B4F2C9 (DXR_PROMH) 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:	PMI2281

Organism

Proteus mirabilis (strain HI4320) [Complete proteome] [HAMAP]

Taxonomic identifier

529507 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Proteus › Proteus mirabilis

Protein attributes

Sequence length	397 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-Rule MF_00183
Catalytic activity	2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH. HAMAP-Rule MF_00183
Cofactor	Divalent cation By similarity. HAMAP-Rule MF_00183
Pathway	Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. HAMAP-Rule MF_00183
Subunit structure	Homodimer By similarity. HAMAP-Rule 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	isopentenyl diphosphate biosynthetic process, mevalonate-independent pathway Inferred from electronic annotation. Source: UniProtKB-UniPathway 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 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 – 397	397	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP-Rule MF_00183		PRO_1000098510
Regions
	Nucleotide binding	7 – 36	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	231	1	Divalent metal cation By similarity
	Binding site	125	1	Substrate By similarity
	Binding site	152	1	Substrate By similarity
	Binding site	186	1	Substrate By similarity
	Binding site	209	1	Substrate By similarity
	Binding site	231	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	B4F2C9 [UniParc]. Last modified September 23, 2008. Version 1. Checksum: E33098472E1C7567	FASTA	397	43,298
	10 20 30 40 50 60 MKQITILGST GSIGTSTLSV IENNPDEFQV LALVAGKNAT KMAQQCRAFQ PKYAVMSDEK 70 80 90 100 110 120 SAGELKQLLA NTSCKTEILS GSDAVNEIAA LDEADQVMSA ITGVAGLKPT LAAIEKGKRI 130 140 150 160 170 180 LLANKESLIT SGRLFFDAVA KYGAKVLPID SEHNAIYQSL PTGIQDNLGH ASLEAHGITS 190 200 210 220 230 240 ILLTGSGGPF RYTPLDELDA MTPDQACAHP NWSMGRKISV DSATMMNKGL EYIEARYFFN 250 260 270 280 290 300 ASEAEMEVII HPQSVIHSMV RYRDGSIIAQ IGEPDMRTPI AYSMAYPHRT QSGAKALDFF 310 320 330 340 350 360 EIQALEFIRP DYQRYPCLAL AIEASQRGQA STTVLNAANE VVVDAFLNEK VKFTDIAKIN 370 380 390 RKVVEHFDLS EPQSIDDVLE IDKLARLQTQ QIIAQIV

References

[1]

"Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility." Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Walker D., Whithead S. , Thomson N.R., Rather P.N., Parkhill J., Mobley H.L.T. J. Bacteriol. 190:4027-4037(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HI4320.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM942759 Genomic DNA. Translation: CAR44512.1.
RefSeq	YP_002151999.1. NC_010554.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	529507.PMI2281.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAR44512; CAR44512; PMI2281.
GeneID	6800094.
KEGG	pmr:PMI2281.
PATRIC	20519250. VBIProMir120933_2228.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0743.
HOGENOM	HOG000007221.
KO	K00099.
OMA	AHPNWVM.
Enzyme and pathway databases
BioCyc	PMIR529507:GJIW-2323-MONOMER.
UniPathway	UPA00056; UER00092.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_00183. DXP_reductoisom.
InterPro	IPR003821. DXP_reductoisomerase. IPR013644. DXP_reductoisomerase_C. IPR013512. DXP_reductoisomerase_N. IPR026877. DXPR_C. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR30525. PTHR30525. 1 hit.
Pfam	PF08436. DXP_redisom_C. 1 hit. PF02670. DXP_reductoisom. 1 hit. PF13288. DXPR_C. 1 hit. [Graphical view]
PIRSF	PIRSF006205. Dxp_reductismrs. 1 hit.
SUPFAM	SSF69055. SSF69055. 1 hit.
TIGRFAMs	TIGR00243. Dxr. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DXR_PROMH

Accession

Primary (citable) accession number: B4F2C9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	September 23, 2008
Last modified:	May 1, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program