B4UD63 (DXR_ANASK) 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:	AnaeK_3649

Organism

Anaeromyxobacter sp. (strain K) [Complete proteome] [HAMAP]

Taxonomic identifier

447217 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Cystobacterineae › Myxococcaceae › Anaeromyxobacter

Protein attributes

Sequence length	390 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 – 390	390	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_1000118491
Regions
	Nucleotide binding	7 – 36	30	NADP By similarity
Sites
	Metal binding	147	1	Divalent metal cation By similarity
	Metal binding	149	1	Divalent metal cation By similarity
	Metal binding	218	1	Divalent metal cation By similarity
	Binding site	122	1	Substrate By similarity
	Binding site	149	1	Substrate By similarity
	Binding site	173	1	Substrate By similarity
	Binding site	196	1	Substrate By similarity
	Binding site	218	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	B4UD63 [UniParc]. Last modified September 23, 2008. Version 1. Checksum: 2BB94687F044CF6E	FASTA	390	40,997
	10 20 30 40 50 60 MKRVAILGST GSIGVQALDV VGRFPDRFEV VGLAAGRNAP RLLEQIRRFR PRVVSVCDEA 70 80 90 100 110 120 AARAVRAEAP PGTEVLSGDA GAVAVASHPD AAFVLAAISG GAGLRSTAAA IEAGKPVGLA 130 140 150 160 170 180 NKESMVLAGE LLMARAAAKG VPILPVDSEH SAIHQSLVGH NRGEVRRLIL TASGGPLRCT 190 200 210 220 230 240 PEAELATVTP ERALKHPNWS MGDKITIDSA TLMNKGLEVI EARWLFGVEQ QRIDIVVHPE 250 260 270 280 290 300 SVVHSMVEYV DGSIVAQLGI SDMRGPISYA MGHPERMPLD LPPLDLGRLG KLTFEPPDPA 310 320 330 340 350 360 RFPAYTLAYR ALELGGTAPA VLSGADEAAV AAFLARRCSF TGIAEVCADV LEAHVVEPVR 370 380 390 SVEQALAASE HGRREAEKRV GARAHAPAGR

References

[1]

"Complete sequence of Anaeromyxobacter sp. K." Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikiva G., Beliaev A. Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001131 Genomic DNA. Translation: ACG74861.1.
RefSeq	YP_002135990.1. NC_011145.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	B4UD63.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6787334.
GenomeReviews	Gene locus AnaeK_3649 in contig CP001131_GR.
KEGG	ank:AnaeK_3649.
PATRIC	20942038. VBIAnaSp90767_3690.
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.
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_ANASK

Accession

Primary (citable) accession number: B4UD63

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	September 23, 2008
Last modified:	January 25, 2012
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program