Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei125 – 1251SubstrateUniRule annotation
Metal bindingi150 – 1501Divalent metal cationUniRule annotation
Metal bindingi152 – 1521Divalent metal cationUniRule annotation
Binding sitei152 – 1521SubstrateUniRule annotation
Binding sitei176 – 1761SubstrateUniRule annotation
Binding sitei199 – 1991SubstrateUniRule annotation
Metal bindingi221 – 2211Divalent metal cationUniRule annotation
Binding sitei221 – 2211SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 3930NADPUniRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3883881-deoxy-D-xylulose 5-phosphate reductoisomerasePRO_0000163747Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
388
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 117Combined sources
Helixi15 – 2612Combined sources
Helixi27 – 304Combined sources
Beta strandi31 – 4010Combined sources
Helixi42 – 5110Combined sources
Beta strandi55 – 606Combined sources
Helixi62 – 643Combined sources
Helixi65 – 717Combined sources
Turni72 – 743Combined sources
Beta strandi76 – 827Combined sources
Helixi83 – 908Combined sources
Beta strandi95 – 995Combined sources
Helixi104 – 1063Combined sources
Helixi107 – 1159Combined sources
Beta strandi118 – 1225Combined sources
Helixi126 – 1294Combined sources
Helixi132 – 14211Combined sources
Beta strandi145 – 1484Combined sources
Helixi151 – 1599Combined sources
Helixi165 – 1673Combined sources
Beta strandi168 – 1758Combined sources
Turni179 – 1824Combined sources
Helixi185 – 1884Combined sources
Helixi193 – 1975Combined sources
Helixi206 – 2138Combined sources
Helixi216 – 22914Combined sources
Helixi233 – 2353Combined sources
Beta strandi236 – 2405Combined sources
Beta strandi246 – 2527Combined sources
Beta strandi257 – 2615Combined sources
Helixi267 – 2759Combined sources
Helixi289 – 2924Combined sources
Beta strandi294 – 2963Combined sources
Turni302 – 3043Combined sources
Helixi306 – 31712Combined sources
Helixi321 – 33717Combined sources
Helixi345 – 35612Combined sources
Helixi365 – 38420Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R0KX-ray1.91A/B/C/D1-388[»]
1R0LX-ray2.70A/B/C/D1-388[»]
ProteinModelPortaliQ9X5F2.
SMRiQ9X5F2. Positions 3-386.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X5F2.

Family & Domainsi

Sequence similaritiesi

Belongs to the DXR family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000007220.
KOiK00099.
OMAiGFCPLSE.
OrthoDBiEOG6R2H04.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00183. DXP_reductoisom.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti226 – 2261Y → F in CAB60758 (PubMed:11004410).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1R0KX-ray1.91A/B/C/D1-388[»]
1R0LX-ray2.70A/B/C/D1-388[»]
ProteinModelPortaliQ9X5F2.
SMRiQ9X5F2. Positions 3-386.
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.
OrthoDBiEOG6R2H04.

Enzyme and pathway databases

UniPathwayiUPA00056; UER00092.

Miscellaneous databases

EvolutionaryTraceiQ9X5F2.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00183. DXP_reductoisom.
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...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 31821 / ZM4 / CP4.

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: December 9, 2015
This is version 113 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.