DXR_ZYMMO
ID DXR_ZYMMO Reviewed; 388 AA.
AC Q9X5F2; Q5NND6; Q9RIA9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 144.
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=ZMO1150;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=11004410; DOI=10.1111/j.1574-6968.2000.tb09329.x;
RA Grolle S., Bringer-Meyer S., Sahm H.;
RT "Isolation of the dxr gene of Zymomonas mobilis and characterization of the
RT 1-deoxy-D-xylulose 5-phosphate reductoisomerase.";
RL FEMS Microbiol. Lett. 191:131-137(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Lee H.J., Kang H.S.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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).
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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Note=Divalent cation. Prefers Mg(2+), Mn(2+) or Co(2+).;
CC -!- ACTIVITY REGULATION: Inhibited by fosmidomycin.
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 -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the DXR family. {ECO:0000255|HAMAP-
CC Rule:MF_00183}.
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DR EMBL; AJ250714; CAB60758.1; -; Genomic_DNA.
DR EMBL; AF124757; AAD29659.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV89774.1; -; Genomic_DNA.
DR RefSeq; WP_011240977.1; NZ_CP035711.1.
DR PDB; 1R0K; X-ray; 1.91 A; A/B/C/D=1-388.
DR PDB; 1R0L; X-ray; 2.70 A; A/B/C/D=1-388.
DR PDBsum; 1R0K; -.
DR PDBsum; 1R0L; -.
DR AlphaFoldDB; Q9X5F2; -.
DR SMR; Q9X5F2; -.
DR STRING; 264203.ZMO1150; -.
DR EnsemblBacteria; AAV89774; AAV89774; ZMO1150.
DR GeneID; 58026925; -.
DR KEGG; zmo:ZMO1150; -.
DR eggNOG; COG0743; Bacteria.
DR HOGENOM; CLU_035714_4_0_5; -.
DR OMA; PIDSEHF; -.
DR OrthoDB; 1200722at2; -.
DR UniPathway; UPA00056; UER00092.
DR EvolutionaryTrace; Q9X5F2; -.
DR Proteomes; UP000001173; Chromosome.
DR GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:UniProtKB-UniRule.
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 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; Cobalt; Isoprene biosynthesis; Magnesium; Manganese;
KW Metal-binding; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..388
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase"
FT /id="PRO_0000163747"
FT BINDING 10..39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 150
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 152
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 221
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT CONFLICT 226
FT /note="Y -> F (in Ref. 1; CAB60758)"
FT /evidence="ECO:0000305"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:1R0K"
FT STRAND 31..40
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:1R0K"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:1R0K"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1R0K"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:1R0K"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:1R0K"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:1R0K"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1R0K"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:1R0K"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 206..213
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 216..229
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:1R0K"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:1R0K"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:1R0K"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 267..275
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:1R0K"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:1R0K"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 306..317
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 321..337
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 345..356
FT /evidence="ECO:0007829|PDB:1R0K"
FT HELIX 365..384
FT /evidence="ECO:0007829|PDB:1R0K"
SQ SEQUENCE 388 AA; 41858 MW; 373EB372AA325AAF CRC64;
MSQPRTVTVL GATGSIGHST LDLIERNLDR YQVIALTANR NVKDLADAAK RTNAKRAVIA
DPSLYNDLKE ALAGSSVEAA AGADALVEAA MMGADWTMAA IIGCAGLKAT LAAIRKGKTV
ALANKESLVS AGGLMIDAVR EHGTTLLPVD SEHNAIFQCF PHHNRDYVRR IIITASGGPF
RTTSLAEMAT VTPERAVQHP NWSMGAKISI DSATMMNKGL ELIEAYHLFQ IPLEKFEILV
HPQSVIHSMV EYLDGSILAQ IGSPDMRTPI GHTLAWPKRM ETPAESLDFT KLRQMDFEAP
DYERFPALTL AMESIKSGGA RPAVMNAANE IAVAAFLDKK IGFLDIAKIV EKTLDHYTPA
TPSSLEDVFA IDNEARIQAA ALMESLPA
