DXR

Functionⁱ

Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).By similarity

Catalytic activityⁱ

2-C-methyl-D-erythritol 4-phosphate + NADP⁺ = 1-deoxy-D-xylulose 5-phosphate + NADPH.

Cofactorⁱ

Mg²⁺By similarity, Mn²⁺By similarityNote: Binds 1 divalent cation per subunit. Mg²⁺ or Mn²⁺.By similarity

Pathwayⁱ: isopentenyl diphosphate biosynthesis via DXP pathway

This protein is involved in step 1 of the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:

1-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplastic (DXR)
no protein annotated in this organism
no protein annotated in this organism
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ISPF)
no protein annotated in this organism
no protein annotated in this organism

This subpathway is part of the pathway isopentenyl diphosphate biosynthesis via DXP pathway, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate, the pathway isopentenyl diphosphate biosynthesis via DXP pathway and in Isoprenoid biosynthesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	136	NADPBy similarity	1
Binding siteⁱ	205	SubstrateBy similarity	1
Binding siteⁱ	206	NADPBy similarity	1
Metal bindingⁱ	231	Divalent metal cationBy similarity	1
Binding siteⁱ	232	SubstrateBy similarity	1
Metal bindingⁱ	233	Divalent metal cationBy similarity	1
Binding siteⁱ	293	SubstrateBy similarity	1
Metal bindingⁱ	315	Divalent metal cationBy similarity	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	84 – 89	NADPBy similarity		6
Nucleotide bindingⁱ	113 – 117	NADPBy similarity		5

GO - Molecular functionⁱ

1-deoxy-D-xylulose-5-phosphate reductoisomerase activity Source: GO_Central
manganese ion binding Source: GO_Central
NADPH binding Source: GO_Central

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process Source: GO_Central

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	Isoprene biosynthesis
Ligand	Magnesium, Manganese, Metal-binding, NADP

Enzyme and pathway databases

BRENDAⁱ	1.1.1.267 4889
UniPathwayⁱ	UPA00056; UER00092

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: 1-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplastic (EC:1.1.1.267) Short name: 1-deoxyxylulose-5-phosphate reductoisomerase Short name: DOXP reductoisomerase Short name: DXP reductoisomerase
Gene namesⁱ	Name:DXR ORF Names:PF14_0641
Organismⁱ	Plasmodium falciparum (isolate 3D7)
Taxonomic identifierⁱ	36329 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodiidae › Plasmodium › Plasmodium (Laverania) › Plasmodium falciparum
Proteomesⁱ	UP000001450 Componentⁱ: Chromosome 14

Organism-specific databases

EuPathDBⁱ	PlasmoDB:PF3D7_1467300

EuPathDBⁱ

PlasmoDB:PF3D7_1467300

Subcellular locationⁱ

apicoplast By similarity

GO - Cellular componentⁱ

apicoplast
Source: GeneDB
Inferred from direct assayⁱ
- 21573242

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Apicoplast, Plastid

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transit peptideⁱ	1 – 72	ApicoplastBy similarityAdd BLAST		72
ChainⁱPRO_0000415609	73 – 488	1-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplasticAdd BLAST		416

Interactionⁱ

Subunit structureⁱ

Homodimer.By similarity

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	78 – 84	Combined sources	7
Helixⁱ	88 – 103	Combined sources	16
Beta strandⁱ	107 – 116	Combined sources	10
Helixⁱ	118 – 128	Combined sources	11
Beta strandⁱ	131 – 136	Combined sources	6
Helixⁱ	138 – 140	Combined sources	3
Helixⁱ	141 – 148	Combined sources	8
Beta strandⁱ	151 – 153	Combined sources	3
Beta strandⁱ	157 – 160	Combined sources	4
Helixⁱ	161 – 170	Combined sources	10
Beta strandⁱ	176 – 179	Combined sources	4
Helixⁱ	184 – 195	Combined sources	12
Beta strandⁱ	199 – 202	Combined sources	4
Helixⁱ	205 – 221	Combined sources	17
Beta strandⁱ	226 – 229	Combined sources	4
Helixⁱ	232 – 239	Combined sources	8
Helixⁱ	243 – 246	Combined sources	4
Beta strandⁱ	251 – 253	Combined sources	3
Helixⁱ	256 – 259	Combined sources	4
Beta strandⁱ	262 – 269	Combined sources	8
Turnⁱ	273 – 276	Combined sources	4
Helixⁱ	279 – 284	Combined sources	6
Helixⁱ	287 – 291	Combined sources	5
Helixⁱ	300 – 308	Combined sources	9
Helixⁱ	310 – 323	Combined sources	14
Helixⁱ	327 – 329	Combined sources	3
Beta strandⁱ	330 – 334	Combined sources	5
Beta strandⁱ	340 – 346	Combined sources	7
Beta strandⁱ	351 – 355	Combined sources	5
Helixⁱ	361 – 369	Combined sources	9
Helixⁱ	383 – 386	Combined sources	4
Beta strandⁱ	388 – 390	Combined sources	3
Turnⁱ	396 – 398	Combined sources	3
Helixⁱ	400 – 411	Combined sources	12
Helixⁱ	415 – 431	Combined sources	17
Helixⁱ	437 – 450	Combined sources	14
Helixⁱ	460 – 485	Combined sources	26

