B0V6F3 (DXR_ACIBY) 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:	ABAYE1581

Organism

Acinetobacter baumannii (strain AYE) [Complete proteome] [HAMAP]

Taxonomic identifier

509173 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter › Acinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length	398 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 – 398	398	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_1000098470
Regions
	Nucleotide binding	8 – 37	30	NADP By similarity
Sites
	Metal binding	151	1	Divalent metal cation By similarity
	Metal binding	153	1	Divalent metal cation By similarity
	Metal binding	231	1	Divalent metal cation By similarity
	Binding site	126	1	Substrate By similarity
	Binding site	153	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)
	B0V6F3 [UniParc]. Last modified April 8, 2008. Version 1. Checksum: AD5A8F5842524EF6	FASTA	398	43,022
	10 20 30 40 50 60 MTQSVCILGV TGSIGRSTLK ILGQHPDKYS VFAVSAHSRI SELVEICKQF RPKVVVVPEQ 70 80 90 100 110 120 KIAELKTLFA QQNISDIDVL AGQEGLVDIA SHTDVDIVMA AIVGAAGLLP TLAAVKAGKR 130 140 150 160 170 180 VLLANKEALV MSGEIMMQAA RDHQALLLPV DSEHNAIFQS LPHNYLQADR TGQPQLGVSK 190 200 210 220 230 240 ILLTASGGPF LNHSLEQLVH VTPQQACKHP NWSMGQKISV DSATLMNKGL ELIEACHLFS 250 260 270 280 290 300 ISEHFVTVVV HPQSIIHSMV QYVDGSTLAQ MGNPDMCTPI AHALAWPERL QTNVPALDLF 310 320 330 340 350 360 EYSQLNFQAP DTQKFPALNL ARQAMRAGGL APTILNAANE IAVEAFLMER IGFTSIPQVV 370 380 390 EHTLEKLENA AAESIECILD KDKVARSVAQ QYISSIGG

References

[1]

"Comparative analysis of Acinetobacters: three genomes for three lifestyles." Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., Weissenbach J., Cruveiller S. PLoS ONE 3:E1805-E1805(2008) [PubMed: 18350144] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AYE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU459141 Genomic DNA. Translation: CAM86478.1.
RefSeq	YP_001713478.1. NC_010410.1.
3D structure databases
ProteinModelPortal	B0V6F3.
SMR	B0V6F3. Positions 3-396.
ModBase	Search...
Protein-protein interaction databases
STRING	B0V6F3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6003039.
GenomeReviews	Gene locus ABAYE1581 in contig CU459141_GR.
PATRIC	20726518. VBIAciBau69881_1577.
Organism-specific databases
CMR	Search...
Phylogenomic databases
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.
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_ACIBY

Accession

Primary (citable) accession number: B0V6F3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	April 8, 2008
Last modified:	January 25, 2012
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program