Q01QM3 (DXR_SOLUE) 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:	Acid_7136

Organism

Solibacter usitatus (strain Ellin6076) [Complete proteome] [HAMAP]

Taxonomic identifier

234267 [NCBI]

Taxonomic lineage

Bacteria › Acidobacteria › Solibacteres › Solibacterales › Solibacteraceae › Candidatus Solibacter

Protein attributes

Sequence length	397 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 – 397	397	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_1000020316
Regions
	Nucleotide binding	7 – 36	30	NADP By similarity
Sites
	Metal binding	154	1	Divalent metal cation By similarity
	Metal binding	156	1	Divalent metal cation By similarity
	Metal binding	225	1	Divalent metal cation By similarity
	Binding site	129	1	Substrate By similarity
	Binding site	156	1	Substrate By similarity
	Binding site	180	1	Substrate By similarity
	Binding site	203	1	Substrate By similarity
	Binding site	225	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q01QM3 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: F39528EB8791091A	FASTA	397	42,696
	10 20 30 40 50 60 MKTIAVLGST GSIGTNTLDV VRRNRHLYEV YSLVAGQNIE LLTGQILEFR PKLAVVASAA 70 80 90 100 110 120 VLDLLTASLQ AAGLPKSEWP DLLSGDAARV AAVRAPEVDT VISAIVGVAG LEATYEAVCL 130 140 150 160 170 180 GKRVGLANKE VLVSGGSLVM EAVRKFGAEL LPVDSEHNGA HQCLRAGNRA QVSRLILTAS 190 200 210 220 230 240 GGPFRNTPVS ELPFVTPGQA LNHPTWKMGN RITIDCATLM NKGFEVIEAC WLFDFAPRDV 250 260 270 280 290 300 GVVIHPQSTV HAMIEYSDGS VLAQISATDM RMPIQYALTY PDRADAPVPK IDWAEARKWE 310 320 330 340 350 360 FLPPDLEKFP LLKLAYQCQE SGGSATCILN AADEIAVEAF LQGRIGFLSI HEIVQETLSR 370 380 390 MPSRTPASVG DILEIDRESR TLARELANCR AAGTVTA

References

[1]

"Three genomes from the phylum Acidobacteria provide insight into the lifestyles of these microorganisms in soils." Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., Davidsen T.M. , DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R. Appl. Environ. Microbiol. 75:2046-2056(2009) [PubMed: 19201974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ellin6076.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000473 Genomic DNA. Translation: ABJ88047.1.
RefSeq	YP_828332.1. NC_008536.1.
3D structure databases
ProteinModelPortal	Q01QM3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q01QM3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4424840.
GenomeReviews	Gene locus Acid_7136 in contig CP000473_GR.
KEGG	sus:Acid_7136.
NMPDR	fig|234267.9.peg.6765.
PATRIC	32016988. VBICanSol30224_7443.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0743.
HOGENOM	HBG430762.
OMA	IHSMVEY.
PhylomeDB	Q01QM3.
ProtClustDB	PRK05447.
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_SOLUE

Accession

Primary (citable) accession number: Q01QM3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 14, 2006
Last modified:	January 25, 2012
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program