DXR_MYCTU
ID DXR_MYCTU Reviewed; 413 AA.
AC P9WNS1; L0TDT3; P64012; Q10798;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 50.
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=Rv2870c;
GN ORFNames=MTCY274.01c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP45672.1; -; Genomic_DNA.
DR PIR; A70923; A70923.
DR RefSeq; NP_217386.2; NC_000962.3.
DR RefSeq; WP_003414613.1; NZ_NVQJ01000006.1.
DR PDB; 2C82; X-ray; 1.90 A; A/B=1-413.
DR PDB; 2JCV; X-ray; 2.20 A; A/B=2-389.
DR PDB; 2JCX; X-ray; 2.10 A; A/B=2-389.
DR PDB; 2JCY; X-ray; 2.35 A; A/B=2-389.
DR PDB; 2JD0; X-ray; 2.30 A; A/B=2-389.
DR PDB; 2JD1; X-ray; 2.00 A; A/B=2-389.
DR PDB; 2JD2; X-ray; 2.15 A; A/B=2-389.
DR PDB; 2Y1C; X-ray; 1.90 A; A/B=2-389.
DR PDB; 2Y1D; X-ray; 2.05 A; A/B=2-389.
DR PDB; 2Y1E; X-ray; 1.65 A; A/B=2-389.
DR PDB; 2Y1F; X-ray; 1.96 A; A/B=2-389.
DR PDB; 2Y1G; X-ray; 1.95 A; A/B=2-389.
DR PDB; 3RAS; X-ray; 2.55 A; A/B=2-389.
DR PDB; 3ZHX; X-ray; 2.00 A; A/B=2-389.
DR PDB; 3ZHY; X-ray; 2.30 A; A/B=2-389.
DR PDB; 3ZHZ; X-ray; 2.25 A; A/B=2-389.
DR PDB; 3ZI0; X-ray; 1.90 A; A/B=2-389.
DR PDB; 4A03; X-ray; 1.65 A; A/B=2-389.
DR PDB; 4AIC; X-ray; 2.05 A; A/B=2-389.
DR PDB; 4OOE; X-ray; 1.83 A; A/B/C/D=1-389.
DR PDB; 4OOF; X-ray; 2.30 A; A/B=1-389.
DR PDB; 4RCV; X-ray; 2.29 A; A/B=1-389.
DR PDBsum; 2C82; -.
DR PDBsum; 2JCV; -.
DR PDBsum; 2JCX; -.
DR PDBsum; 2JCY; -.
DR PDBsum; 2JD0; -.
DR PDBsum; 2JD1; -.
DR PDBsum; 2JD2; -.
DR PDBsum; 2Y1C; -.
DR PDBsum; 2Y1D; -.
DR PDBsum; 2Y1E; -.
DR PDBsum; 2Y1F; -.
DR PDBsum; 2Y1G; -.
DR PDBsum; 3RAS; -.
DR PDBsum; 3ZHX; -.
DR PDBsum; 3ZHY; -.
DR PDBsum; 3ZHZ; -.
DR PDBsum; 3ZI0; -.
DR PDBsum; 4A03; -.
DR PDBsum; 4AIC; -.
DR PDBsum; 4OOE; -.
DR PDBsum; 4OOF; -.
DR PDBsum; 4RCV; -.
DR AlphaFoldDB; P9WNS1; -.
DR SMR; P9WNS1; -.
DR STRING; 83332.Rv2870c; -.
DR BindingDB; P9WNS1; -.
DR ChEMBL; CHEMBL5630; -.
DR SwissLipids; SLP:000001174; -.
DR PaxDb; P9WNS1; -.
DR DNASU; 887800; -.
DR GeneID; 45426858; -.
DR GeneID; 887800; -.
DR KEGG; mtu:Rv2870c; -.
DR TubercuList; Rv2870c; -.
DR eggNOG; COG0743; Bacteria.
DR OMA; PIDSEHF; -.
DR PhylomeDB; P9WNS1; -.
DR BRENDA; 1.1.1.267; 3445.
DR UniPathway; UPA00056; UER00092.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IDA:MTBBASE.
DR GO; GO:0050897; F:cobalt ion binding; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0030145; F:manganese ion binding; IDA:MTBBASE.
DR GO; GO:0070402; F:NADPH binding; IDA:MTBBASE.
DR GO; GO:0051484; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process; IDA:MTBBASE.
DR GO; GO:0051483; P:terpenoid biosynthetic process, mevalonate-independent; IMP:MTBBASE.
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..413
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase"
FT /id="PRO_0000163678"
FT BINDING 18..47
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 151
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 153
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 222
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:4A03"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:4A03"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:4A03"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3ZHZ"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:4A03"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:4A03"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:4A03"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:4A03"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:4A03"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:2JD2"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4A03"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:4A03"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:4A03"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:3ZHX"
FT HELIX 207..215
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 217..230
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:4A03"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:4A03"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:4A03"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 268..276
FT /evidence="ECO:0007829|PDB:4A03"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:4A03"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 322..338
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 346..356
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:4A03"
FT HELIX 368..386
FT /evidence="ECO:0007829|PDB:4A03"
SQ SEQUENCE 413 AA; 42853 MW; 44E19577CE4D814F CRC64;
MTNSTDGRAD GRLRVVVLGS TGSIGTQALQ VIADNPDRFE VVGLAAGGAH LDTLLRQRAQ
TGVTNIAVAD EHAAQRVGDI PYHGSDAATR LVEQTEADVV LNALVGALGL RPTLAALKTG
ARLALANKES LVAGGSLVLR AARPGQIVPV DSEHSALAQC LRGGTPDEVA KLVLTASGGP
FRGWSAADLE HVTPEQAGAH PTWSMGPMNT LNSASLVNKG LEVIETHLLF GIPYDRIDVV
VHPQSIIHSM VTFIDGSTIA QASPPDMKLP ISLALGWPRR VSGAAAACDF HTASSWEFEP
LDTDVFPAVE LARQAGVAGG CMTAVYNAAN EEAAAAFLAG RIGFPAIVGI IADVLHAADQ
WAVEPATVDD VLDAQRWARE RAQRAVSGMA SVAIASTAKP GAAGRHASTL ERS
