B1JUE4 (DXR_BURCC) 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:	Bcenmc03_2033

Organism

Burkholderia cenocepacia (strain MC0-3) [Complete proteome] [HAMAP]

Taxonomic identifier

406425 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

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_1000098476
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)
	B1JUE4 [UniParc]. Last modified April 29, 2008. Version 1. Checksum: F8E11B68AA2256C5	FASTA	398	41,924
	10 20 30 40 50 60 MQKRLTLLGS TGSIGDSTLD VVARHPERFS VYALTAHRNG DKLVEQCLRF APEVAVVGDA 70 80 90 100 110 120 ATAAHVDAKL RAAGSKTVVL HGPQALVDVS KSDGCDTVVA AIVGAAGLAP SLAAARAGKR 130 140 150 160 170 180 ILLANKEALV MSGAIFMDAV RDHGAILLPV DSEHNAIFQC MPRDAAEHGG ISKIILTASG 190 200 210 220 230 240 GPFRTREPAT LVDVTPDEAC KHPNWVMGRK ISVDSATMMN KGLEVIEAHW IFGLPGDRID 250 260 270 280 290 300 VLIHPQSVIH SLVSYRDGSV LAQLGNPDMR TPIAHALAFP ERVDAGVDQL DLAQIAQLSF 310 320 330 340 350 360 EKPDYARFPC LALALKALEE GGIASAALNA ANEVAVEAFL ERRIGFMAIA ATVDAVLNTL 370 380 390 PNRAPDGLDD VLAADAEARR LAAAIIAKAP APRVERTV

References

[1]

"Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-3." Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. , Kyrpides N., Mikhailova N., Tiedje J., Richardson P. Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MC0-3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000958 Genomic DNA. Translation: ACA91194.1.
RefSeq	YP_001765316.1. NC_010508.1.
3D structure databases
ProteinModelPortal	B1JUE4.
SMR	B1JUE4. Positions 2-391.
ModBase	Search...
Protein-protein interaction databases
STRING	B1JUE4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6123697.
GenomeReviews	Gene locus Bcenmc03_2033 in contig CP000958_GR.
KEGG	bcm:Bcenmc03_2033.
PATRIC	19091195. VBIBurCen61509_2102.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG430762.
OMA	IHSMVEY.
ProtClustDB	PRK05447.
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_BURCC

Accession

Primary (citable) accession number: B1JUE4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	April 29, 2008
Last modified:	January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program