Reviewed, UniProtKB/Swiss-Prot Q2SWZ2 (DXR_BURTA)

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:	BTH_I2033

Organism

Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]

Taxonomic identifier

271848 [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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW terpenoid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	1-deoxy-D-xylulose-5-phosphate reductoisomerase activity Inferred from electronic annotation. Source: HAMAP 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_1000020233
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)
	Q2SWZ2-1 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 128F3E70D3E00690	FASTA	398	41,724
	10 20 30 40 50 60 MQKRLTLLGS TGSIGDSTLD VVTRHPERFA VHALTAHRNG DKLVAQCLRF APDVAVVGDA 70 80 90 100 110 120 ETAARVEAQL RAAGSKTQVA YGKQALVDVS KSDGCDTVVA AIVGAAGLAP SLAAARAGKR 130 140 150 160 170 180 ILLANKEALV MSGAIFMDAV RDHGAILLPV DSEHNAIFQC MPRDAAEHGG IAKIIVTASG 190 200 210 220 230 240 GPFRTREPVT LASVTPDEAC KHPNWVMGRK ISVDSATMMN KGLEVIEAHW LFGLPSERID 250 260 270 280 290 300 VLIHPQSVIH SLVSYCDGSV LAQLGNPDMR TPIAHALAFP ERVDAGVAQL DLAQIATLTF 310 320 330 340 350 360 EKPDYARFPC LALAIDALEA GGVASAALNA ANEIAVDAFL SRRIRFTAIA QTVDAVLSGL 370 380 390 SNRTPSGLDD VIGADADARR AATAFIDKLP APSVERAA

References

[1]

Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R., Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D., Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F., Roberts K., Hatch B., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000086 Genomic DNA. Translation: ABC36321.1.
RefSeq	YP_442557.1.
3D structure databases
SMR	Q2SWZ2. Positions 2-392.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2SWZ2.
Genome annotation databases
GeneID	3846968.
GenomeReviews	Gene locus BTH_I2033 in contig CP000086_GR.
KEGG	bte:BTH_I2033.
TIGR	BTH_I2033.
Phylogenomic databases
eggNOG	COG0743.
HOGENOM	HBG430762.
OMA	IHSMVEY.
Enzyme and pathway databases
BioCyc	BTHA271848:BTH_I2033-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]
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_BURTA

Accession

Primary (citable) accession number: Q2SWZ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 24, 2006
Last modified:	February 9, 2010
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)