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Protein

1-deoxy-D-xylulose 5-phosphate reductoisomerase

Gene

dxr

Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).

Catalytic activityi

2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH.UniRule annotation

Cofactori

Mg2+, Mn2+, Co2+Note: Divalent cation. Prefers Mg2+, Mn2+ or Co2+.

Enzyme regulationi

Inhibited by fosmidomycin.

Pathwayi: isopentenyl diphosphate biosynthesis via DXP pathway

This protein is involved in step 1 of the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate.UniRule annotation
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr)
  2. Bifunctional enzyme IspD/IspF (ispDF)
  3. 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE)
  4. Bifunctional enzyme IspD/IspF (ispDF)
  5. 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) (ispG)
  6. 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH)
This subpathway is part of the pathway isopentenyl diphosphate biosynthesis via DXP pathway, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate, the pathway isopentenyl diphosphate biosynthesis via DXP pathway and in Isoprenoid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei125SubstrateUniRule annotation1
Metal bindingi150Divalent metal cationUniRule annotation1
Metal bindingi152Divalent metal cationUniRule annotation1
Binding sitei152SubstrateUniRule annotation1
Binding sitei176SubstrateUniRule annotation1
Binding sitei199SubstrateUniRule annotation1
Metal bindingi221Divalent metal cationUniRule annotation1
Binding sitei221SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 39NADPUniRule annotationAdd BLAST30

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Isoprene biosynthesis

Keywords - Ligandi

Cobalt, Magnesium, Manganese, Metal-binding, NADP

Enzyme and pathway databases

UniPathwayiUPA00056; UER00092.

Names & Taxonomyi

Protein namesi
Recommended name:
1-deoxy-D-xylulose 5-phosphate reductoisomeraseUniRule annotation (EC:1.1.1.267UniRule annotation)
Short name:
DXP reductoisomeraseUniRule annotation
Alternative name(s):
1-deoxyxylulose-5-phosphate reductoisomeraseUniRule annotation
2-C-methyl-D-erythritol 4-phosphate synthaseUniRule annotation
Gene namesi
Name:dxrUniRule annotation
Ordered Locus Names:ZMO1150
OrganismiZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Taxonomic identifieri264203 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas
Proteomesi
  • UP000001173 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001637471 – 3881-deoxy-D-xylulose 5-phosphate reductoisomeraseAdd BLAST388

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1388
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 11Combined sources7
Helixi15 – 26Combined sources12
Helixi27 – 30Combined sources4
Beta strandi31 – 40Combined sources10
Helixi42 – 51Combined sources10
Beta strandi55 – 60Combined sources6
Helixi62 – 64Combined sources3
Helixi65 – 71Combined sources7
Turni72 – 74Combined sources3
Beta strandi76 – 82Combined sources7
Helixi83 – 90Combined sources8
Beta strandi95 – 99Combined sources5
Helixi104 – 106Combined sources3
Helixi107 – 115Combined sources9
Beta strandi118 – 122Combined sources5
Helixi126 – 129Combined sources4
Helixi132 – 142Combined sources11
Beta strandi145 – 148Combined sources4
Helixi151 – 159Combined sources9
Helixi165 – 167Combined sources3
Beta strandi168 – 175Combined sources8
Turni179 – 182Combined sources4
Helixi185 – 188Combined sources4
Helixi193 – 197Combined sources5
Helixi206 – 213Combined sources8
Helixi216 – 229Combined sources14
Helixi233 – 235Combined sources3
Beta strandi236 – 240Combined sources5
Beta strandi246 – 252Combined sources7
Beta strandi257 – 261Combined sources5
Helixi267 – 275Combined sources9
Helixi289 – 292Combined sources4
Beta strandi294 – 296Combined sources3
Turni302 – 304Combined sources3
Helixi306 – 317Combined sources12
Helixi321 – 337Combined sources17
Helixi345 – 356Combined sources12
Helixi365 – 384Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R0KX-ray1.91A/B/C/D1-388[»]
1R0LX-ray2.70A/B/C/D1-388[»]
ProteinModelPortaliQ9X5F2.
SMRiQ9X5F2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X5F2.

