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Protein

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

Gene

dxs

Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
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)DescriptionActionsGraphical viewLength
Binding sitei78Thiamine pyrophosphateUniRule annotation1
Metal bindingi150MagnesiumUniRule annotation1
Metal bindingi179MagnesiumUniRule annotation1
Binding sitei179Thiamine pyrophosphateUniRule annotation1
Binding sitei288Thiamine pyrophosphateUniRule annotation1
Binding sitei370Thiamine pyrophosphateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processIsoprene biosynthesis, Thiamine biosynthesis
LigandMagnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

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:BMEI1498
OrganismiBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Taxonomic identifieri224914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
Proteomesi
  • UP000000419 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001890921 – 6431-deoxy-D-xylulose-5-phosphate synthaseAdd BLAST643

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi224914.BAWG_0726.

Structurei

3D structure databases

ProteinModelPortaliQ8YFM2.
SMRiQ8YFM2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni119 – 121Thiamine pyrophosphate bindingUniRule annotation3
Regioni151 – 152Thiamine pyrophosphate bindingUniRule annotation2

Sequence similaritiesi

Belongs to the transketolase family. DXPS subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C2V. Bacteria.
COG1154. LUCA.
HOGENOMiHOG000012988.
KOiK01662.
OMAiAINHAGH.

Family and domain databases

CDDicd02007. TPP_DXS. 1 hit.
Gene3Di3.40.50.920. 1 hit.
HAMAPiMF_00315. DXP_synth. 1 hit.
InterProiView protein in InterPro
IPR005477. Dxylulose-5-P_synthase.
IPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR033248. Transketolase_C.
IPR005474. Transketolase_N.
PANTHERiPTHR43322. PTHR43322. 1 hit.
PfamiView protein in Pfam
PF13292. DXP_synthase_N. 1 hit.
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
SMARTiView protein in SMART
SM00861. Transket_pyr. 1 hit.
SUPFAMiSSF52518. SSF52518. 3 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsiTIGR00204. dxs. 1 hit.
PROSITEiView protein in PROSITE
PS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8YFM2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRPSTPLLD KAPTPDRLRA LPEQDLPQLA EELRTELIDA VSTTGGHLGA
60 70 80 90 100
GLGVVELTVA LHHVFNTPYD RIIWDVGHQA YPHKILTGRR DRIRTLRQAG
110 120 130 140 150
GLSGFTKRAE SEYDPFGAAH SSTSISAGLG MAVASELSGE KRNVIAVIGD
160 170 180 190 200
GSMSAGMAYE AMNNAGALDA RLIVILNDND MSIAPPTGAM SAYLARLVSG
210 220 230 240 250
RTYRSVREAA KQVAQKLPKF LQDKARKSEE YARAFFTGGT LFEELGFYYV
260 270 280 290 300
GPIDGHNLDH LLPVLKNVRD TQKGPVLIHV VTQKGKGYAP AEAAADKYHG
310 320 330 340 350
VNKFDVITGK QAKPPANAPS YTKIFGTSLI EEARHDDKIV AVTAAMPTGT
360 370 380 390 400
GLDLFGEAFP KRVFDVGIAE QHAVTFAAGL ASEGYKPFCA IYSTFLQRGY
410 420 430 440 450
DQVVHDVSIQ NLPVRFPIDR AGLVGADGPT HAGSFDTGFL AALPGFVVMA
460 470 480 490 500
ASDEAELRHM VRTAAEYDEG PISFRYPRGD GVGVDLPERG SVLEIGKGRI
510 520 530 540 550
VREGTKVALL SFGTRLQECL AAAEELGAAG LSTTVADARF AKPLDHDLIR
560 570 580 590 600
RLAREHEVLV MVEEGAVGGF GSHVLQFLAT DGLLDRGFKV RALTLPDIYQ
610 620 630 640
DHGKPDAMYA EAGLDRTGIV RTVFAALHRD ELGHEALPTP FRA
Length:643
Mass (Da):69,186
Last modified:March 1, 2002 - v1
Checksum:i6DD95A4377235340
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008917 Genomic DNA. Translation: AAL52679.1.
PIRiAD3439.
RefSeqiWP_004686580.1. NZ_GG703778.1.

Genome annotation databases

EnsemblBacteriaiAAL52679; AAL52679; BMEI1498.
GeneIDi29594346.
KEGGibme:BMEI1498.
bmel:DK63_1992.
PATRICifig|224914.52.peg.2093.

Similar proteinsi

Entry informationi

Entry nameiDXS_BRUME
AccessioniPrimary (citable) accession number: Q8YFM2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: March 1, 2002
Last modified: June 7, 2017
This is version 104 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Brucella melitensis
    Brucella melitensis (strain 16M): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families