A0PQ95 (DXR_MYCUA) 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:	MUL_2085

Organism

Mycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]

Taxonomic identifier

362242 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	402 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 – 402	402	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_1000118494
Regions
	Nucleotide binding	18 – 47	30	NADP By similarity
Sites
	Metal binding	151	1	Divalent metal cation By similarity
	Metal binding	153	1	Divalent metal cation By similarity
	Metal binding	222	1	Divalent metal cation By similarity
	Binding site	128	1	Substrate By similarity
	Binding site	153	1	Substrate By similarity
	Binding site	177	1	Substrate By similarity
	Binding site	200	1	Substrate By similarity
	Binding site	222	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0PQ95 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: D2EBB6ACB664DDB0	FASTA	402	41,961
	10 20 30 40 50 60 MTTATDGFAD GRLRVLVLGS TGSIGTQALE VIAANPDRFE VVGLAAGGSN LDTLRRQRAE 70 80 90 100 110 120 TGVTEIAIAD ERAAQLAGDI AYQEPDAVTR LVEETEADVV LNALVGALGL RPTLAALASG 130 140 150 160 170 180 ARLALANKES LVAGGPLVLQ AAQPGQIVPV DSEHSALAQC LRAGTPDEVA KLVLTASGGP 190 200 210 220 230 240 FRGWSAADLQ EVTPEQAGAH PTWSMGPMNT LNSASLVNKG LELIETHLLF GISYERIEVV 250 260 270 280 290 300 VHPQSIVHSM VTFVDGSTIA QASPPDMKLP ISLALGWPRR VPGAARYCDF SQAQTWEFEP 310 320 330 340 350 360 LDDEVFPAVE LARHAGETGG CMTAVYNAAN EEAAAAFLAG RISFPAIVGT IADVLHAADQ 370 380 390 400 WAVSPANVDD VLDAQRWARQ RAQRAIAKAS PAGACEKVSG LA

References

[1]

"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer." Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T. Genome Res. 17:192-200(2007) [PubMed: 17210928] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Agy99.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000325 Genomic DNA. Translation: ABL04514.1.
RefSeq	YP_905985.1. NC_008611.1.
3D structure databases
ProteinModelPortal	A0PQ95.
SMR	A0PQ95. Positions 11-387.
ModBase	Search...
Protein-protein interaction databases
STRING	A0PQ95.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000074038; EBMYCP00000072043; EBMYCG00000074033.
GeneID	4551008.
GenomeReviews	Gene locus MUL_2085 in contig CP000325_GR.
KEGG	mul:MUL_2085.
PATRIC	18171244. VBIMycUlc37413_2468.
Organism-specific databases
GenoList	MUL_2085.
CMR	Search...
Phylogenomic databases
eggNOG	COG0743.
GeneTree	EBGT00050000016490.
HOGENOM	HBG430762.
OMA	IHSMVEY.
PhylomeDB	A0PQ95.
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_MYCUA

Accession

Primary (citable) accession number: A0PQ95

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	January 9, 2007
Last modified:	December 14, 2011
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