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Protein

1-deoxy-D-xylulose-5-phosphate synthase

Gene

dxs

Organism
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).UniRule annotation

Catalytic activityi

Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO2.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation
  • thiamine diphosphateUniRule annotationNote: Binds 1 thiamine pyrophosphate per subunit.UniRule annotation

Pathwayi: 1-deoxy-D-xylulose 5-phosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. 1-deoxy-D-xylulose-5-phosphate synthase (dxs), 1-deoxy-D-xylulose-5-phosphate synthase (dxs)
This subpathway is part of the pathway 1-deoxy-D-xylulose 5-phosphate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate, the pathway 1-deoxy-D-xylulose 5-phosphate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei76 – 761Thiamine pyrophosphateUniRule annotation
Metal bindingi148 – 1481MagnesiumUniRule annotation
Metal bindingi177 – 1771MagnesiumUniRule annotation
Binding sitei177 – 1771Thiamine pyrophosphateUniRule annotation
Binding sitei284 – 2841Thiamine pyrophosphateUniRule annotation
Binding sitei365 – 3651Thiamine pyrophosphateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Isoprene biosynthesis, Thiamine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciFTUL177416:GNBP-1036-MONOMER.
UniPathwayiUPA00064; UER00091.

Names & Taxonomyi

Protein namesi
Recommended name:
1-deoxy-D-xylulose-5-phosphate synthaseUniRule annotation (EC:2.2.1.7UniRule annotation)
Alternative name(s):
1-deoxyxylulose-5-phosphate synthaseUniRule annotation
Short name:
DXP synthaseUniRule annotation
Short name:
DXPSUniRule annotation
Gene namesi
Name:dxsUniRule annotation
Ordered Locus Names:FTT_1018c
OrganismiFrancisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Taxonomic identifieri177416 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
Proteomesi
  • UP000001174 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6156151-deoxy-D-xylulose-5-phosphate synthasePRO_0000256420Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

IntActiQ5NG39. 1 interaction.
STRINGi177416.FTT_1018c.

Structurei

3D structure databases

ProteinModelPortaliQ5NG39.
SMRiQ5NG39. Positions 1-178.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni117 – 1193Thiamine pyrophosphate bindingUniRule annotation
Regioni149 – 1502Thiamine pyrophosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the transketolase family. DXPS subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C2V. Bacteria.
COG1154. LUCA.
HOGENOMiHOG000012988.
KOiK01662.
OMAiHAVGPFD.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 3 hits.
HAMAPiMF_00315. DXP_synth. 1 hit.
InterProiIPR005477. Dxylulose-5-P_synthase.
IPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR033248. Transketolase_C.
IPR033247. Transketolase_fam.
IPR005474. Transketolase_N.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 2 hits.
PfamiPF13292. DXP_synthase_N. 1 hit.
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 3 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsiTIGR00204. dxs. 1 hit.
PROSITEiPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5NG39-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKYTILDKI NTPSDLKLIP ESQLKILSAE LRAFLVDTLD VSGGHFASSL
60 70 80 90 100
GATELTVALH YVYNAPYDNI VWDVGHQTYI HKILTGRKDK LVTIKKDGGI
110 120 130 140 150
SGFPKRSESE YDTFGVGHSS TSISAALGMA IADRLQGKSS NTVAVIGDGA
160 170 180 190 200
ITGGMAFEAL NHAGGIKEDI LVILNDNEMS ISDNVGGLSA HFSKIISGGF
210 220 230 240 250
YNSIREKGKE VLKNIPPIFE FVKKVETQTK GMFVPANFFE DLGFYYVGPI
260 270 280 290 300
DGHDVTELVK TLRILKDHKG PKLLHVITKK GKGYTKAESD PIKFHHVAPS
310 320 330 340 350
FHSGENITTK ISKPTYSNIF GDWICQKAAK DKRLVGITPA MKEGSDLIRF
360 370 380 390 400
SQLYPHRYFD VAIAEQHAVT FAGGLACQGL KPVVAIYSTF LQRAYDQVIH
410 420 430 440 450
DIALQNLDVL YAVDRAGLVG ADGATHDGSF DLAFMRCIPN HVIMTPSDEN
460 470 480 490 500
EAYHMLEFGY EYNGPAMVRY PRGAGIGAEI TGSLDLELGK AKIVKQGSKI
510 520 530 540 550
AILNFGTLLP LAKQLAEKYH ATVIDMRFVK PLDEIMLDKV SQTHEIILTL
560 570 580 590 600
EENCIAGGAG SAVNEYFVAK DLSNKIIVRN FGLQDKFLNH GTKDLLLAQS
610
KLCVENISQE LDKLI
Length:615
Mass (Da):67,342
Last modified:February 1, 2005 - v1
Checksum:i7B63D7081B51A6E4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA. Translation: CAG45651.1.
RefSeqiWP_003021112.1. NZ_CP010290.1.
YP_170003.1. NC_006570.2.

Genome annotation databases

EnsemblBacteriaiCAG45651; CAG45651; FTT_1018c.
GeneIDi3191556.
KEGGiftu:FTT_1018c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA. Translation: CAG45651.1.
RefSeqiWP_003021112.1. NZ_CP010290.1.
YP_170003.1. NC_006570.2.

3D structure databases

ProteinModelPortaliQ5NG39.
SMRiQ5NG39. Positions 1-178.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5NG39. 1 interaction.
STRINGi177416.FTT_1018c.

Protocols and materials databases

DNASUi3191556.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG45651; CAG45651; FTT_1018c.
GeneIDi3191556.
KEGGiftu:FTT_1018c.

Phylogenomic databases

eggNOGiENOG4105C2V. Bacteria.
COG1154. LUCA.
HOGENOMiHOG000012988.
KOiK01662.
OMAiHAVGPFD.

Enzyme and pathway databases

UniPathwayiUPA00064; UER00091.
BioCyciFTUL177416:GNBP-1036-MONOMER.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 3 hits.
HAMAPiMF_00315. DXP_synth. 1 hit.
InterProiIPR005477. Dxylulose-5-P_synthase.
IPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR033248. Transketolase_C.
IPR033247. Transketolase_fam.
IPR005474. Transketolase_N.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 2 hits.
PfamiPF13292. DXP_synthase_N. 1 hit.
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 3 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsiTIGR00204. dxs. 1 hit.
PROSITEiPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDXS_FRATT
AccessioniPrimary (citable) accession number: Q5NG39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: February 1, 2005
Last modified: September 7, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.