Reviewed, UniProtKB/Swiss-Prot Q2L155 (DXR_BORA1)

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:	BAV1740

Organism

Bordetella avium (strain 197N) [Complete proteome] [HAMAP]

Taxonomic identifier

360910 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	399 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 – 399	399	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_1000020220
Regions
	Nucleotide binding	10 – 39	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	232	1	Divalent metal cation By similarity
	Binding site	128	1	Substrate By similarity
	Binding site	155	1	Substrate By similarity
	Binding site	187	1	Substrate By similarity
	Binding site	210	1	Substrate By similarity
	Binding site	232	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2L155-1 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: C5D2CFE3003299BE	FASTA	399	42,312
	10 20 30 40 50 60 MSGFQRIAVL GSTGSIGDST LDVIARYPER FGVYALSAFS RMDKLAAQAL ATGAAVVVVP 70 80 90 100 110 120 DNNAATRFRQ AWSPSRALPE IRVGAQALAD TAADAGCDTV MAAIVGIAGL PAALAAAQSG 130 140 150 160 170 180 KRVLLANKEA LVAAGSIFMS AVRQSGAELL PIDSEHNAIF QCLPQGERAG APSTPAKTVR 190 200 210 220 230 240 KLILTASGGP FRRHSPEDLQ DVTPDQACAH PNWSMGRKIS VDSATMLNKG LEVIEAHWLF 250 260 270 280 290 300 AMPADRIEVL IHPQSVVHSL VEYDDGSVLA QMGQPDMRTP ISYGLGFPER LDAGVSPLDL 310 320 330 340 350 360 AKWGRLDFET PDLERFPCLR LSYEALRAGQ AACVALNAAN EIAVAAFLEG RLPYPWIARV 370 380 390 IDAALEWQAG RPSVTLDHLT DVLALDAQVR AYAGNLGLA

References

[1]

"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction." Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M. J. Bacteriol. 188:6002-6015(2006) [PubMed: 16885469] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM167904 Genomic DNA. Translation: CAJ49348.1.
RefSeq	YP_786258.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	6266768.
GenomeReviews	Gene locus BAV1740 in contig AM167904_GR.
KEGG	bav:BAV1740.
NMPDR	fig|521.1.peg.1680.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2L155.
OMA	IHSMVEY.
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_BORA1

Accession

Primary (citable) accession number: Q2L155

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	March 7, 2006
Last modified:	November 3, 2009
This is version 26 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)