A4QF22 (DXR_CORGB) Reviewed, UniProtKB/Swiss-Prot

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:	cgR_1844

Organism

Corynebacterium glutamicum (strain R) [Complete proteome] [HAMAP]

Taxonomic identifier

340322 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	392 AA.
Sequence status	Complete.
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. HAMAP MF_00183
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. HAMAP MF_00183
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	isoprenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	1-deoxy-D-xylulose-5-phosphate reductoisomerase activity Inferred from electronic annotation. Source: EC NADPH binding Inferred from electronic annotation. Source: InterPro 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 – 392	392	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_1000020254
Regions
	Nucleotide binding	11 – 40	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	221	1	Divalent metal cation By similarity
	Binding site	127	1	Substrate By similarity
	Binding site	152	1	Substrate By similarity
	Binding site	176	1	Substrate By similarity
	Binding site	199	1	Substrate By similarity
	Binding site	221	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4QF22 [UniParc]. Last modified May 15, 2007. Version 1. Checksum: FFCAA3800DC9A35E	FASTA	392	40,974
	10 20 30 40 50 60 MGVVTKKILI LGSTGSIGTQ ALDVIADNSD KFEVVGIAAG GSQPDLVISQ AQQLGLAADK 70 80 90 100 110 120 VAVADAQAAA VVSKALGGEI ISGTDAAKIL VETTKADTVL NALVGSLGLA ATLATLESGA 130 140 150 160 170 180 HLALANKESL VAGGEFVTSK AKLGQIIPVD SEHSAMAQCL RSGTRDEVAR IVLTASGGPF 190 200 210 220 230 240 RGWTREKMWE VTPEQAAAHP TWAMGQMNTL NSATLINKGL ELIEATLLFE TDADLIDVTV 250 260 270 280 290 300 HPQSIIHSMI TFTDGATIAQ ASPPSMKLPI ALALDWPHRV PKAQPALDFT AAHTWTFEPV 310 320 330 340 350 360 DDAAFPAVQL ARHVAKQKGT YPAVYNAANE EAAEAFLRGR IKFPQIVDVV DEVLQGASQF 370 380 390 AGVASHVDDI LATESEARAR ANALINRLAT NL

References

[1]

"Comparative analysis of the Corynebacterium glutamicum group and complete genome sequence of strain R." Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M., Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M. Microbiology 153:1042-1058(2007) [PubMed: 17379713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: R.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP009044 Genomic DNA. Translation: BAF54838.1.
RefSeq	YP_001138740.1. NC_009342.1.
3D structure databases
ProteinModelPortal	A4QF22.
SMR	A4QF22. Positions 7-386.
ModBase	Search...
Protein-protein interaction databases
STRING	A4QF22.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4992791.
GenomeReviews	Gene locus cgR_1844 in contig AP009044_GR.
KEGG	cgt:cgR_1844.
PATRIC	21508302. VBICorGlu58097_1898.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0743.
HOGENOM	HBG430762.
OMA	IHSMVEY.
ProtClustDB	PRK05447.
Family and domain databases
HAMAP	MF_00183. DXP_reductoisom. [Tree]
InterPro	IPR003821. DXP_reductoisomerase. IPR013644. DXP_reductoisomerase_C. IPR013512. DXP_reductoisomerase_N. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00099.
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_CORGB

Accession

Primary (citable) accession number: A4QF22

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 15, 2007
Last modified:	December 14, 2011
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program