Reviewed, UniProtKB/Swiss-Prot Q9A709 (DXR_CAUCR)

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:	CC_1917

Organism

Caulobacter crescentus (Caulobacter vibrioides) [Complete proteome] [HAMAP]

Taxonomic identifier

155892 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Caulobacterales › Caulobacteraceae › Caulobacter

Protein attributes

Sequence length	399 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 – 399	399	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_0000163628
Regions
	Nucleotide binding	13 – 42	30	NADP By similarity
Sites
	Metal binding	153	1	Divalent metal cation By similarity
	Metal binding	155	1	Divalent metal cation By similarity
	Metal binding	224	1	Divalent metal cation By similarity
	Binding site	128	1	Substrate By similarity
	Binding site	155	1	Substrate By similarity
	Binding site	179	1	Substrate By similarity
	Binding site	202	1	Substrate By similarity
	Binding site	224	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9A709-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: B68D94C6D0A47C25	FASTA	399	41,457
	10 20 30 40 50 60 MGALTSPRKV VVLGSTGSIG LSTLSLFEES GAPVQILALT AGRNVERLIE QARRWKPSLA 70 80 90 100 110 120 VIEDESRLDD LRAGLAGTGV EAAAGADAVR DAAAMGADWV MSAIVGAAGL APTVAAARTG 130 140 150 160 170 180 AVIALANKES LVCAGPALLA IAKAAGGSVI PVDSEHSAIF QVLQSECAHR VSRLILTASG 190 200 210 220 230 240 GPFRTWDKAA MARATPEQAI AHPNWSMGAK ISVDSATMMN KGLEMIEASY LFATPEDRVD 250 260 270 280 290 300 VVIHPQSVIH SLVEYVDGST LAQLGPPDMR APIACAFAWP DRLPWPAPRL DLAAYGQLTF 310 320 330 340 350 360 ESPDVERFPA IGIAREALRL GGGAPAAMNA ANEVAVAAFL DRRIGFLDIA GAVAGTLERM 370 380 390 NSLGDLSVAE SDAVETAMLI DGSARRIAAE VVAQKRQRA

References

[1]

"Complete genome sequence of Caulobacter crescentus." Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E., Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R., Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B., DeBoy R.T., Dodson R.J. , Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001) [PubMed: 11259647] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 19089 / CB15.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE005673 Genomic DNA. Translation: AAK23892.1.
PIR	H87486.
RefSeq	NP_420724.1.
3D structure databases
HSSP	HSSP built from PDB template 1K5H based on UniProtKB P45568.
ModBase	Search...
Genome annotation databases
GeneID	942615.
GenomeReviews	Gene locus CC_1917 in contig AE005673_GR.
KEGG	ccr:CC_1917.
NMPDR	fig|190650.1.peg.1904.
TIGR	CC_1917.
Phylogenomic databases
HOGENOM	Q9A709.
OMA	IHSMVEY.
Enzyme and pathway databases
BRENDA	1.1.1.267. 2191.
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_CAUCR

Accession

Primary (citable) accession number: Q9A709

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 27, 2002
Last sequence update:	June 1, 2001
Last modified:	November 3, 2009
This is version 50 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)