DXR_YERPY
ID DXR_YERPY Reviewed; 398 AA.
AC B1JQG4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=YPK_1070;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPIII;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Homodimer. {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; CP000950; ACA67371.1; -; Genomic_DNA.
DR RefSeq; WP_002212135.1; NZ_CP009792.1.
DR PDB; 3IIE; X-ray; 2.21 A; A/B=1-398.
DR PDBsum; 3IIE; -.
DR AlphaFoldDB; B1JQG4; -.
DR SMR; B1JQG4; -.
DR EnsemblBacteria; ACA67371; ACA67371; YPK_1070.
DR GeneID; 57977513; -.
DR KEGG; ypy:YPK_1070; -.
DR PATRIC; fig|502800.11.peg.1702; -.
DR OMA; PIDSEHF; -.
DR UniPathway; UPA00056; UER00092.
DR EvolutionaryTrace; B1JQG4; -.
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; Isoprene biosynthesis; Metal-binding; NADP; Oxidoreductase.
FT CHAIN 1..398
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase"
FT /id="PRO_1000098532"
FT BINDING 7..36
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 186
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 231
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:3IIE"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:3IIE"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:3IIE"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:3IIE"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:3IIE"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:3IIE"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:3IIE"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:3IIE"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:3IIE"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:3IIE"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:3IIE"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:3IIE"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:3IIE"
FT HELIX 126..142
FT /evidence="ECO:0007829|PDB:3IIE"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:3IIE"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:3IIE"
FT HELIX 162..166
FT /evidence="ECO:0007829|PDB:3IIE"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:3IIE"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:3IIE"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:3IIE"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:3IIE"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:3IIE"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:3IIE"
FT HELIX 217..223
FT /evidence="ECO:0007829|PDB:3IIE"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:3IIE"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:3IIE"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:3IIE"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:3IIE"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:3IIE"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:3IIE"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:3IIE"
FT HELIX 316..327
FT /evidence="ECO:0007829|PDB:3IIE"
FT HELIX 329..347
FT /evidence="ECO:0007829|PDB:3IIE"
FT HELIX 355..365
FT /evidence="ECO:0007829|PDB:3IIE"
FT HELIX 375..394
FT /evidence="ECO:0007829|PDB:3IIE"
SQ SEQUENCE 398 AA; 43115 MW; C9B1FC9E0166D057 CRC64;
MKQLTILGST GSIGNSTLSV VRANPELFKV TALVAGRNVR EMAQQCLEFS PRYAAMSDEH
SAKSLRLLLA EQGSDTEVYS GETAACELAA LDDVDQVMAA IVGIAGLPST LAAIRAGKQV
LLANKESLIT CGKLFMDEVK RSRAQLLPID SEHNAIFQSL PERIQRQLGY SSLNENGVSR
IILTGSGGPF RETPLSQFSD VTPDQACAHP NWSMGRKISV DSATMMNKGL EYIEARWLFN
ASAEQIEVVL HPQSVIHSMV RYHDGSILAQ MGTPDMRTPI AHAMAYPMRV SSGVAPLDFC
KVGALTFTTP DYQRYPCLKL AIDACNAGQA ATTALNAANE ISVMAFLDSK IRFTDIEVIN
RTVVEGLLLS EPTSVEEVLV IDRKARDVAA QVIAKLNN
