DXR_THEMA
ID DXR_THEMA Reviewed; 376 AA.
AC Q9WZZ1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183};
DE Short=DXP reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183};
DE EC=1.1.1.267 {ECO:0000255|HAMAP-Rule:MF_00183};
DE AltName: Full=1-deoxyxylulose-5-phosphate reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183};
DE AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00183};
GN Name=dxr {ECO:0000255|HAMAP-Rule:MF_00183}; OrderedLocusNames=TM_0889;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction of
CC 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-
CC phosphate (MEP). {ECO:0000255|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:0000255|HAMAP-Rule:MF_00183};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00183}.
CC -!- SIMILARITY: Belongs to the DXR family. {ECO:0000255|HAMAP-
CC Rule:MF_00183}.
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DR EMBL; AE000512; AAD35970.1; -; Genomic_DNA.
DR PIR; B72321; B72321.
DR RefSeq; NP_228697.1; NC_000853.1.
DR RefSeq; WP_004080699.1; NZ_CP011107.1.
DR PDB; 3A06; X-ray; 2.00 A; A/B=1-376.
DR PDB; 3A14; X-ray; 2.00 A; A/B=1-376.
DR PDBsum; 3A06; -.
DR PDBsum; 3A14; -.
DR AlphaFoldDB; Q9WZZ1; -.
DR SMR; Q9WZZ1; -.
DR STRING; 243274.THEMA_00190; -.
DR EnsemblBacteria; AAD35970; AAD35970; TM_0889.
DR KEGG; tma:TM0889; -.
DR eggNOG; COG0743; Bacteria.
DR InParanoid; Q9WZZ1; -.
DR OMA; PIDSEHF; -.
DR OrthoDB; 1200722at2; -.
DR BRENDA; 1.1.1.267; 6331.
DR UniPathway; UPA00056; UER00092.
DR EvolutionaryTrace; Q9WZZ1; -.
DR Proteomes; UP000008183; Chromosome.
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 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; PTHR30525; 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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF69055; SSF69055; 1.
DR TIGRFAMs; TIGR00243; Dxr; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isoprene biosynthesis; Metal-binding; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..376
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase"
FT /id="PRO_0000163723"
FT BINDING 9..37
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 142
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 144
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 209
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:3A06"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:3A06"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:3A06"
FT STRAND 28..38
FT /evidence="ECO:0007829|PDB:3A06"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:3A06"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:3A06"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:3A06"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:3A06"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3A06"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:3A06"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:3A06"
FT HELIX 118..134
FT /evidence="ECO:0007829|PDB:3A06"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:3A06"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:3A06"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:3A06"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:3A06"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:3A06"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:3A06"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:3A06"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:3A06"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:3A06"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:3A06"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:3A06"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:3A06"
FT HELIX 255..263
FT /evidence="ECO:0007829|PDB:3A06"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:3A06"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:3A06"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:3A06"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:3A06"
FT HELIX 303..321
FT /evidence="ECO:0007829|PDB:3A06"
FT HELIX 329..339
FT /evidence="ECO:0007829|PDB:3A06"
FT TURN 340..343
FT /evidence="ECO:0007829|PDB:3A06"
FT HELIX 350..371
FT /evidence="ECO:0007829|PDB:3A06"
SQ SEQUENCE 376 AA; 42200 MW; C0D3B68DB0C4BF57 CRC64;
MEERTLVILG ATGSIGTQTL DVLKKVKGIR LIGISFHSNL ELAFKIVKEF NVKNVAITGD
VEFEDSSINV WKGSHSIEEM LEALKPDITM VAVSGFSGLR AVLASLEHSK RVCLANKESL
VCGGFLVKKK LKEKGTELIP VDSEHSAIFQ VMEPEVEKVV LTASGGALRD WKISKIDRAR
PEDVLKHPVW NMGARITVDS ATMVNKAFEV LEAMELFELP FEKIEVKIHR EGLVHGAVVL
PDGNVKMVVS PPDMRIPISY ALFYPRRVAL EPFFLRTISL SFEDPDPEKY PAFFLLKEIK
DSYALRTAFN AADEVAVEAF LKGRIRFGGI HRVIEKTLEE FQGYPQPRTL DDVERIHFEA
IKKAERVTEW LSSTSY
