Reviewed, UniProtKB/Swiss-Prot Q1LSV3 (DXR_BAUCH)

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:	BCI_0531

Organism

Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]

Taxonomic identifier

374463 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length	398 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-PP biosynthesis via DXP pathway; isopentenyl-PP 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 – 398	398	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_1000020218
Regions
	Nucleotide binding	7 – 36	30	NADP By similarity
Sites
	Metal binding	150	1	Divalent metal cation By similarity
	Metal binding	152	1	Divalent metal cation By similarity
	Metal binding	231	1	Divalent metal cation By similarity
	Binding site	125	1	Substrate By similarity
	Binding site	152	1	Substrate By similarity
	Binding site	186	1	Substrate By similarity
	Binding site	209	1	Substrate By similarity
	Binding site	231	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1LSV3-1 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: EA2B63D193C903CC	FASTA	398	43,611
	10 20 30 40 50 60 MKYLTILGST GSIGTSTLTV IKQNPDKFTV RALVAKNNFT LMTKQCLDFR PSWVGMVDKR 70 80 90 100 110 120 AARELKANLA QLGIAINIIS GNQAACELAA LKEIDTVMAA IAGVDGLLST LSALRAGKRV 130 140 150 160 170 180 LLANKESLVS CGRLFMNEVH QHNAQLLPVD SEHNAIFQIL PEPIQRQLGC LSLSKYGVSQ 190 200 210 220 230 240 IILTGSGGPF RQTPLDALAT ITSDQACIHP NWSMGRKISV DSATMMNKGL EYIEARCLFN 250 260 270 280 290 300 ASTDQIEVLL HPQSIFHSMV RYVDGSVLAQ LAYPDMRIPI TYALSYPTRV PIKVTPLNFL 310 320 330 340 350 360 QLGTLSFDQP DNKRYPCLQL AIEASKLGQA ATTTLNAANE VAVAAFLQRK IRFTDIASVN 370 380 390 QMVLDKINLE EPSSIEEVLC IDRQARINAH LSIRYLAL

References

[1]

"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters." Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A. PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000238 Genomic DNA. Translation: ABF14058.1.
RefSeq	YP_588961.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4056432.
GenomeReviews	Gene locus BCI_0531 in contig CP000238_GR.
KEGG	bci:BCI_0531.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1LSV3.
OMA	Q1LSV3. IHSMVEY.
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_BAUCH

Accession

Primary (citable) accession number: Q1LSV3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 30, 2006
Last modified:	June 16, 2009
This is version 23 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)