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4Y67	X-ray	1.60	A/B	75-488	[»]
	4Y6P	X-ray	1.90	A/B	75-488	[»]
	4Y6R	X-ray	1.90	A/B	75-488	[»]
	4Y6S	X-ray	2.10	A/B	75-488	[»]
	5JAZ	X-ray	1.40	A/B	75-488	[»]
	5JBI	X-ray	1.70	A/B	75-488	[»]
	5JC1	X-ray	1.65	A/B	75-488	[»]
	5JMP	X-ray	1.70	A/B	75-488	[»]
	5JMW	X-ray	1.55	A/B	75-488	[»]
	5JNL	X-ray	1.60	A/B	75-488	[»]
	5JO0	X-ray	1.80	A/B	75-488	[»]
ProteinModelPortalⁱ	Q8IKG4
SMRⁱ	Q8IKG4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	269 – 270	Binding to substrate phosphate groupBy similarity		2
Regionⁱ	311 – 315	Substrate bindingBy similarity		5

Sequence similaritiesⁱ

Belongs to the DXR family.Curated

Keywords - Domainⁱ

Transit peptide

Phylogenomic databases

HOGENOMⁱ	HOG000007220
InParanoidⁱ	Q8IKG4
KEGG Orthology (KO) More...KOⁱ	K00099
OMAⁱ	DSEHFGL
PhylomeDBⁱ	Q8IKG4

Family and domain databases

HAMAPⁱ	MF_00183 DXP_reductoisom, 1 hit
InterProⁱ	View protein in InterPro IPR003821 DXP_reductoisomerase IPR013644 DXP_reductoisomerase_C IPR013512 DXP_reductoisomerase_N IPR026877 DXPR_C IPR036169 DXPR_C_sf IPR036291 NAD(P)-bd_dom_sf
PANTHERⁱ	PTHR30525 PTHR30525, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF08436 DXP_redisom_C, 1 hit PF02670 DXP_reductoisom, 1 hit PF13288 DXPR_C, 1 hit
SUPFAMⁱ	SSF51735 SSF51735, 1 hit SSF69055 SSF69055, 1 hit
TIGRFAMsⁱ	TIGR00243 Dxr, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

Q8IKG4-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MKKYIYIYFF FITITINDLV INNTSKCVSI ERRKNNAYIN YGIGYNGPDN 
        60         70         80         90        100
KITKSRRCKR IKLCKKDLID IGAIKKPINV AIFGSTGSIG TNALNIIREC 
       110        120        130        140        150
NKIENVFNVK ALYVNKSVNE LYEQAREFLP EYLCIHDKSV YEELKELVKN 
       160        170        180        190        200
IKDYKPIILC GDEGMKEICS SNSIDKIVIG IDSFQGLYST MYAIMNNKIV 
       210        220        230        240        250
ALANKESIVS AGFFLKKLLN IHKNAKIIPV DSEHSAIFQC LDNNKVLKTK 
       260        270        280        290        300
CLQDNFSKIN NINKIFLCSS GGPFQNLTMD ELKNVTSENA LKHPKWKMGK 
       310        320        330        340        350
KITIDSATMM NKGLEVIETH FLFDVDYNDI EVIVHKECII HSCVEFIDKS 
       360        370        380        390        400
VISQMYYPDM QIPILYSLTW PDRIKTNLKP LDLAQVSTLT FHKPSLEHFP 
       410        420        430        440        450
CIKLAYQAGI KGNFYPTVLN ASNEIANNLF LNNKIKYFDI SSIISQVLES 
       460        470        480 
FNSQKVSENS EDLMKQILQI HSWAKDKATD IYNKHNSS

