Reviewed, UniProtKB/Swiss-Prot Q9PMV3 (DXR_CAMJE)

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:	Cj1346c

Organism

Campylobacter jejuni [Complete proteome] [HAMAP]

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	356 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-PP biosynthesis via DXP pathway; isopentenyl-PP 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 – 356	356	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_0000163626
Regions
	Nucleotide binding	4 – 30	27	NADP By similarity
Sites
	Metal binding	131	1	Divalent metal cation By similarity
	Metal binding	133	1	Divalent metal cation By similarity
	Metal binding	200	1	Divalent metal cation By similarity
	Binding site	112	1	Substrate By similarity
	Binding site	133	1	Substrate By similarity
	Binding site	155	1	Substrate By similarity
	Binding site	178	1	Substrate By similarity
	Binding site	200	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9PMV3-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: C6E4DCF376C06D45	FASTA	356	39,548
	10 20 30 40 50 60 MILFGSTGSI GVNALKLAAL KNIPISALAC GDNIALLNEQ IARFKPKFVS IKDSKNKHLV 70 80 90 100 110 120 KHDRVFIGQE GLEQILTECQ DKLLLNAIVG FAGLKSTLKA KELGKNIALA NKESLVVAGS 130 140 150 160 170 180 FLKGAKFLPV DSEHAALKFL LEGKKNIAKL YITASGGAFY RYKIKDLNQV SVKDALKHPN 190 200 210 220 230 240 WNMGAKITID SATMANKLFE IIEAYHLYDF KEIDALIEPR SLVHAMCEFK NGASTAYFSK 250 260 270 280 290 300 ADMKLAISDA IFEKQDTPIL EAVDFSKMPA LKFHPISTKK YPIFKLKNTF LKEPNLGVII 310 320 330 340 350 NAANEVGVYN FLENKSGFLD IAKCIFKALD HFGVPKISSI EEVFEYDFKT REYLRS

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL111168 Genomic DNA. Translation: CAL35458.1.
PIR	G81278.
RefSeq	YP_002344734.1.
3D structure databases
HSSP	HSSP built from PDB template 1K5H based on UniProtKB P45568.
ModBase	Search...
Genome annotation databases
GeneID	905638.
GenomeReviews	Gene locus Cj1346c in contig AL111168_GR.
KEGG	cje:Cj1346c.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	Q9PMV3. IHSMVEY.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ1346C-MON.
BRENDA	1.1.1.267. 255835.
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_CAMJE

Accession

Primary (citable) accession number: Q9PMV3
Secondary accession number(s): Q0P8R3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 46 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)