Reviewed, UniProtKB/Swiss-Prot B3DQ62 (DXR_BIFLD)

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:	BLD_0115

Organism

Bifidobacterium longum (strain DJO10A) [Complete proteome] [HAMAP]

Taxonomic identifier

205913 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium

Protein attributes

Sequence length	396 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 – 396	396	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_1000098473
Regions
	Nucleotide binding	12 – 41	30	NADP By similarity
Sites
	Metal binding	155	1	Divalent metal cation By similarity
	Metal binding	157	1	Divalent metal cation By similarity
	Metal binding	226	1	Divalent metal cation By similarity
	Binding site	131	1	Substrate By similarity
	Binding site	157	1	Substrate By similarity
	Binding site	181	1	Substrate By similarity
	Binding site	204	1	Substrate By similarity
	Binding site	226	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	B3DQ62-1 [UniParc]. Last modified July 22, 2008. Version 1. Checksum: 8D5892C074919673	FASTA	396	41,986
	10 20 30 40 50 60 MSIASNSTVI ILGSTGSIGT QGLDVISRHP ERFTVTGLAA GGAHIELLAQ QAAQFHVSEA 70 80 90 100 110 120 AVFDETKVPA LQAALAQAGA QGVRVTGGPD SVIAMAGSGA NVVLNGITGS IGLEPSIAAL 130 140 150 160 170 180 KAGSQLALAN KESVVAGGHL LFSAQVRENQ INPVDSEHSA IWQSLRSGTH AEVAKLVVTA 190 200 210 220 230 240 SGGPFRGWKR ADMENITPEQ ALHHPTWNMG PVVTINSSTL MNKGLEVIEA SRLFNVPPER 250 260 270 280 290 300 IDVTVHPQSI VHSMVEFVDG ATICQASPPD MRLPIALGLS APDRMTNVAA ACDWTQAATW 310 320 330 340 350 360 TFEPLDDEAF PAVQLARHCL AASEKHTAVL NAANEQAVHA FLEHRLPYLG IVDTVKAVLD 370 380 390 QMDAELRGNP LFTDVEEMNQ LELEARRRAD DLINKQ

References

[1]

"Comparative genomic analysis of the gut bacterium Bifidobacterium longum reveals loci susceptible to deletion during pure culture growth." Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R., Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V., Slesarev A.I., Weimer B., O'Sullivan D.J. BMC Genomics 9:247-247(2008) [PubMed: 18505588] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000605 Genomic DNA. Translation: ACD97561.1.
RefSeq	YP_001954059.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	6362709.
GenomeReviews	Gene locus BLD_0115 in contig CP000605_GR.
KEGG	blj:BLD_0115.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	GLLPTIE.
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

DXR_BIFLD

Accession

Primary (citable) accession number: B3DQ62

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	July 22, 2008
Last modified:	November 3, 2009
This is version 12 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)