Length:488

Mass (Da):55,757

Last modified:March 1, 2003 - v1

Checksum:ⁱ4E280C81CDFAD3EF

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AE014187 Genomic DNA Translation: AAN37254.1
NCBI Reference Sequences More...RefSeqⁱ	XP_001348815.1, XM_001348779.1

Genome annotation databases

GeneDBⁱ	PF3D7_1467300.1:pep
GeneIDⁱ	812223
KEGGⁱ	pfa:PF14_0641

Protein	Similar proteins		Species	Score	Length
Q8IKG4	1-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplastic	)	PLAFX		488
1-deoxy-D-xylulose 5-phosphate reductoisomerase		PLAFO		488
1-deoxy-D-xylulose 5-phosphate reductoisomerase		Plasmodium falciparum NF135/5.C10		488
1-deoxy-D-xylulose 5-phosphate reductoisomerase		Plasmodium falciparum MaliPS096_E11		488
1-deoxy-D-xylulose 5-phosphate reductoisomerase		Plasmodium falciparum UGT5.1		488
+28

Protein	Similar proteins		Species	Score	Length
Q8IKG4	1-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplastic	)	PLAFX		488
1-deoxy-D-xylulose 5-phosphate reductoisomerase		PLAFO		488
1-deoxy-D-xylulose 5-phosphate reductoisomerase		Plasmodium falciparum NF135/5.C10		488
1-deoxy-D-xylulose 5-phosphate reductoisomerase		Plasmodium falciparum MaliPS096_E11		488
1-deoxy-D-xylulose 5-phosphate reductoisomerase		Plasmodium falciparum UGT5.1		488
+63

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AE014187 Genomic DNA Translation: AAN37254.1
NCBI Reference Sequences More...RefSeqⁱ	XP_001348815.1, XM_001348779.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4Y67	X-ray	1.60	A/B	75-488	[»]
	4Y6P	X-ray	1.90	A/B	75-488	[»]
	4Y6R	X-ray	1.90	A/B	75-488	[»]
	4Y6S	X-ray	2.10	A/B	75-488	[»]
	5JAZ	X-ray	1.40	A/B	75-488	[»]
	5JBI	X-ray	1.70	A/B	75-488	[»]
	5JC1	X-ray	1.65	A/B	75-488	[»]
	5JMP	X-ray	1.70	A/B	75-488	[»]
	5JMW	X-ray	1.55	A/B	75-488	[»]
	5JNL	X-ray	1.60	A/B	75-488	[»]
	5JO0	X-ray	1.80	A/B	75-488	[»]
ProteinModelPortalⁱ	Q8IKG4
SMRⁱ	Q8IKG4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneDBⁱ	PF3D7_1467300.1:pep
GeneIDⁱ	812223
KEGGⁱ	pfa:PF14_0641

Organism-specific databases

EuPathDBⁱ	PlasmoDB:PF3D7_1467300

EuPathDBⁱ

PlasmoDB:PF3D7_1467300

Phylogenomic databases

HOGENOMⁱ	HOG000007220
InParanoidⁱ	Q8IKG4
KEGG Orthology (KO) More...KOⁱ	K00099
OMAⁱ	DSEHFGL
PhylomeDBⁱ	Q8IKG4

Enzyme and pathway databases

UniPathwayⁱ	UPA00056; UER00092
BRENDAⁱ	1.1.1.267 4889

Family and domain databases

HAMAPⁱ	MF_00183 DXP_reductoisom, 1 hit
InterProⁱ	View protein in InterPro IPR003821 DXP_reductoisomerase IPR013644 DXP_reductoisomerase_C IPR013512 DXP_reductoisomerase_N IPR026877 DXPR_C IPR036169 DXPR_C_sf IPR036291 NAD(P)-bd_dom_sf
PANTHERⁱ	PTHR30525 PTHR30525, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF08436 DXP_redisom_C, 1 hit PF02670 DXP_reductoisom, 1 hit PF13288 DXPR_C, 1 hit
SUPFAMⁱ	SSF51735 SSF51735, 1 hit SSF69055 SSF69055, 1 hit
TIGRFAMsⁱ	TIGR00243 Dxr, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	DXR_PLAF7
Accessionⁱ	Q8IKG4Primary (citable) accession number: Q8IKG4
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 22, 2012
	Last sequence update:	March 1, 2003
	Last modified:	October 25, 2017
	This is version 92 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)

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UniProtKB - Q8IKG4 (DXR_PLAF7)

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1-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplastic

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: isopentenyl diphosphate biosynthesis via DXP pathway

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Functionⁱ

Pathwayⁱ: isopentenyl diphosphate biosynthesis via DXP pathway

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