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Q5NN52 (DXS1_ZYMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

EC=2.2.1.7
Alternative name(s):
1-deoxyxylulose-5-phosphate synthase 1
Short name=DXP synthase 1
Short name=DXPS 1
Gene names
Name:dxs1
Ordered Locus Names:ZMO1234
OrganismZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) [Complete proteome] [HAMAP]
Taxonomic identifier264203 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas

Protein attributes

Sequence length649 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-Rule MF_00315

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_00315

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-Rule MF_00315

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00315

Sequence similarities

Belongs to the transketolase family. DXPS subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6496491-deoxy-D-xylulose-5-phosphate synthase 1 HAMAP-Rule MF_00315
PRO_0000256510

Regions

Region120 – 1223Thiamine pyrophosphate binding By similarity
Region152 – 1532Thiamine pyrophosphate binding By similarity

Sites

Metal binding1511Magnesium By similarity
Metal binding1801Magnesium By similarity
Binding site791Thiamine pyrophosphate By similarity
Binding site1801Thiamine pyrophosphate By similarity
Binding site2891Thiamine pyrophosphate By similarity
Binding site3711Thiamine pyrophosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5NN52 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 772C535FBA83BE7A

FASTA64970,307
        10         20         30         40         50         60 
MFPNDKTPLL DKIKTPAELR QLDRNSLRQL ADELRKETIS AVGVTGGHLG SGLGVIELTV 

        70         80         90        100        110        120 
ALHYVFNTPK DALVWDVGHQ TYPHKILTGR RDRIRTLRQR DGLSGFTQRA ESEYDAFGAA 

       130        140        150        160        170        180 
HSSTSISAAL GFAMASKLSD SDDKAVAIIG DGSMTAGMAY EAMNNAKAAG KRLIVILNDN 

       190        200        210        220        230        240 
EMSISPPVGA LSSYLSRLIS SRPFMNLRDI MRGVVNRMPK GLATAARKAD EYARGMATGG 

       250        260        270        280        290        300 
TFFEELGFYY VGPVDGHNLD QLIPVLENVR DAKDGPILVH VVTRKGQGYA PAEAAKDKYH 

       310        320        330        340        350        360 
AVQRLDVVSG KQAKAPPGPP SYTSVFSEQL IKEAKQDDKI VTITAAMPTG TGLDRFQQYF 

       370        380        390        400        410        420 
PERMFDVGIA EQHAVTFAAG LAAAGYKPFC CLYSTFLQRG YDQLVHDVAI QNLPVRFAVD 

       430        440        450        460        470        480 
RAGLVGADGA THAGSFDLAF MVNLPNMVVM APSDERELAN MVHSMAHYDQ GPISVRYPRG 

       490        500        510        520        530        540 
NGVGVSLEGE KEILPIGKGR LIRRGKKVAI LSLGTRLEES LKAADRLDAQ GLSTSVADMR 

       550        560        570        580        590        600 
FAKPLDEALT RQLLKSHQVI ITIEEGALGG FATQVLTMAS DEGLMDDGLK IRTLRLPDRF 

       610        620        630        640 
QPQDKQERQY AEAGLDADGI VAAVISALHR NSKPVEVVEM ANMGSIARA 

« Hide

References

[1]"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4."
Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. expand/collapse author list , Kang H.L., Lee S.Y., Lee K.J., Kang H.S.
Nat. Biotechnol. 23:63-68(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008692 Genomic DNA. Translation: AAV89858.1.
RefSeqYP_162969.1. NC_006526.2.

3D structure databases

ProteinModelPortalQ5NN52.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264203.ZMO1234.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV89858; AAV89858; ZMO1234.
GeneID3189041.
KEGGzmo:ZMO1234.
PATRIC32567764. VBIZymMob102260_1170.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1154.
HOGENOMHOG000012988.
KOK01662.
OMAMSTIRQK.
OrthoDBEOG6BKJ6P.

Enzyme and pathway databases

UniPathwayUPA00064; UER00091.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
3.40.50.970. 3 hits.
HAMAPMF_00315. DXP_synth.
InterProIPR005477. Dxylulose-5-P_synthase.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view]
PfamPF13292. DXP_synthase_N. 1 hit.
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 3 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsTIGR00204. dxs. 1 hit.
PROSITEPS00801. TRANSKETOLASE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDXS1_ZYMMO
AccessionPrimary (citable) accession number: Q5NN52
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: February 1, 2005
Last modified: June 11, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways