O66722 (DXR_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
1-deoxyxylulose-5-phosphate reductoisomerase
2-C-methyl-D-erythritol 4-phosphate synthase

Gene names

Name:	dxr
Ordered Locus Names:	aq_404

Organism

Aquifex aeolicus (strain VF5)

Taxonomic identifier

224324 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	380 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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) By similarity. HAMAP MF_00183
Catalytic activity	2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH. HAMAP MF_00183
Cofactor	Divalent cation By similarity. HAMAP MF_00183
Pathway	Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. HAMAP MF_00183
Sequence similarities	Belongs to the DXR family.

Ontologies

Keywords
Biological process	Isoprene biosynthesis
Ligand	Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	isoprenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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
	Chain	1 – 380	380	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_0000163598
Regions
	Nucleotide binding	6 – 35	30	NADP By similarity
Sites
	Metal binding	139	1	Divalent metal cation By similarity
	Metal binding	141	1	Divalent metal cation By similarity
	Metal binding	210	1	Divalent metal cation By similarity
	Binding site	118	1	Substrate By similarity
	Binding site	141	1	Substrate By similarity
	Binding site	165	1	Substrate By similarity
	Binding site	188	1	Substrate By similarity
	Binding site	210	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O66722 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 405A54733E892831	FASTA	380	42,963
	10 20 30 40 50 60 MKLGVLGSTG SVGSQTLQVY ENFRDEIELV GILANRASEK LLQQAKKYKP KYVVSYQEPA 70 80 90 100 110 120 KEWLESLPEG VKYLKGDEGL KAIIEESERL MNAISGIYGI KPAYEVIKAG KTLLASNKES 130 140 150 160 170 180 ILCLGEIIRK NRERVIPVDS EHNALFQLLS SVKREEVKHV YLTASGGPFK DKSLEELKTA 190 200 210 220 230 240 SVEEALRHPR WNMGAKITID SATLMNKGFE MLEAHFLFDF PIENIKVVIH PQSFVHGILE 250 260 270 280 290 300 LIDNSFLMHT SQTDMKIPIM HALFYPKRKE YPFKKVSLLE LSPITFEKVD TTKFKAIDLA 310 320 330 340 350 360 KWAGFMGGVY IPVLVGADEE AVNLFLNKKI GFLDIVDLIE QALSEVNIKD PQSVEEILEA 370 380 VEWGRQKVRE IYERKYAGKG

References

[1]	"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000657 Genomic DNA. Translation: AAC06688.1.
PIR	F70336.
RefSeq	NP_213282.1. NC_000918.1.
3D structure databases
ProteinModelPortal	O66722.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1193048.
GenomeReviews	Gene locus aq_404 in contig AE000657_GR.
KEGG	aae:aq_404.
NMPDR	fig|224324.1.peg.297.
PATRIC	20958392. VBIAquAeo85532_0332.
Phylogenomic databases
HOGENOM	HBG430762.
OMA	IHSMVEY.
PhylomeDB	O66722.
ProtClustDB	PRK05447.
Enzyme and pathway databases
BioCyc	AAEO224324:AQ_404-MONOMER.
Family and domain databases
HAMAP	MF_00183. DXP_reductoisom. [Tree]
InterPro	IPR003821. DXP_reductoisomerase. IPR013644. DXP_reductoisomerase_C. IPR013512. DXP_reductoisomerase_N. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00099.
Pfam	PF08436. DXP_redisom_C. 1 hit. PF02670. DXP_reductoisom. 1 hit. [Graphical view]
PIRSF	PIRSF006205. Dxp_reductismrs. 1 hit.
TIGRFAMs	TIGR00243. Dxr. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DXR_AQUAE

Accession

Primary (citable) accession number: O66722

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	August 1, 1998
Last modified:	January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program