Reviewed, UniProtKB/Swiss-Prot B7I9U9 (DXR_ACIB5)

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:	AB57_2316

Organism

Acinetobacter baumannii (strain AB0057) [Complete proteome] [HAMAP]

Taxonomic identifier

480119 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	398 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW 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 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_1000118489
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)
	B7I9U9-1 [UniParc]. Last modified February 10, 2009. 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 genome sequence analysis of multidrug-resistant Acinetobacter baumannii." Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M., Bonomo R.A., Gill S.R. J. Bacteriol. 190:8053-8064(2008) [PubMed: 18931120] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP001182 Genomic DNA. Translation: ACJ42432.1.
RefSeq	YP_002319668.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	7045743.
GenomeReviews	Gene locus AB57_2316 in contig CP001182_GR.
KEGG	abn:AB57_2316.
Organism-specific databases
CMR	Search...
Family and domain databases
HAMAP	MF_00183. [Tree]
InterPro	IPR003821. DXP_reductoisomerase. IPR013644. DXP_reductoisomerase_C. IPR013512. DXP_reductoisomerase_N. [Graphical view]
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_ACIB5

Accession

Primary (citable) accession number: B7I9U9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 10, 2009
Last modified:	September 22, 2009
This is version 7 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)