Q313H2 (DXR_DESDG) 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:	Dde_1123

Organism

Desulfovibrio desulfuricans (strain G20) [Complete proteome] [HAMAP]

Taxonomic identifier

207559 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio › Desulfovibrio alaskensis

Protein attributes

Sequence length	407 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
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 – 407	407	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP-Rule MF_00183		PRO_1000020255
Regions
	Nucleotide binding	24 – 53	30	NADP By similarity
Sites
	Metal binding	166	1	Divalent metal cation By similarity
	Metal binding	168	1	Divalent metal cation By similarity
	Metal binding	237	1	Divalent metal cation By similarity
	Binding site	141	1	Substrate By similarity
	Binding site	168	1	Substrate By similarity
	Binding site	192	1	Substrate By similarity
	Binding site	215	1	Substrate By similarity
	Binding site	237	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q313H2 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: 7C196C23DA5135E3	FASTA	407	43,573
	10 20 30 40 50 60 MNGYISPLPD AAWNSRFPRS LVLLGSTGSI GTSALRVVER QPELFRITAL AGARNVRLLA 70 80 90 100 110 120 RQAAAYRPPH LAVINGNAAD ELASLLPAGY RPRIHTGQEG YEFLAALPEA DCVLSAQVGA 130 140 150 160 170 180 AGLRATVAAA RAGKTIALAN KESLVLAGGL IRRLCHETGA SVLPVDSEHN AIFQALQGHD 190 200 210 220 230 240 AAQMRRIILT ASGGPFRGRD RTFLQSVTRE QALNHPNWSM GAKISIDSAT LMNKGLEVIE 250 260 270 280 290 300 ACHLYNAPLE KVEVVVHPQS IIHSLVEYND GSQIAHMGTP DMRIAIAYCL GWPRVMHTGV 310 320 330 340 350 360 EPLDLLSVGS LTFESPDISL FPCLELARKA YAGGNGLPVV LNAANEVAVD LFLQGAIAFL 370 380 390 400 DIPRLIEAAM QAHDAAPHQN MYDEVESILT LDKTTRRVTA DLAGARG

References

[1]

"Complete genome sequence and updated annotation of Desulfovibrio alaskensis G20." Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L., Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S., Nolan M. , Lapidus A.L., Palumbo A.V., Wall J.D. J. Bacteriol. 193:4268-4269(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: G20.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000112 Genomic DNA. Translation: ABB37924.1.
RefSeq	YP_387619.1. NC_007519.1.
3D structure databases
ProteinModelPortal	Q313H2.
ModBase	Search...
Protein-protein interaction databases
STRING	207559.Dde_1123.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABB37924; ABB37924; Dde_1123.
GeneID	3755147.
KEGG	dde:Dde_1123.
PATRIC	21741195. VBIDesDes50040_1130.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0743.
HOGENOM	HOG000007221.
KO	K00099.
OMA	FIDGSVM.
ProtClustDB	PRK05447.
Enzyme and pathway databases
BioCyc	DALA207559:GH1L-975-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_DESDG

Accession

Primary (citable) accession number: Q313H2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	December 6, 2005
Last modified:	May 1, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program