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Q1LTI9 (DXS_BAUCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
1-deoxy-D-xylulose-5-phosphate synthase

EC=2.2.1.7
Alternative name(s):
1-deoxyxylulose-5-phosphate synthase
Short name=DXP synthase
Short name=DXPS
Gene names
Name:dxs
Ordered Locus Names:BCI_0275
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

Protein attributes

Sequence length623 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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) By similarity. HAMAP MF_00315

Catalytic activity

Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO2. HAMAP MF_00315

Cofactor

Binds 1 thiamine pyrophosphate per subunit By similarity.

Pathway

Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1. HAMAP MF_00315

Subunit structure

Homodimer By similarity. HAMAP MF_00315

Sequence similarities

Belongs to the transketolase family. DXPS subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6236231-deoxy-D-xylulose-5-phosphate synthase HAMAP MF_00315
PRO_0000256382

Sequences

Sequence LengthMass (Da)Tools
Q1LTI9 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: DF9007B00050FAD0

FASTA62368,720
        10         20         30         40         50         60 
MSMQIKRYPT LDLADNPIKL RLLPKESLLT LCDELRQFLL TSVSGSSGHF ASGLGTVELT 

        70         80         90        100        110        120 
VALHYVYNTP FDNVIWDVGH QAYPHKILTG RRECIATIRQ RNGLHPFPWR EESEYDILSV 

       130        140        150        160        170        180 
GHSSTSISAG LGMAVAATYE GIGRKTVCVI GDGAMTAGMA FEALNHAGDI KSDLLVILND 

       190        200        210        220        230        240 
NKMSISRNVG ALNNHLAQIL SGKLYLRINE SSKKALHGMP YLKELAKRTK EQIKNIIVPN 

       250        260        270        280        290        300 
CTLFEELGFN YIGPVDGHDV QGMVHILKNM RCMKGPQLLH IITQKGRGYA PAEKDPTTWH 

       310        320        330        340        350        360 
AVPKFDPAIG QLPYQNISNY PTYSDVFGDW LCNAATSNKK LIAITPAMRE GSGMAKFANQ 

       370        380        390        400        410        420 
FPQQYFDVAI AEQHAVTFAA GLAISGYKPV VAIYSTFLQR AYDQVIHDVA IQKLPVLFAI 

       430        440        450        460        470        480 
DRGGVVGADG QTHQGAFDLS YLRCVPNMVI MTPSDENECR LMLHTGYHYN NGPSAVRYPR 

       490        500        510        520        530        540 
GNGIGVEYSL LRILPLGKAI VCRQGTKIAI LNFGTLLTQA KKVAKTFDAT LVDMRFVKPL 

       550        560        570        580        590        600 
DIELINQLAI SHQALVTLEE NAVIGGAGSG VNEYLMRQRL LVPVLNIGLP DYFIPQGSQE 

       610        620 
EIRAELKLDS DGIMEQIKQW LAR 

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000238 Genomic DNA. Translation: ABF13902.1.
RefSeqYP_588725.1. NC_007984.1.

3D structure databases

ProteinModelPortalQ1LTI9.
SMRQ1LTI9. Positions 4-622.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1LTI9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4056487.
GenomeReviewsGene locus BCI_0275 in contig CP000238_GR.
KEGGbci:BCI_0275.
PATRIC21074053. VBIBauCic75062_0262.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1154.
HOGENOMHBG571647.
OMAEAMNAHA.
PhylomeDBQ1LTI9.

Enzyme and pathway databases

BioCycBCIC186490:BCI_0275-MONOMER.

Family and domain databases

HAMAPMF_00315. DXP_synth.
[Tree]
InterProIPR001017. DH_E1.
IPR005477. Dxylulose-5-P_synthase.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
KOK01662.
PfamPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52922. Transketo_C_like. 1 hit.
TIGRFAMsTIGR00204. Dxs. 1 hit.
PROSITEPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDXS_BAUCH
AccessionPrimary (citable) accession number: Q1LTI9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: May 30, 2006
Last modified: January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families