Reviewed, UniProtKB/Swiss-Prot Q89KP9 (DXR_BRAJA)

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:	bll4855

Organism

Bradyrhizobium japonicum [Complete proteome] [HAMAP]

Taxonomic identifier

375 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium

Protein attributes

Sequence length	407 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 – 407	407	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_0000163621
Regions
	Nucleotide binding	22 – 51	30	NADP By similarity
Sites
	Metal binding	162	1	Divalent metal cation By similarity
	Metal binding	164	1	Divalent metal cation By similarity
	Metal binding	233	1	Divalent metal cation By similarity
	Binding site	137	1	Substrate By similarity
	Binding site	164	1	Substrate By similarity
	Binding site	188	1	Substrate By similarity
	Binding site	211	1	Substrate By similarity
	Binding site	233	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q89KP9-1 [UniParc]. Last modified June 20, 2003. Version 1. Checksum: F1202A78BB89D0C6	FASTA	407	42,699
	10 20 30 40 50 60 MSAVPLRNNK AAASAVRSVT VLGATGSIGD STMDLLRASP ERYRVEALTA NGNVEALAKL 70 80 90 100 110 120 AKEFSARFVA IADTSKFAEL KAALAGTSTE CGAGESAVIE AGARPADWVM AAVSGAAGLK 130 140 150 160 170 180 PALAAVDRGA HVALANKECL VCAGDFFMQR AAKAGACILP ADSEHNALFQ ALGSGNRDEL 190 200 210 220 230 240 VRVIITASGG PFRTWKPADI EQATLAQALK HPNWSMGQKI TIDSASMMNK GLEVIEASYL 250 260 270 280 290 300 FALSPDEIDV LVHPQSIIHG MVEFSDRSVV AQLGSPDMRT PIAHCLGWPD RIKGPAAKLD 310 320 330 340 350 360 LAKIGQLTFE APDFERFPGL RLAYDSLRTG KGATTVYNAA NEVAVAAFIA GKIRFGAIAR 370 380 390 400 LVEATLEDWI RGGNQTPLTS ADDAISVDHV ARNRAAALLP QIALKAS

References

[1]

"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110." Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S. DNA Res. 9:189-197(2002) [PubMed: 12597275] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: USDA 110.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000040 Genomic DNA. Translation: BAC50120.1.
RefSeq	NP_771495.1.
3D structure databases
HSSP	HSSP built from PDB template 1K5H based on UniProtKB P45568.
ModBase	Search...
Genome annotation databases
GeneID	1052114.
GenomeReviews	Gene locus bll4855 in contig BA000040_GR.
KEGG	bja:bll4855.
NMPDR	fig|224911.1.peg.4855.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q89KP9.
OMA	IHSMVEY.
Enzyme and pathway databases
BioCyc	BJAP224911:BLL4855-MON.
BRENDA	1.1.1.267. 280.
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_BRAJA

Accession

Primary (citable) accession number: Q89KP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2003
Last sequence update:	June 20, 2003
Last modified:	November 3, 2009
This is version 37 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)