Q0S275 (DXR_RHOSR) 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:	RHA1_ro06588

Organism

Rhodococcus sp. (strain RHA1) [Complete proteome] [HAMAP]

Taxonomic identifier

101510 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length	398 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 – 398	398	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_1000020303
Regions
	Nucleotide binding	25 – 54	30	NADP By similarity
Sites
	Metal binding	159	1	Divalent metal cation By similarity
	Metal binding	161	1	Divalent metal cation By similarity
	Metal binding	230	1	Divalent metal cation By similarity
	Binding site	136	1	Substrate By similarity
	Binding site	161	1	Substrate By similarity
	Binding site	185	1	Substrate By similarity
	Binding site	208	1	Substrate By similarity
	Binding site	230	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0S275 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 687C0DA5198E9EB2	FASTA	398	41,238
	10 20 30 40 50 60 MAGGPHFIRK NGWVDENRPT RVLLLGSTGS IGTQALEVVA ANPDKFTVVG LAAGGANVEL 70 80 90 100 110 120 LDRQIRETGV SSVAVADPSA AASLARPGVL SGPDAVTELV RTTEADVVLN ALVGSLGLEP 130 140 150 160 170 180 TLAALESGAR LALANKESLV AGGPLVTAAA APGQIVPVDS EHSALAQCLR GGSADEVDRL 190 200 210 220 230 240 VLTASGGPFR GWTADRLESV TPEQAGAHPT WSMGPMNTLN SATLVNKGLE LIETHLLFGV 250 260 270 280 290 300 DYDRIDVTVH PQSIVHSMVT FTDGSTLAQA SPPDMKLPIA LALGWPHRIA GAAAACDFST 310 320 330 340 350 360 ASTWDFEPLD SQVFPAVDLA REAGKGGGCL TAVYNAANEV AAQAFLDGII RFPRIVRTVA 370 380 390 SVLSEADEWS APPATVEDVL AADGWARERA RQLVKQEG

References

[1]

"The complete genome of Rhodococcus sp. RHA1 provides insights into a catabolic powerhouse." McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H. , Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W., Eltis L.D. Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006) [PubMed: 17030794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RHA1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000431 Genomic DNA. Translation: ABG98361.1.
RefSeq	YP_706519.1. NC_008268.1.
3D structure databases
ProteinModelPortal	Q0S275.
SMR	Q0S275. Positions 21-394.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0S275.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4224139.
GenomeReviews	Gene locus RHA1_ro06588 in contig CP000431_GR.
KEGG	rha:RHA1_ro06588.
PATRIC	23212143. VBIRhoJos26306_6643.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0743.
HOGENOM	HBG430762.
OMA	IHSMVEY.
PhylomeDB	Q0S275.
ProtClustDB	PRK05447.
Enzyme and pathway databases
BioCyc	RSP101510:RHA1_RO06588-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_RHOSR

Accession

Primary (citable) accession number: Q0S275

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program