Q732P8 (DXR_BACC1) 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:	BCE_3862

Organism

Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]

Taxonomic identifier

222523 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

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
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_0000163602
Regions
	Nucleotide binding	7 – 36	30	NADP By similarity
Sites
	Metal binding	146	1	Divalent metal cation By similarity
	Metal binding	148	1	Divalent metal cation By similarity
	Metal binding	217	1	Divalent metal cation By similarity
	Binding site	121	1	Substrate By similarity
	Binding site	148	1	Substrate By similarity
	Binding site	172	1	Substrate By similarity
	Binding site	195	1	Substrate By similarity
	Binding site	217	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q732P8 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 6E27027DAA9BFD80	FASTA	380	42,317
	10 20 30 40 50 60 MKNISLLGAS GSIGTQTLDV LRSHPDQFRL VAFSVGKNID YAVKVIQEFS PQIVSVQREE 70 80 90 100 110 120 DVLKLQAVSG NTKIVYGSEG LLEVALHPDA EIVVNAVVGS VGLLPTLRAI EAKKTIGIAN 130 140 150 160 170 180 KETLVTAGHL VMEAARKHNV SLLPVDSEHS AIFQCLNGEN EKRISRLIIT ASGGSFRDKT 190 200 210 220 230 240 RDELHHVTVE DALRHPNWSM GSKITIDSAT MMNKGLEVIE AHWLFGIPYE QIDVVLHKES 250 260 270 280 290 300 IIHSMVEFED RSVMAQLGSP DMRVPIQYAL TYPDRLPLSD TKQLNLWEMG TLHFEKMNQE 310 320 330 340 350 360 RFRCLRFAYE AGKTGGSMPA VMNAANEVAV EAFLQKRIGF LTVEDLIEKA MNHHNVIARP 370 380 SLEEILEIDA TTRRFVMEQI

References

[1]

"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10987.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017194 Genomic DNA. Translation: AAS42767.1.
RefSeq	NP_980159.1. NC_003909.8.
3D structure databases
ProteinModelPortal	Q732P8.
ModBase	Search...
Protein-protein interaction databases
STRING	Q732P8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000029468; EBBACP00000028818; EBBACG00000029459.
GeneID	2749994.
GenomeReviews	Gene locus BCE_3862 in contig AE017194_GR.
KEGG	bca:BCE_3862.
NMPDR	fig|222523.1.peg.3831.
PATRIC	18856380. VBIBacCer118379_3689.
TIGR	BCE_3862.
Phylogenomic databases
eggNOG	COG0743.
GeneTree	EBGT00050000001768.
HOGENOM	HBG430762.
OMA	IHSMVEY.
ProtClustDB	PRK05447.
Enzyme and pathway databases
BioCyc	BCER405917:BCE_3862-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_BACC1

Accession

Primary (citable) accession number: Q732P8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program