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Protein

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

Gene

dxs

Organism
Rhodopseudomonas palustris (strain TIE-1)
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)
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 sitei79 – 791Thiamine pyrophosphateUniRule annotation
Metal bindingi151 – 1511MagnesiumUniRule annotation
Metal bindingi180 – 1801MagnesiumUniRule annotation
Binding sitei180 – 1801Thiamine pyrophosphateUniRule annotation
Binding sitei290 – 2901Thiamine pyrophosphateUniRule annotation
Binding sitei372 – 3721Thiamine 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

BioCyciRPAL395960:GHPC-1035-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:Rpal_1022
OrganismiRhodopseudomonas palustris (strain TIE-1)
Taxonomic identifieri395960 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
Proteomesi
  • UP000001725 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6416411-deoxy-D-xylulose-5-phosphate synthasePRO_1000115763Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB3QFY7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni120 – 1223Thiamine pyrophosphate bindingUniRule annotation
Regioni152 – 1532Thiamine pyrophosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the transketolase family. DXPS subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000012988.
KOiK01662.
OMAiHAVGPFD.
OrthoDBiEOG68Q0SV.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 3 hits.
HAMAPiMF_00315. DXP_synth.
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. 2 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.

B3QFY7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEFSKTPLL DTIRTPEDLR KLRIDQVRQV ADELRLETID AVSVTGGHFG
60 70 80 90 100
AGLGVVELTT ALHYVFDTPR DRLIWDVGHQ AYPHKILTGR RDRIRTLRTG
110 120 130 140 150
GGLSGFTKRT ESDHDPFGAG HSSTSISAGL GMAVASELAG KKNNVIAVIG
160 170 180 190 200
DGSISAGMAY EAMNNAGAMN SRLIVILNDN NMSIAPPVGA MSAYLSRLYS
210 220 230 240 250
GKTYRSLREA GKQIGKHLPK LIADRAARAE EYSRGFMMGG GTLFEELGFY
260 270 280 290 300
YVGPVDGHNL DHLLPILQNV RDADTGPFLI HVVTQKGKGY GPAEAAADKY
310 320 330 340 350
HAVVKFDIAT GAQAKAKSNA PSYQNVFGQS LVKEAQKDDK IVGITAAMPS
360 370 380 390 400
GTGIDIFEKA FPKRTFDVGI AEQHAVTFAA GLATEGYKPF CAIYSTFLQR
410 420 430 440 450
AYDQIVHDVA IQKLPVRFAI DRAGLVGADG ATHAGSFDNA YLGCLPNMVI
460 470 480 490 500
MAAADEAELV HMVATQVAID DRPSAVRYPR GEGRGVEMPE VGIPLEIGKG
510 520 530 540 550
RVIRQGNKVA LLSFGTRLAE AEKAADELAT LGLSTTVADA RFMKPLDVEL
560 570 580 590 600
VLKLARDHEV LLTIEEGSIG GFGSHVMQTL AEHGMLDGEV KMRALVLPDV
610 620 630 640
FMDHDNPVAM YARAGLDAKA IVKKVFDVLG KDAATETSKL A
Length:641
Mass (Da):68,804
Last modified:September 2, 2008 - v1
Checksum:iD0B87B589FCAB05D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001096 Genomic DNA. Translation: ACE99578.1.
RefSeqiWP_011156487.1. NC_011004.1.

Genome annotation databases

EnsemblBacteriaiACE99578; ACE99578; Rpal_1022.
KEGGirpt:Rpal_1022.
PATRICi23306464. VBIRhoPal88240_1053.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001096 Genomic DNA. Translation: ACE99578.1.
RefSeqiWP_011156487.1. NC_011004.1.

3D structure databases

ProteinModelPortaliB3QFY7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACE99578; ACE99578; Rpal_1022.
KEGGirpt:Rpal_1022.
PATRICi23306464. VBIRhoPal88240_1053.

Phylogenomic databases

HOGENOMiHOG000012988.
KOiK01662.
OMAiHAVGPFD.
OrthoDBiEOG68Q0SV.

Enzyme and pathway databases

UniPathwayiUPA00064; UER00091.
BioCyciRPAL395960:GHPC-1035-MONOMER.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 3 hits.
HAMAPiMF_00315. DXP_synth.
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. 2 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsiTIGR00204. dxs. 1 hit.
PROSITEiPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TIE-1.

Entry informationi

Entry nameiDXS_RHOPT
AccessioniPrimary (citable) accession number: B3QFY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 2, 2008
Last modified: May 11, 2016
This is version 55 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

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.