Reviewed, UniProtKB/Swiss-Prot Q6FCG9 (DXR_ACIAD)

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:	ACIAD1376

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

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	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_0000163594
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)
	Q6FCG9-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 1E4300E890377230	FASTA	398	43,383
	10 20 30 40 50 60 MTQSVCILGV TGSIGQSTLK VLAQHPDKYS IYAITAHSRI QELVEICKQF KPKRVVVPDE 70 80 90 100 110 120 HIDQLRQLLL QAGLADIDIL SGTTGLVSVA QDEAVDVVMA AIVGAAGLLP TLAAVKAGKR 130 140 150 160 170 180 VLLANKEALV MSGNIMMQAA RDHQALLLPV DSEHNAIFQS LPSNYLTLEN TGQPQLGVSR 190 200 210 220 230 240 ILLTASGGPF LDYPLEQLSE VTPQQACKHP NWSMGQKISV DSATLMNKGL ELIEACHLFS 250 260 270 280 290 300 ISEHFVTVVV HPQSIIHSMV QYIDGSTLAQ MGNPDMCTPI AHALAWPDRL QTHVPALDLF 310 320 330 340 350 360 THTHLDFREP DTNKFPALNL ARQAMRAGGL SPCILNAANE IAVDAFLKLQ IKFTVIPEVI 370 380 390 EHVLNHVQND TAVNIEQVLE TDMIARQIAH QYVNQIRG

References

[1]

"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR543861 Genomic DNA. Translation: CAG68242.1.
RefSeq	YP_046064.1.
3D structure databases
SMR	Q6FCG9. Positions 3-397.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FCG9.
Genome annotation databases
GeneID	2879772.
GenomeReviews	Gene locus ACIAD1376 in contig CR543861_GR.
KEGG	aci:ACIAD1376.
NMPDR	fig|62977.3.peg.607.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0743.
HOGENOM	HBG430762.
OMA	IHSMVEY.
PhylomeDB	Q6FCG9.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD1376-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]
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_ACIAD

Accession

Primary (citable) accession number: Q6FCG9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	July 19, 2004
Last modified:	February 9, 2010
This is version 39 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)