Q5PAI9 (DXR_ANAMM) 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:	AM743

Organism

Anaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]

Taxonomic identifier

234826 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

Protein attributes

Sequence length	396 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 – 396	396	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_0000163597
Regions
	Nucleotide binding	12 – 41	30	NADP By similarity
Sites
	Metal binding	153	1	Divalent metal cation By similarity
	Metal binding	155	1	Divalent metal cation By similarity
	Metal binding	222	1	Divalent metal cation By similarity
	Binding site	128	1	Substrate By similarity
	Binding site	155	1	Substrate By similarity
	Binding site	177	1	Substrate By similarity
	Binding site	200	1	Substrate By similarity
	Binding site	222	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5PAI9 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 2BBCAE2FEBCC1C52	FASTA	396	42,383
	10 20 30 40 50 60 MLHMGRKRVS VFGSTGCIGQ KAVQILRDNP DDFEVVALVA KQDAHLLASQ ARLLSANMAV 70 80 90 100 110 120 VAEDAAYETL RELLRGTCVE VGAGTAGVMD AASRDVDSAV MAITGIAALH PVIRLIKSGV 130 140 150 160 170 180 KSIALANKES VVCGGELLIN AAKQTGVNIV PVDSEHNAVF QILAHDGCVA RVTLTASGGP 190 200 210 220 230 240 FLRWTREQMQ AVTPSDALAH PVWKMGRKIS VDSATMVNKA LEVIEAHYLF SLDPDSIDVT 250 260 270 280 290 300 VHPESVVHAV AAYPNGTSIS LMSVPDMGIP TLHALYWPQS ATVCGSTLDL ASYGKLTFME 310 320 330 340 350 360 PDLERFPALG FGFEALRSSK PRAACIALNA ANEVAVEAFL NFEIAFLDIP NIIMSAMDKL 370 380 390 ACCEVNSISE AGEYDLICRA RTREICDTLK VSEFIR

References

[1]

"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins." Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr. Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: St. Maries.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000030 Genomic DNA. Translation: AAV86691.1.
RefSeq	YP_153946.1. NC_004842.2.
3D structure databases
ProteinModelPortal	Q5PAI9.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5PAI9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3170951.
GenomeReviews	Gene locus AM743 in contig CP000030_GR.
KEGG	ama:AM743.
PATRIC	20947457. VBIAnaMar46146_0645.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0743.
HOGENOM	HBG430762.
OMA	IHSMVEY.
PhylomeDB	Q5PAI9.
ProtClustDB	PRK05447.
Enzyme and pathway databases
BioCyc	AMAR234826:AM743-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]
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_ANAMM

Accession

Primary (citable) accession number: Q5PAI9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	January 4, 2005
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program