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O25121 (DXS_HELPY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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:HP_0354
OrganismHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]
Taxonomic identifier85962 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length618 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 – 6186181-deoxy-D-xylulose-5-phosphate synthase HAMAP-Rule MF_00315
PRO_0000189119

Regions

Region111 – 1133Thiamine pyrophosphate binding By similarity
Region143 – 1442Thiamine pyrophosphate binding By similarity

Sites

Metal binding1421Magnesium By similarity
Metal binding1711Magnesium By similarity
Binding site701Thiamine pyrophosphate By similarity
Binding site1711Thiamine pyrophosphate By similarity
Binding site2781Thiamine pyrophosphate By similarity
Binding site3601Thiamine pyrophosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
O25121 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 87334832DAFE3383

FASTA61867,634
        10         20         30         40         50         60 
MILQNKTFDL NPNDIAGLEL VCQTLRNRIL EVVSANGGHL SSSLGAVELI VGMHALFDCQ 

        70         80         90        100        110        120 
KNPFIFDTSH QAYAHKLLTG RFESFSTLRQ FKGLSGFTKP SESAYDYFIA GHSSTSVSIG 

       130        140        150        160        170        180 
VGVAKAFCLK QALGMPIALL GDGSISAGIF YEALNELGDR KYPMIMILND NEMSISTPIG 

       190        200        210        220        230        240 
ALSKALSQLM KGPFYQSFRS KVKKILSTLP ESVNYLASRF EESFKLITPG VFFEELGINY 

       250        260        270        280        290        300 
IGPINGHDLS AIIETLKLAK ELKEPVLIHA QTLKGKGYKI AEGRYEKWHG VGPFDLDTGL 

       310        320        330        340        350        360 
SKKSKSAILS PTEAYSNTLL ELAKKDEKIV GVTAAMPSGT GLDKLIDAYP LRFFDVAIAE 

       370        380        390        400        410        420 
QHALTSSSAM AKEGFKPFVS IYSTFLQRAY DSIVHDACIS SLPIKLAIDR AGIVGEDGET 

       430        440        450        460        470        480 
HQGLLDVSYL RSIPNMVIFA PRDNETLKNA VRFANEHDSS PCAFRYPRGS FALKEGVFEP 

       490        500        510        520        530        540 
SGFVLGQSEL LKKEGEILLI GYGNGVGRAH LVQLALKEKN IECALLDLRF LKPLDPNLSA 

       550        560        570        580        590        600 
IVAPYQKLYV FSDNYKLGGV ASAILEFLSE QNILKPVKSF EIIDEFIMHG NTALVEKSLG 

       610 
LDTESLTDAI LKDLGQER 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000511 Genomic DNA. Translation: AAD07422.1.
PIRB64564.
RefSeqNP_207152.1. NC_000915.1.

3D structure databases

ProteinModelPortalO25121.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-3091N.
IntActO25121. 4 interactions.
MINTMINT-163092.
STRING85962.HP0354.

PTM databases

PhosSiteP11041029.

Proteomic databases

PRIDEO25121.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD07422; AAD07422; HP_0354.
GeneID898853.
KEGGhpy:HP0354.
PATRIC20591941. VBIHelPyl33062_0367.

Phylogenomic databases

eggNOGCOG1154.
KOK01662.
OMATGKQFKS.
OrthoDBEOG6BKJ6P.
ProtClustDBPRK05444.

Enzyme and pathway databases

BioCycHPY:HP0354-MONOMER.
UniPathwayUPA00064; UER00091.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
HAMAPMF_00315. DXP_synth.
InterProIPR005477. Dxylulose-5-P_synthase.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
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]
SUPFAMSSF52922. SSF52922. 1 hit.
TIGRFAMsTIGR00204. dxs. 1 hit.
PROSITEPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDXS_HELPY
AccessionPrimary (citable) accession number: O25121
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 96 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

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names