Reviewed, UniProtKB/Swiss-Prot Q5HT65 (DXR_CAMJR)

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:	CJE1535

Organism

Campylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]

Taxonomic identifier

195099 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	356 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	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_0000163627
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)
	Q5HT65-1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: DCD9A1CBE305EAF8	FASTA	356	39,518
	10 20 30 40 50 60 MILFGSTGSI GVNALKLAAL KNIPISALAC GDNIALLNEQ IARFKPKFVA IKDSKNKHLV 70 80 90 100 110 120 KHDRVFIGQE GLEQILTECQ DKLLLNAIVG FAGLKSTLKA KELGKNIALA NKESLVVAGS 130 140 150 160 170 180 FLKGAKFLPV DSEHAALKFL LEGKKNIAKL YITASGGAFY KYKIKDLNQV SLKDALKHPN 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]

"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species." Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. , Badger J.H., Fraser C.M., Nelson K.E. PLoS Biol. 3:72-85(2005) [PubMed: 15660156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000025 Genomic DNA. Translation: AAW35972.1.
RefSeq	YP_179520.1.
3D structure databases
SMR	Q5HT65. Positions 2-356.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5HT65.
Genome annotation databases
GeneID	3232163.
GenomeReviews	Gene locus CJE1535 in contig CP000025_GR.
KEGG	cjr:CJE1535.
NMPDR	fig|195099.3.peg.1572.
TIGR	CJE1535.
Phylogenomic databases
eggNOG	COG0743.
HOGENOM	HBG430762.
OMA	IHSMVEY.
Enzyme and pathway databases
BioCyc	CJEJ195099:CJE_1535-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]
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_CAMJR

Accession

Primary (citable) accession number: Q5HT65

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	February 15, 2005
Last modified:	February 9, 2010
This is version 36 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)