Q9X5F2 (DXR_ZYMMO) 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:	ZMO1150

Organism

Zymomonas mobilis [Complete proteome] [HAMAP]

Taxonomic identifier

542 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Sphingomonadaceae › Zymomonas

Protein attributes

Sequence length	388 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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). 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. Prefers magnesium, manganese or cobalt.
Enzyme regulation	Inhibited by fosmidomycin. 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
Subunit structure	Homodimer.
Sequence similarities	Belongs to the DXR family.

Ontologies

Keywords
Biological process	Isoprene biosynthesis
Ligand	Cobalt Magnesium Manganese Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	3D-structure 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 – 388

388

1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183

PRO_0000163747

Regions

Nucleotide binding

10 – 39

30

NADP By similarity

Sites

Metal binding

150

1

Divalent metal cation By similarity

Metal binding

152

1

Divalent metal cation By similarity

Metal binding

221

1

Divalent metal cation By similarity

Binding site

125

1

Substrate By similarity

Binding site

152

1

Substrate By similarity

Binding site

176

1

Substrate By similarity

Binding site

199

1

Substrate By similarity

Binding site

221

1

Substrate By similarity

Experimental info

Sequence conflict

226

1

Y → F in CAB60758. Ref.1

Secondary structure

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388

Helix Strand Turn

Details...

Beta strand

5 – 11

7

Helix

15 – 26

12

Helix

27 – 30

4

Beta strand

31 – 40

10

Helix

42 – 51

10

Beta strand

55 – 60

6

Helix

62 – 64

3

Helix

65 – 71

7

Turn

72 – 74

3

Beta strand

76 – 82

7

Helix

83 – 90

8

Beta strand

95 – 99

5

Helix

104 – 106

3

Helix

107 – 115

9

Beta strand

118 – 122

5

Helix

126 – 129

4

Helix

132 – 142

11

Beta strand

145 – 148

4

Helix

151 – 159

9

Helix

165 – 167

3

Beta strand

168 – 175

8

Turn

179 – 182

4

Helix

185 – 188

4

Helix

193 – 197

5

Helix

206 – 213

8

Helix

216 – 229

14

Helix

233 – 235

3

Beta strand

236 – 240

5

Beta strand

246 – 252

7

Beta strand

257 – 261

5

Helix

267 – 275

9

Helix

289 – 292

4

Beta strand

294 – 296

3

Turn

302 – 304

3

Helix

306 – 317

12

Helix

321 – 337

17

Helix

345 – 356

12

Helix

365 – 384

20

Sequences

	Sequence		Length	Mass (Da)
	Q9X5F2 [UniParc]. Last modified February 15, 2005. Version 3. Checksum: 373EB372AA325AAF	FASTA	388	41,858
	10 20 30 40 50 60 MSQPRTVTVL GATGSIGHST LDLIERNLDR YQVIALTANR NVKDLADAAK RTNAKRAVIA 70 80 90 100 110 120 DPSLYNDLKE ALAGSSVEAA AGADALVEAA MMGADWTMAA IIGCAGLKAT LAAIRKGKTV 130 140 150 160 170 180 ALANKESLVS AGGLMIDAVR EHGTTLLPVD SEHNAIFQCF PHHNRDYVRR IIITASGGPF 190 200 210 220 230 240 RTTSLAEMAT VTPERAVQHP NWSMGAKISI DSATMMNKGL ELIEAYHLFQ IPLEKFEILV 250 260 270 280 290 300 HPQSVIHSMV EYLDGSILAQ IGSPDMRTPI GHTLAWPKRM ETPAESLDFT KLRQMDFEAP 310 320 330 340 350 360 DYERFPALTL AMESIKSGGA RPAVMNAANE IAVAAFLDKK IGFLDIAKIV EKTLDHYTPA 370 380 TPSSLEDVFA IDNEARIQAA ALMESLPA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of the dxr gene of Zymomonas mobilis and characterization of the 1-deoxy-D-xylulose 5-phosphate reductoisomerase." Grolle S., Bringer-Meyer S., Sahm H. FEMS Microbiol. Lett. 191:131-137(2000) [PubMed: 11004410] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: ATCC 31821 / ZM4 / CP4.
[2]	Lee H.J., Kang H.S. Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 31821 / ZM4 / CP4.
[3]	"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4." Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. , Kang H.L., Lee S.Y., Lee K.J., Kang H.S. Nat. Biotechnol. 23:63-68(2005) [PubMed: 15592456] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31821 / ZM4 / CP4.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ250714 Genomic DNA. Translation: CAB60758.1.
AF124757 Genomic DNA. Translation: AAD29659.1.
AE008692 Genomic DNA. Translation: AAV89774.1.

RefSeq

YP_162885.1. NC_006526.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1R0K	X-ray	1.91	A/B/C/D	1-388	[»]
1R0L	X-ray	2.70	A/B/C/D	1-388	[»]

ProteinModelPortal

Q9X5F2.

SMR

Q9X5F2. Positions 3-386.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3188958.

GenomeReviews

Gene locus ZMO1150 in contig AE008692_GR.

KEGG

zmo:ZMO1150.

NMPDR

fig|264203.3.peg.343.

PATRIC

32567594. VBIZymMob102260_1089.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HBG430762.

OMA

IHSMVEY.

ProtClustDB

PRK05447.

Enzyme and pathway databases

BioCyc

ZMOB264203:ZMO1150-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_ZYMMO

Accession

Primary (citable) accession number: Q9X5F2
Secondary accession number(s): Q5NND6, Q9RIA9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	February 15, 2005
Last modified:	January 25, 2012
This is version 83 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program