O96693 (DXR_PLAFX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplast
Short name=1-deoxyxylulose-5-phosphate reductoisomerase
Short name=DOXP reductoisomerase
Short name=DXP reductoisomerase
EC=1.1.1.267

Gene names

Name:

DXR

Organism

Plasmodium falciparum (isolate HB3)

Taxonomic identifier

137071 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Laverania) › Plasmodium falciparum

Protein attributes

Sequence length	488 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP). Ref.1
Catalytic activity	2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH. Ref.1
Cofactor	Binds 1 divalent cation per subunit. Magnesium or manganese. Ref.2
Enzyme regulation	Inhibited by fosmidomycin and its derivative FT900098. Ref.1
Pathway	Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. HAMAP-Rule MF_00183
Subunit structure	Homodimer. Ref.2
Subcellular location	Plastid › apicoplast Ref.1.
Sequence similarities	Belongs to the DXR family.

Ontologies

Keywords
Biological process	Isoprene biosynthesis
Cellular component	Apicoplast Plastid
Domain	Transit peptide
Ligand	Magnesium Manganese Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	isopentenyl diphosphate biosynthetic process, mevalonate-independent pathway Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	apicoplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	1-deoxy-D-xylulose-5-phosphate reductoisomerase activity Inferred from electronic annotation. Source: EC NADPH binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 72

72

Apicoplast Probable

Chain

73 – 488

416

1-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplast HAMAP-Rule MF_00183

PRO_0000415608

Regions

Nucleotide binding

84 – 89

6

NADP HAMAP-Rule MF_00183

Nucleotide binding

113 – 117

5

NADP HAMAP-Rule MF_00183

Region

269 – 270

2

Binding to substrate phosphate group HAMAP-Rule MF_00183

Region

311 – 315

5

Substrate binding HAMAP-Rule MF_00183

Sites

Metal binding

231

1

Divalent metal cation

Metal binding

233

1

Divalent metal cation

Metal binding

315

1

Divalent metal cation

Binding site

136

1

NADP

Binding site

205

1

Substrate

Binding site

206

1

NADP

Binding site

232

1

Substrate

Binding site

293

1

Substrate

Secondary structure

1

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488

Helix Strand Turn

Details...

Beta strand

78 – 84

7

Helix

88 – 103

16

Beta strand

107 – 116

10

Helix

118 – 128

11

Beta strand

131 – 136

6

Helix

138 – 140

3

Helix

142 – 145

4

Helix

147 – 150

4

Beta strand

157 – 160

4

Helix

161 – 170

10

Beta strand

176 – 179

4

Helix

183 – 195

13

Beta strand

199 – 202

4

Helix

206 – 221

16

Beta strand

226 – 229

4

Helix

232 – 240

9

Helix

243 – 246

4

Beta strand

251 – 253

3

Helix

256 – 259

4

Beta strand

262 – 269

8

Turn

273 – 276

4

Helix

279 – 282

4

Turn

287 – 289

3

Helix

301 – 307

7

Helix

310 – 323

14

Helix

327 – 329

3

Beta strand

330 – 334

5

Beta strand

340 – 346

7

Beta strand

351 – 355

5

Helix

361 – 369

9

Helix

383 – 386

4

Beta strand

388 – 390

3

Turn

396 – 398

3

Helix

400 – 411

12

Helix

415 – 431

17

Helix

437 – 450

14

Helix

460 – 483

24

Sequences

	Sequence		Length	Mass (Da)
	O96693 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 4E280C81CDFAD3EF	FASTA	488	55,757
	10 20 30 40 50 60 MKKYIYIYFF FITITINDLV INNTSKCVSI ERRKNNAYIN YGIGYNGPDN KITKSRRCKR 70 80 90 100 110 120 IKLCKKDLID IGAIKKPINV AIFGSTGSIG TNALNIIREC NKIENVFNVK ALYVNKSVNE 130 140 150 160 170 180 LYEQAREFLP EYLCIHDKSV YEELKELVKN IKDYKPIILC GDEGMKEICS SNSIDKIVIG 190 200 210 220 230 240 IDSFQGLYST MYAIMNNKIV ALANKESIVS AGFFLKKLLN IHKNAKIIPV DSEHSAIFQC 250 260 270 280 290 300 LDNNKVLKTK CLQDNFSKIN NINKIFLCSS GGPFQNLTMD ELKNVTSENA LKHPKWKMGK 310 320 330 340 350 360 KITIDSATMM NKGLEVIETH FLFDVDYNDI EVIVHKECII HSCVEFIDKS VISQMYYPDM 370 380 390 400 410 420 QIPILYSLTW PDRIKTNLKP LDLAQVSTLT FHKPSLEHFP CIKLAYQAGI KGNFYPTVLN 430 440 450 460 470 480 ASNEIANNLF LNNKIKYFDI SSIISQVLES FNSQKVSENS EDLMKQILQI HSWAKDKATD IYNKHNSS

References

[1]

"Inhibitors of the nonmevalonate pathway of isoprenoid biosynthesis as antimalarial drugs." Jomaa H., Wiesner J., Sanderbrand S., Altincicek B., Weidemeyer C., Hintz M., Turbachova I., Eberl M., Zeidler J., Lichtenthaler H.K., Soldati D., Beck E. Science 285:1573-1576(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION. Strain: Isolate HB3.

[2]

"Molecular basis of fosmidomycin's action on the human malaria parasite Plasmodium falciparum." Umeda T., Tanaka N., Kusakabe Y., Nakanishi M., Kitade Y., Nakamura K.T. Sci. Rep. 1:E9-E9(2011) Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEXES WITH NADPH; FOSMIDOMYCIN DERIVATIVE FR900098; MAGNESIUM AND MANGANESE, COFACTOR, SUBUNIT. Strain: Isolate FCR-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF111813 Genomic DNA. Translation: AAD03739.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3AU8	X-ray	1.86	A/B	1-488	[»]
3AU9	X-ray	1.90	A/B	1-488	[»]
3AUA	X-ray	2.15	A/B	1-488	[»]
4GAE	X-ray	2.30	A/B	75-488	[»]

ProteinModelPortal

O96693.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

1.1.1.267. 1455.

UniPathway

UPA00056; UER00092.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

HAMAP

MF_00183. DXP_reductoisom.

InterPro

IPR003821. DXP_reductoisomerase.
IPR013644. DXP_reductoisomerase_C.
IPR013512. DXP_reductoisomerase_N.
IPR026877. DXPR_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

PANTHER

PTHR30525. PTHR30525. 1 hit.

Pfam

PF08436. DXP_redisom_C. 1 hit.
PF02670. DXP_reductoisom. 1 hit.
PF13288. DXPR_C. 1 hit.
[Graphical view]

SUPFAM

SSF69055. SSF69055. 1 hit.

TIGRFAMs

TIGR00243. Dxr. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

O96693.

Entry information

Entry name

DXR_PLAFX

Accession

Primary (citable) accession number: O96693

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 22, 2012
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)