP-Rule:MF_00183};
DE AltName: Full=1-deoxyxylulose-5-phosphate reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00183};
DE AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00183};
GN Name=dxr {ECO:0000256|HAMAP-Rule:MF_00183};
GN ORFNames=SAMN05661109_00153 {ECO:0000313|EMBL:SER41042.1};
OS Corynebacterium cystitidis DSM 20524.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1121357 {ECO:0000313|EMBL:SER41042.1, ECO:0000313|Proteomes:UP000198929};
RN [1] {ECO:0000313|EMBL:SER41042.1, ECO:0000313|Proteomes:UP000198929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20524 {ECO:0000313|EMBL:SER41042.1,
RC ECO:0000313|Proteomes:UP000198929};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NADPH-dependent rearrangement and reduction of
CC 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-
CC phosphate (MEP). {ECO:0000256|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: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|HAMAP-Rule:MF_00183};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|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:0000256|ARBA:ARBA00005094, ECO:0000256|HAMAP-
CC Rule:MF_00183}.
CC -!- SIMILARITY: Belongs to the DXR family. {ECO:0000256|ARBA:ARBA00006825,
CC ECO:0000256|HAMAP-Rule:MF_00183}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00183}.
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DR EMBL; FOGQ01000001; SER41042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9NYN2; -.
DR STRING; 1121357.SAMN05661109_00153; -.
DR UniPathway; UPA00056; UER00092.
DR Proteomes; UP000198929; Unassembled WGS sequence.
DR GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:UniProtKB-UniRule.
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 GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
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 Isomerase {ECO:0000313|EMBL:SER41042.1};
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP-
KW Rule:MF_00183}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00183};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00183};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00183};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00183};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00183}.
FT DOMAIN 5..131
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02670"
FT DOMAIN 143..226
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08436"
FT DOMAIN 259..376
FT /note="DXP reductoisomerase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13288"
FT BINDING 11
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 12
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 13
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 14
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 37
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 40
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 123
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 124
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 125
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 147
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 148
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 149
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 149
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 173
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 196
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 202
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 209
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 214
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 215
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 218
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT BINDING 218
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
SQ SEQUENCE 387 AA; 40771 MW; AC6325CAFF812605 CRC64;
MKKKIVILGS TGSIGTQAIE VVEANPDRFE VVGISAAGSN PNLVVQQARA LRLSAEQVAV
AKPEAARQVS QELGGTVLSG EEAARLLVDK HRADTVLNGL VGSMGLAATL ATLKTGVTLA
LANKESLVAG GTFVTSQAQP GQIVPVDSEH SAMAQCLRAG RADEVARYVL TASGGPFRGQ
TREQMWDVTP EQAAAHPTWS MGQMNTLNSA TMVNKGLELI EATLLFNVAP ELIDVTVHPQ
SIIHSAVTFV DGSTIAQASP PSMKLPISHA LAWPRRVADA QPALDFSQSH DWRFEPLDDE
AFPAVQLARD VATQGGTFPA VYNAANEEAA AAFLGGRIRF PQIVDVVAEI VGGAADFAVP
ATSFEDVVTV EDEARRRANA LIDEIAD
//
