Reviewed, UniProtKB/Swiss-Prot Q819Y3 (DXR2_BACCR)

Names and origin

Protein names

Recommended name:
    1-deoxy-D-xylulose 5-phosphate reductoisomerase 2
      Short name=DXP reductoisomerase 2
    EC=1.1.1.267
Alternative name(s):
    1-deoxyxylulose-5-phosphate reductoisomerase 2
    2-C-methyl-D-erythritol 4-phosphate synthase 2

Gene names

Name:	dxr2
Ordered Locus Names:	BC_3819

Organism

Bacillus cereus (strain ATCC 14579 / DSM 31) [Complete proteome] [HAMAP]

Taxonomic identifier

226900 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	380 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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 – 380	380	1-deoxy-D-xylulose 5-phosphate reductoisomerase 2 HAMAP MF_00183		PRO_0000163604
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)
	Q819Y3-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 3C2DB6AF973A01D9	FASTA	380	42,256
	10 20 30 40 50 60 MKNISLLGAS GSIGTQTLDV LRSHPDQFRL VAFSVGKNID YAVKVIQEFS PQIVSVQREE 70 80 90 100 110 120 DVLKLQSVSG 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 TKQLNLWEIG TLHFEKMDQE 310 320 330 340 350 360 RFRCLRFAYE AGKAGGSMPA VMNAANEVAV EAFLQKRIGF LTVEDLIEKA MNHHNVIARP 370 380 SLEEILEIDA ATRRFVMEQI

References

[1]

"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis." Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C. Nature 423:87-91(2003) [PubMed: 12721630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016877 Genomic DNA. Translation: AAP10741.1.
RefSeq	NP_833540.1.
3D structure databases
HSSP	HSSP built from PDB template 1K5H based on UniProtKB P45568.
ModBase	Search...
Protein-protein interaction databases
STRING	Q819Y3.
Genome annotation databases
GeneID	1206164.
GenomeReviews	Gene locus BC_3819 in contig AE016877_GR.
KEGG	bce:BC3819.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q819Y3.
OMA	IHSMVEY.
Enzyme and pathway databases
BioCyc	BCER226900:BC_3819-MON.
Family and domain databases
HAMAP	MF_00183. [Tree]
InterPro	IPR003821. DXP_reductoisomerase. IPR013644. DXP_reductoisomerase_C. IPR013512. DXP_reductoisomerase_N. [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

DXR2_BACCR

Accession

Primary (citable) accession number: Q819Y3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 42 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)