Reviewed, UniProtKB/Swiss-Prot Q2GKQ8 (DXR_ANAPZ)

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:	APH_0440

Organism

Anaplasma phagocytophilum (strain HZ) [Complete proteome] [HAMAP]

Taxonomic identifier

212042 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma › phagocytophilum group

Protein attributes

Sequence length	385 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-PP biosynthesis via DXP pathway; isopentenyl-PP 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 – 385	385	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_1000077331
Regions
	Nucleotide binding	7 – 36	30	NADP By similarity
Sites
	Metal binding	148	1	Divalent metal cation By similarity
	Metal binding	150	1	Divalent metal cation By similarity
	Metal binding	217	1	Divalent metal cation By similarity
	Binding site	123	1	Substrate By similarity
	Binding site	150	1	Substrate By similarity
	Binding site	172	1	Substrate By similarity
	Binding site	195	1	Substrate By similarity
	Binding site	217	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2GKQ8-1 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: 253AE0A7AF9BEB47	FASTA	385	41,579
	10 20 30 40 50 60 MKKVSVFGST GFIGKTTVGI LSGNTEDFKV IALVAGSNVS LLAQQAKLLN AEMAVIADDA 70 80 90 100 110 120 QYEELKRSLH GSGIRVAAGK EAVLEAAALS VDTAVMAITG IVALSAVMRL IESGVGTIAL 130 140 150 160 170 180 ASKESVVCGG VLLRDAACKS GTRIVPVDSE HNAVFRLLSQ GDNPYKITIT ASGGPFLHWS 190 200 210 220 230 240 HDQLKSVTIE DALVHPVWKM GKKISVDSAT MMNKALEVLE ASYLFELGYR KIDVVIHPES 250 260 270 280 290 300 IVHALAFYQD GTSTALMSLP DMSIPILHAL YWPHRKEVSV REVDLIAYGK LTFIRPDFER 310 320 330 340 350 360 FPALKAAFDI LQSSERDVAS IVFNAANEVA VESFLNSEIT FLEIVNIVLH VMNKVPYGKV 370 380 SSLADIMEYD LLGRCIAREV ISDAS

References

[1]

"Comparative genomics of emerging human ehrlichiosis agents." Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N. , Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H. PLoS Genet. 2:208-222(2006) [PubMed: 16482227] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000235 Genomic DNA. Translation: ABD44127.1.
RefSeq	YP_505043.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3930540.
GenomeReviews	Gene locus APH_0440 in contig CP000235_GR.
KEGG	aph:APH_0440.
NMPDR	fig|212042.5.peg.429.
TIGR	APH_0440.
Phylogenomic databases
HOGENOM	Q2GKQ8.
OMA	Q2GKQ8. IHSMVEY.
Enzyme and pathway databases
BioCyc	APHA212042:APH_0440-MON.
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_ANAPZ

Accession

Primary (citable) accession number: Q2GKQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	March 21, 2006
Last modified:	June 16, 2009
This is version 26 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)