Reviewed, UniProtKB/Swiss-Prot Q9KA69 (DXR_BACHD)

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:	BH2421

Organism

Bacillus halodurans [Complete proteome] [HAMAP]

Taxonomic identifier

86665 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	382 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 – 382	382	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_0000163608
Regions
	Nucleotide binding	7 – 36	30	NADP By similarity
Sites
	Metal binding	147	1	Divalent metal cation By similarity
	Metal binding	149	1	Divalent metal cation By similarity
	Metal binding	218	1	Divalent metal cation By similarity
	Binding site	122	1	Substrate By similarity
	Binding site	149	1	Substrate By similarity
	Binding site	173	1	Substrate By similarity
	Binding site	196	1	Substrate By similarity
	Binding site	218	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9KA69-1 [UniParc]. Last modified February 21, 2001. Version 2. Checksum: 65EEAC0B018757BB	FASTA	382	42,208
	10 20 30 40 50 60 MKGISVLGAT GSIGTQTLDV LANHRDKFRL VAMSVGKNLT LAEEQIHQFK PPLVSVMTDE 70 80 90 100 110 120 DRKTLASKVP EGTRVVCGEE GLIEVATAEK AEILVNAVIG SVGLAPTLAA IEAKKTIALA 130 140 150 160 170 180 NKETLVTAGH LVTEKAREHG VKLLPVDSEH SAIFQALQGE RMDRLHRIII TASGGSFRDK 190 200 210 220 230 240 SRDELNGVTV EDALKHPNWS MGAKITIDSA TMMNKGLEVI EAHWLFNLPY EKIDVLLHKE 250 260 270 280 290 300 SIIHSMVEFV DRSVIAQLGT PDMRVPIQYA LSYPDRLEFH EGQQLNLWEV GKLHFAPLDM 310 320 330 340 350 360 ERFRCMAFAY ESGKQGGTMP TVLNAANEEA VELFLNNQLS FLGIEDVIEK ALERHERIDS 370 380 PSLADILHVD QETRAFVHSL IK

References

[1]

"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis." Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K. Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000004 Genomic DNA. Translation: BAB06140.1. Different initiation.
PIR	E83952.
RefSeq	NP_243287.2.
3D structure databases
HSSP	HSSP built from PDB template 1K5H based on UniProtKB P45568.
ModBase	Search...
Genome annotation databases
GeneID	890927.
GenomeReviews	Gene locus BH2421 in contig BA000004_GR.
KEGG	bha:BH2421.
NMPDR	fig|272558.1.peg.2421.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9KA69.
Enzyme and pathway databases
BioCyc	BHAL272558:BH2421-MON.
BRENDA	1.1.1.267. 191865.
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_BACHD

Accession

Primary (citable) accession number: Q9KA69

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	February 21, 2001
Last modified:	September 22, 2009
This is version 48 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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