Q8G7Y7 (DXR_BIFLO) 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:	BL0097

Organism

Bifidobacterium longum (strain NCC 2705)

Taxonomic identifier

206672 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium

Protein attributes

Sequence length	396 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 Reference 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 – 396	396	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_0000163616
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)
	Q8G7Y7 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 3211E2783BB0C95A	FASTA	396	42,014
	10 20 30 40 50 60 MSIASNSTVI ILGSTGSIGT QGLDVISRHP ERFTVTGLAA GGAHIELLAQ QAAQFHVSEV 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]

"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract." Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F. Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed: 12381787] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCC 2705.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014295 Genomic DNA. Translation: AAN23962.1.
RefSeq	NP_695326.1. NC_004307.2.
3D structure databases
ProteinModelPortal	Q8G7Y7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1022356.
GenomeReviews	Gene locus BL0097 in contig AE014295_GR.
KEGG	blo:BL0097.
NMPDR	fig|206672.1.peg.95.
PATRIC	21117237. VBIBifLon107831_0104.
Phylogenomic databases
HOGENOM	HBG430762.
OMA	IAKLYIT.
PhylomeDB	Q8G7Y7.
ProtClustDB	PRK05447.
Enzyme and pathway databases
BioCyc	BLON206672:BL0097-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_BIFLO

Accession

Primary (citable) accession number: Q8G7Y7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2003
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program