Q7VYC4 (DXR_BORPE) 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:	BP1425

Organism

Bordetella pertussis

Taxonomic identifier

520 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	399 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 – 399	399	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_0000163620
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)
	Q7VYC4 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 8319C8E5B9748768	FASTA	399	42,097
	10 20 30 40 50 60 MTRFQRVAVL GSTGSIGDST LDVIARHPDR LGVYALSAYS RMDKLAAQAA ACGAAVVVVP 70 80 90 100 110 120 DDAAAARFRA AWRGKAAMPE VRVGPRALAE TAAAPECTTV MAAIVGAAGL PAALAAAQAG 130 140 150 160 170 180 KRVLLANKEA LVAAGSLFMA AVRENGAELL PIDSEHNAIF QCMPQGARAA APTAPAPGVR 190 200 210 220 230 240 RLLLTASGGP FRRQDPADLH EVTPAQACAH PNWSMGRKIS VDSATMLNKG LEVIEAHWLF 250 260 270 280 290 300 AMPSERIDVL IHPQSVVHSM VEYDDGSVLA QLGQPDMRTP IAYGLGFPER LASGVGLLDL 310 320 330 340 350 360 TRWGRLDFEQ PDLQRFPCLA LSFAALRAGQ PACVALNAAN EVAVAAFLEG RLRYTWIARV 370 380 390 IEAVLEWQAK QASVTLTSLD DVLDLDARAR SFAGNLGLA

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tohama I / ATCC BAA-589 / NCTC 13251.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640415 Genomic DNA. Translation: CAE41715.1.
RefSeq	NP_880167.1. NC_002929.2.
3D structure databases
ProteinModelPortal	Q7VYC4.
SMR	Q7VYC4. Positions 5-396.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2665122.
GenomeReviews	Gene locus BP1425 in contig BX470248_GR.
KEGG	bpe:BP1425.
PATRIC	21156064. VBIBorPer7866_1528.
Phylogenomic databases
HOGENOM	HBG430762.
OMA	IHSMVEY.
PhylomeDB	Q7VYC4.
ProtClustDB	PRK05447.
Enzyme and pathway databases
BioCyc	BPER257313:BP1425-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_BORPE

Accession

Primary (citable) accession number: Q7VYC4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program