Family & Domainsi

Sequence similaritiesi

Belongs to the DXR family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000007220.
KOiK00099.
OMAiGFCPLSE.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00183. DXP_reductoisom. 1 hit.
InterProiIPR003821. DXP_reductoisomerase.
IPR013644. DXP_reductoisomerase_C.
IPR013512. DXP_reductoisomerase_N.
IPR026877. DXPR_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF08436. DXP_redisom_C. 1 hit.
PF02670. DXP_reductoisom. 1 hit.
PF13288. DXPR_C. 1 hit.
[Graphical view]
PIRSFiPIRSF006205. Dxp_reductismrs. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF69055. SSF69055. 1 hit.
TIGRFAMsiTIGR00243. Dxr. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9X5F2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQPRTVTVL GATGSIGHST LDLIERNLDR YQVIALTANR NVKDLADAAK
60 70 80 90 100
RTNAKRAVIA DPSLYNDLKE ALAGSSVEAA AGADALVEAA MMGADWTMAA
110 120 130 140 150
IIGCAGLKAT LAAIRKGKTV ALANKESLVS AGGLMIDAVR EHGTTLLPVD
160 170 180 190 200
SEHNAIFQCF PHHNRDYVRR IIITASGGPF RTTSLAEMAT VTPERAVQHP
210 220 230 240 250
NWSMGAKISI DSATMMNKGL ELIEAYHLFQ IPLEKFEILV HPQSVIHSMV
260 270 280 290 300
EYLDGSILAQ IGSPDMRTPI GHTLAWPKRM ETPAESLDFT KLRQMDFEAP
310 320 330 340 350
DYERFPALTL AMESIKSGGA RPAVMNAANE IAVAAFLDKK IGFLDIAKIV
360 370 380
EKTLDHYTPA TPSSLEDVFA IDNEARIQAA ALMESLPA
Length:388
Mass (Da):41,858
Last modified:February 15, 2005 - v3
Checksum:i373EB372AA325AAF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti226Y → F in CAB60758 (PubMed:11004410).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250714 Genomic DNA. Translation: CAB60758.1.
AF124757 Genomic DNA. Translation: AAD29659.1.
AE008692 Genomic DNA. Translation: AAV89774.1.
RefSeqiWP_011240977.1. NC_006526.2.

Genome annotation databases

EnsemblBacteriaiAAV89774; AAV89774; ZMO1150.
KEGGizmo:ZMO1150.
PATRICi32567594. VBIZymMob102260_1089.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250714 Genomic DNA. Translation: CAB60758.1.
AF124757 Genomic DNA. Translation: AAD29659.1.
AE008692 Genomic DNA. Translation: AAV89774.1.
RefSeqiWP_011240977.1. NC_006526.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R0KX-ray1.91A/B/C/D1-388[»]
1R0LX-ray2.70A/B/C/D1-388[»]
ProteinModelPortaliQ9X5F2.
SMRiQ9X5F2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV89774; AAV89774; ZMO1150.
KEGGizmo:ZMO1150.
PATRICi32567594. VBIZymMob102260_1089.

Phylogenomic databases

HOGENOMiHOG000007220.
KOiK00099.
OMAiGFCPLSE.

Enzyme and pathway databases

UniPathwayiUPA00056; UER00092.

Miscellaneous databases

EvolutionaryTraceiQ9X5F2.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00183. DXP_reductoisom. 1 hit.
InterProiIPR003821. DXP_reductoisomerase.
IPR013644. DXP_reductoisomerase_C.
IPR013512. DXP_reductoisomerase_N.
IPR026877. DXPR_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF08436. DXP_redisom_C. 1 hit.
PF02670. DXP_reductoisom. 1 hit.
PF13288. DXPR_C. 1 hit.
[Graphical view]
PIRSFiPIRSF006205. Dxp_reductismrs. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF69055. SSF69055. 1 hit.
TIGRFAMsiTIGR00243. Dxr. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDXR_ZYMMO
AccessioniPrimary (citable) accession number: Q9X5F2
Secondary accession number(s): Q5NND6, Q9RIA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 15, 2005
Last modified: November 2, 2016
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.