Reviewed, UniProtKB/Swiss-Prot Q65JJ3 (DXR_BACLD)

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:	BLi01876, BL01237

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	383 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW terpenoid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	1-deoxy-D-xylulose-5-phosphate reductoisomerase activity Inferred from electronic annotation. Source: HAMAP 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 – 383	383	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_0000163609
Regions
	Nucleotide binding	7 – 36	30	NADP By similarity
Sites
	Metal binding	148	1	Divalent metal cation By similarity
	Metal binding	150	1	Divalent metal cation By similarity
	Metal binding	219	1	Divalent metal cation By similarity
	Binding site	123	1	Substrate By similarity
	Binding site	150	1	Substrate By similarity
	Binding site	174	1	Substrate By similarity
	Binding site	197	1	Substrate By similarity
	Binding site	219	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q65JJ3-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 57ACB84D853DC025	FASTA	383	42,594
	10 20 30 40 50 60 MKNICLLGAT GSIGEQTLDV IKAHDDKFRL TAMTFGKNAE KAAEIIETFK PKYVGVGDEH 70 80 90 100 110 120 TYETLKQHSF SYTFKTGIGE EALIEAAVIP EADIVVNALV GSVGLLPTLK AMEHKKTIAL 130 140 150 160 170 180 ANKETLVTAG HIVKEHAQKY DVPLLPVDSE HSAIFQALQG ENPKHIKRLI VTASGGSFRD 190 200 210 220 230 240 RTRRELEGVT VEEALNHPNW SMGAKITIDS ATMMNKGLEV IEAHWLFDLP YDQIDVLLHK 250 260 270 280 290 300 ESIIHSMVEF HDRSVIAQLG TPDMRVPIQY ALSHPERLPF NEAKSLDLWE VGQLNFAQAD 310 320 330 340 350 360 FERFRCLQFA YESGKIGGTM PTVLNAANEE AVAAFLSGRI SFLGIEDIIE KALERHQVIA 370 380 KPSLQEIREV DKDARKFVQT LLT

References

[1]

"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

[2]

"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. , Galleron N., Ehrlich S.D., Berka R.M. Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017333 Genomic DNA. Translation: AAU40771.1. CP000002 Genomic DNA. Translation: AAU23411.1.
RefSeq	YP_079049.1. YP_091464.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q65JJ3.
Genome annotation databases
GeneID	3031070. 3101494.
GenomeReviews	Gene locus BLi01876 in contig AE017333_GR. Gene locus BL01237 in contig CP000002_GR.
KEGG	bld:BLi01876. bli:BL01237.
NMPDR	fig|279010.5.peg.2580.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q65JJ3.
OMA	IHSMVEY.
Enzyme and pathway databases
BioCyc	BLIC279010:BL01237-MON.
Family and domain databases
HAMAP	MF_00183. [Tree]
InterPro	IPR003821. DXP_reductoisomerase. IPR013644. DXP_reductoisomerase_C. IPR013512. DXP_reductoisomerase_N. [Graphical view]
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_BACLD

Accession

Primary (citable) accession number: Q65JJ3
Secondary accession number(s): Q62UZ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	October 25, 2004
Last modified:	November 3, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)