Reviewed, UniProtKB/Swiss-Prot Q636K5 (DXR2_BACCZ)

Names and origin

Protein names

Recommended name:
    1-deoxy-D-xylulose 5-phosphate reductoisomerase 2
      Short name=DXP reductoisomerase 2
    EC=1.1.1.267
Alternative name(s):
    1-deoxyxylulose-5-phosphate reductoisomerase 2
    2-C-methyl-D-erythritol 4-phosphate synthase 2

Gene names

Name:	dxr2
Ordered Locus Names:	BCE33L3580

Organism

Bacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]

Taxonomic identifier

288681 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	380 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 – 380	380	1-deoxy-D-xylulose 5-phosphate reductoisomerase 2 HAMAP MF_00183		PRO_0000163606
Regions
	Nucleotide binding	7 – 36	30	NADP By similarity
Sites
	Metal binding	146	1	Divalent metal cation By similarity
	Metal binding	148	1	Divalent metal cation By similarity
	Metal binding	217	1	Divalent metal cation By similarity
	Binding site	121	1	Substrate By similarity
	Binding site	148	1	Substrate By similarity
	Binding site	172	1	Substrate By similarity
	Binding site	195	1	Substrate By similarity
	Binding site	217	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q636K5-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 689DDF159E83D1B4	FASTA	380	42,239
	10 20 30 40 50 60 MKNISLLGAS GSIGTQTLDV LRSHPDQFRL VAFSVGKNID YAVKVIQEFS PQIVSVQREE 70 80 90 100 110 120 DVLKLQAVSG NTKIVYGSEG LLEVALHPDA EIVVNAVVGS VGLLPTLRAI EAKKTIGIAN 130 140 150 160 170 180 KETLVTAGHL VMEAARKHNV SLLPVDSEHS AIFQCLNGEN EKRISRLIIT ASGGSFRDKT 190 200 210 220 230 240 RDELHHVTVE DALRHPNWSM GSKITIDSAT MMNKGLEVIE AHWLFGIPYE QIDVVLHKES 250 260 270 280 290 300 IIHSMVEFED RSVMAQLGSP DMRVPIQYAL TYPDRLPLSD TKQLNLWEIG TLHFEKMNQE 310 320 330 340 350 360 RFRCLRFAYE AGKAGGSMPA VMNAANEVAV EAFLQKRIGF LTVEDLIEKA MNHHNVIARP 370 380 SLEEILEIDA ATRRFVMEQI

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000001 Genomic DNA. Translation: AAU16686.1.
RefSeq	YP_085162.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q636K5.
Genome annotation databases
GeneID	3025360.
GenomeReviews	Gene locus BCE33L3580 in contig CP000001_GR.
KEGG	bcz:BCZK3580.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q636K5.
OMA	IHSMVEY.
Enzyme and pathway databases
BioCyc	BCER288681:BCE33L3580-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

DXR2_BACCZ

Accession

Primary (citable) accession number: Q636K5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	October 25, 2004
Last modified:	November 3, 2009
This is version 35 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)