Q5L9P6 (DXR_BACFN) 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:	BF3492

Organism

Bacteroides fragilis (strain ATCC 25285 / NCTC 9343) [Complete proteome] [HAMAP]

Taxonomic identifier

272559 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length	388 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 – 388	388	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_0000163614
Regions
	Nucleotide binding	12 – 41	30	NADP By similarity
Sites
	Metal binding	153	1	Divalent metal cation By similarity
	Metal binding	155	1	Divalent metal cation By similarity
	Metal binding	224	1	Divalent metal cation By similarity
	Binding site	128	1	Substrate By similarity
	Binding site	155	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)
	Q5L9P6 [UniParc]. Last modified June 21, 2005. Version 1. Checksum: AD3B728F760ED81D	FASTA	388	42,696
	10 20 30 40 50 60 MNEIKKKQIA ILGSTGSIGT QALQVIEEHP ELYEVYALTA NNKVDLLIAQ ARKFMPEAVV 70 80 90 100 110 120 IANEEKYAQL KEALSDLPVK VYAGAAALCQ IVESGPIDVV LTAMVGYAGL KPTMNAIRAG 130 140 150 160 170 180 KAIALANKET LVVAGELINQ LARQYRTPIL PVDSEHSAVF QCLAGEVGNP IEKVILTASG 190 200 210 220 230 240 GPFRTCTMEQ LKTVTKVQAL KHPNWEMGAK ITIDSASMMN KGFEVIEAKW LFGVQPSQIE 250 260 270 280 290 300 VVVHPQSVIH SMVQFEDGAI KAQLGMPDMR LPIQYAFSYP DRINSSFDRL DFSKCTNLTF 310 320 330 340 350 360 EQPDTKRFRN LALAYESMYR GGNMPCIVNA ANEVVVAAFL RDEISFLGMS DVIEHTMGQV 370 380 SFVQTPTYDD YVATDAEARR IARELICK

References

[1]

"Extensive DNA inversions in the B. fragilis genome control variable gene expression." Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V., Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A., Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A. , Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J., Barrell B.G., Parkhill J. Science 307:1463-1465(2005) [PubMed: 15746427] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25285 / NCTC 9343.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR626927 Genomic DNA. Translation: CAH09181.1.
RefSeq	YP_213095.1. NC_003228.3.
3D structure databases
ProteinModelPortal	Q5L9P6.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5L9P6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3286332.
GenomeReviews	Gene locus BF3492 in contig CR626927_GR.
KEGG	bfs:BF3492.
PATRIC	21043698. VBIBacFra29119_3560.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0743.
HOGENOM	HBG430762.
OMA	IHSMVEY.
ProtClustDB	PRK05447.
Enzyme and pathway databases
BioCyc	BFRA272559:BF3492-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_BACFN

Accession

Primary (citable) accession number: Q5L9P6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	June 21, 2005
Last modified:	January 25, 2012
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program