Q4JV26 (DXR_CORJK) 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
Synonyms:	ispC
Ordered Locus Names:	jk1167

Organism

Corynebacterium jeikeium (strain K411) [Complete proteome] [HAMAP]

Taxonomic identifier

306537 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	408 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 – 408	408	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_0000163643
Regions
	Nucleotide binding	23 – 52	30	NADP By similarity
Sites
	Metal binding	167	1	Divalent metal cation By similarity
	Metal binding	169	1	Divalent metal cation By similarity
	Metal binding	238	1	Divalent metal cation By similarity
	Binding site	144	1	Substrate By similarity
	Binding site	169	1	Substrate By similarity
	Binding site	193	1	Substrate By similarity
	Binding site	216	1	Substrate By similarity
	Binding site	238	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4JV26 [UniParc]. Last modified August 2, 2005. Version 1. Checksum: A39B83E9F8EF08B9	FASTA	408	43,552
	10 20 30 40 50 60 MGRRGVTKKR NRIDRVKTRV VVLGSTGSIG TQALEVMADN PERFELVGIS AHGSKPDVLA 70 80 90 100 110 120 QQVRDFGLDL GRVAVASEHT AEWLDGEFGA HCIRGKDSAR ELVEAVGPEL GECDVILNAL 130 140 150 160 170 180 VGSLGLDATL ATLGTKAKLA LANKESLVAG GQLVLKAADE GQLIPVDSEH SAMAQCLRSG 190 200 210 220 230 240 RVDEVDSLVL TASGGPFRGY TRAQLEDVTP LQAANHPTWS MGQMNTLNSA TMVNKGLELI 250 260 270 280 290 300 EASLLFGIPA EKIDVTVHPQ SIVHSMVTFI DGATIAQASP PSMKLPISLA LGWPDRIADA 310 320 330 340 350 360 QPKLDFTEAT DWHFEPLDDE VFPAVILARQ AVTAGGTMPA VYNAANEEAA VEFLNGRLSF 370 380 390 400 PRIVDTVAAT MEACQHLSAE PNDLEDVLAA EREARAKAHE RMATWLSD

References

[1]

"Complete genome sequence and analysis of the multiresistant nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the human skin flora." Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P., Puehler A. J. Bacteriol. 187:4671-4682(2005) [PubMed: 15968079] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K411.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR931997 Genomic DNA. Translation: CAI37331.1.
RefSeq	YP_250949.1. NC_007164.1.
3D structure databases
ProteinModelPortal	Q4JV26.
SMR	Q4JV26. Positions 17-403.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4JV26.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3432461.
GenomeReviews	Gene locus jk1167 in contig CR931997_GR.
KEGG	cjk:jk1167.
NMPDR	fig|306537.3.peg.1311.
PATRIC	21513264. VBICorJei31838_1181.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0743.
HOGENOM	HBG430762.
OMA	IHSMVEY.
ProtClustDB	PRK05447.
Enzyme and pathway databases
BioCyc	CJEI306537:JK1167-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_CORJK

Accession

Primary (citable) accession number: Q4JV26

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	August 2, 2005
Last modified:	January 25, 2012
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program