Q62JD0 (DXR_BURMA) 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:	BMA1549

Organism

Burkholderia mallei (Pseudomonas mallei) [Complete proteome] [HAMAP]

Taxonomic identifier

13373 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	398 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
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 – 398	398	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_0000163624
Regions
	Nucleotide binding	8 – 37	30	NADP By similarity
Sites
	Metal binding	151	1	Divalent metal cation By similarity
	Metal binding	153	1	Divalent metal cation By similarity
	Metal binding	224	1	Divalent metal cation By similarity
	Binding site	126	1	Substrate By similarity
	Binding site	153	1	Substrate By similarity
	Binding site	179	1	Substrate By similarity
	Binding site	202	1	Substrate By similarity
	Binding site	224	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q62JD0 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 6500410CBCAA8463	FASTA	398	41,622
	10 20 30 40 50 60 MQKRLTLLGS TGSIGDSTLD VVARHPERFA VHALTAHRNG EKLVAQCLRF APDVAVVGDA 70 80 90 100 110 120 ETAARVEAQL RAAGSRTQVA YGKQALVDVS KSDGCDTVVA AIVGAAGLAP SLAAARAGKR 130 140 150 160 170 180 ILLANKEALV MSGAIFMDAV RDHGAILLPV DSEHNAIFQC MPRDAAEHGG IAKIIVTASG 190 200 210 220 230 240 GPFRTREPAT LASVTPDEAC KHPNWVMGRK ISVDSATMMN KGLEVIEAHW LFGLPSEHID 250 260 270 280 290 300 VLIHPQSVIH SLVSYRDGSV LAQLGNPDMR TPIAHALAFP ERVDAGVAQL DLAQIATLTF 310 320 330 340 350 360 EKPDYARFPC LALAIDALEA GGVASAALNA ANEIAVDAFL SRRIRFTAIA QTVGAVLDGL 370 380 390 SNRTPGGLDD VIEADAAARR AATAFIGKLP APGVERAA

References

[1]

"Structural flexibility in the Burkholderia mallei genome." Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E., Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C., Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Khouri H.M. , Kolonay J.F., Madupu R., Mohammoud Y., Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C., Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004) [PubMed: 15377793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 23344.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000010 Genomic DNA. Translation: AAU47749.1.
RefSeq	YP_103189.1. NC_006348.1.
3D structure databases
ProteinModelPortal	Q62JD0.
SMR	Q62JD0. Positions 2-392.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3088281.
GenomeReviews	Gene locus BMA1549 in contig CP000010_GR.
KEGG	bma:BMA1549.
PATRIC	19118154. VBIBurMal55007_1594.
TIGR	BMA1549.
Phylogenomic databases
HOGENOM	HBG430762.
OMA	IHSMVEY.
PhylomeDB	Q62JD0.
ProtClustDB	PRK05447.
Enzyme and pathway databases
BioCyc	BMAL243160:BMA_1549-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_BURMA

Accession

Primary (citable) accession number: Q62JD0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program