A1KML5 (DXR_MYCBP) 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:	BCG_2892c

Organism

Mycobacterium bovis (strain BCG / Pasteur 1173P2) [Complete proteome] [HAMAP]

Taxonomic identifier

410289 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	413 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 – 413	413	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_1000020278
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)
	A1KML5 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 44E19577CE4D814F	FASTA	413	42,853
	10 20 30 40 50 60 MTNSTDGRAD GRLRVVVLGS TGSIGTQALQ VIADNPDRFE VVGLAAGGAH LDTLLRQRAQ 70 80 90 100 110 120 TGVTNIAVAD EHAAQRVGDI PYHGSDAATR LVEQTEADVV LNALVGALGL RPTLAALKTG 130 140 150 160 170 180 ARLALANKES LVAGGSLVLR AARPGQIVPV DSEHSALAQC LRGGTPDEVA KLVLTASGGP 190 200 210 220 230 240 FRGWSAADLE HVTPEQAGAH PTWSMGPMNT LNSASLVNKG LEVIETHLLF GIPYDRIDVV 250 260 270 280 290 300 VHPQSIIHSM VTFIDGSTIA QASPPDMKLP ISLALGWPRR VSGAAAACDF HTASSWEFEP 310 320 330 340 350 360 LDTDVFPAVE LARQAGVAGG CMTAVYNAAN EEAAAAFLAG RIGFPAIVGI IADVLHAADQ 370 380 390 400 410 WAVEPATVDD VLDAQRWARE RAQRAVSGMA SVAIASTAKP GAAGRHASTL ERS

References

[1]

"Genome plasticity of BCG and impact on vaccine efficacy." Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T. Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007) [PubMed: 17372194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BCG / Pasteur 1173P2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM408590 Genomic DNA. Translation: CAL72881.1.
RefSeq	YP_978976.1. NC_008769.1.
3D structure databases
ProteinModelPortal	A1KML5.
SMR	A1KML5. Positions 11-389.
ModBase	Search...
Protein-protein interaction databases
STRING	A1KML5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000018991; EBMYCP00000018741; EBMYCG00000018986.
GeneID	4698567.
GenomeReviews	Gene locus BCG_2892c in contig AM408590_GR.
KEGG	mbb:BCG_2892c.
PATRIC	18016810. VBIMycBov80988_3151.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0743.
GeneTree	EBGT00050000016490.
HOGENOM	HBG430762.
OMA	IHSMVEY.
ProtClustDB	PRK05447.
Enzyme and pathway databases
BioCyc	MBOV410289:BCG_2892C-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_MYCBP

Accession

Primary (citable) accession number: A1KML5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 6, 2007
Last modified:	December 14, 2011
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