Q8NP10 (DXR_CORGL) 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:	Cgl2016, cg2208

Organism

Corynebacterium glutamicum (Brevibacterium flavum)

Taxonomic identifier

1718 [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 Reference 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_0000163642
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)
	Q8NP10 [UniParc]. Last modified October 19, 2002. Version 1. Checksum: C78632E224B1EB24	FASTA	392	40,958
	10 20 30 40 50 60 MGVVTKKILI LGSTGSIGTQ ALDVIADNSD KFEVVGIAAG GSQPDLVISQ AQQLGLAADK 70 80 90 100 110 120 VAVADAQAAA VISKALGGEI 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 AAHTWAFEPV 310 320 330 340 350 360 DDAAFPAVQL ARHVAKQKGT YPAVYNAANE EAAEAFLRGR IKFPQIVDVV DEVLQGASQF 370 380 390 AGVASHVDDI LATESEARAR ANALINRLAT NL

References

[1]	"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000036 Genomic DNA. Translation: BAB99409.1. BX927154 Genomic DNA. Translation: CAF20356.1.
RefSeq	NP_601221.1. NC_003450.3. YP_226257.1. NC_006958.1.
3D structure databases
ProteinModelPortal	Q8NP10.
SMR	Q8NP10. Positions 7-386.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1019972. 3345361.
GenomeReviews	Gene locus Cgl2016 in contig BA000036_GR. Gene locus cg2208 in contig BX927147_GR.
KEGG	cgb:cg2208. cgl:NCgl1940.
PATRIC	21496036. VBICorGlu203724_1954.
Phylogenomic databases
HOGENOM	HBG430762.
OMA	IHSMVEY.
PhylomeDB	Q8NP10.
ProtClustDB	PRK05447.
Enzyme and pathway databases
BioCyc	CGLU196627:CG2208-MONOMER.
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_CORGL

Accession

Primary (citable) accession number: Q8NP10

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2002
Last sequence update:	October 19, 2002
Last modified:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program