Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8G292 (DXS_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 71. 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
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:BS1330_I0437, BR0436
OrganismBrucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]
Taxonomic identifier204722 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella ›

Protein attributes

Sequence length643 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 – 6436431-deoxy-D-xylulose-5-phosphate synthase HAMAP-Rule MF_00315
PRO_0000189093

Regions

Region119 – 1213Thiamine pyrophosphate binding By similarity
Region151 – 1522Thiamine pyrophosphate binding By similarity

Sites

Metal binding1501Magnesium By similarity
Metal binding1791Magnesium By similarity
Binding site781Thiamine pyrophosphate By similarity
Binding site1791Thiamine pyrophosphate By similarity
Binding site2881Thiamine pyrophosphate By similarity
Binding site3701Thiamine pyrophosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8G292 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E42DFB422D129FEA

FASTA64369,180
        10         20         30         40         50         60 
MSRPSTPLLD KAPTPDRLRA LPEQDLPQLA EELRTELIDA VSTTGGHLGA GLGVVELTVA 

        70         80         90        100        110        120 
LHHVFNTPYD RIIWDVGHQA YPHKILTGRR DRIRTLRQAG GLSGFTKRAE SEYDPFGAAH 

       130        140        150        160        170        180 
SSTSISAGLG MAVASELSGE KRNVIAVIGD GSMSAGMAYE AMNNAGALDA RLIVILNDND 

       190        200        210        220        230        240 
MSIAPPTGAM SAYLARLVSG RTYRSVREAA KQVAQKLPKF LQDKARKSEE YARAFFTGGT 

       250        260        270        280        290        300 
LFEELGFYYV GPIDGHNLDH LLPVLKNVRD TQKGPVLIHV VTQKGKGYAP AEAAADKYHG 

       310        320        330        340        350        360 
VNKFDVITGK QAKPPANVPS YTKIFGTSLI EEARHDDKIV AVTAAMPTGT GLDLFGEAFP 

       370        380        390        400        410        420 
KRVFDVGIAE QHAVTFAAGL ASEGYKPFCA IYSTFLQRGY DQVVHDVSIQ NLPVRFPIDR 

       430        440        450        460        470        480 
AGLVGADGPT HAGSFDTGFL AALPGFVVMA ASDEAELRHM VRTAAEYDEG PISFRYPRGD 

       490        500        510        520        530        540 
GVGVDLPERG SVLEIGKGRI VREGTKVALL SFGTRLQECL AAAEELGAAG LSTTVADARF 

       550        560        570        580        590        600 
AKPLDHDLIR RLAREHEVLV MVEEGAVGGF GSHVLQFLAT DGLLDRGLKV RALTLPDIYQ 

       610        620        630        640 
DHGKPDAMYA EAGLDRTGIV RTVFAALHRD ELGHEALPTP FRA

« Hide

References

[1]"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts."
Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. expand/collapse author list , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.
[2]"Revised genome sequence of Brucella suis 1330."
Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.
J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014291 Genomic DNA. Translation: AAN29379.1.
CP002997 Genomic DNA. Translation: AEM17792.1.
RefSeqNP_697464.1. NC_004310.3.
YP_005615284.1. NC_017251.1.

3D structure databases

ProteinModelPortalQ8G292.
ModBaseSearch...

Protein-protein interaction databases

STRING204722.BR0436.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN29379; AAN29379; BR0436.
AEM17792; AEM17792; BS1330_I0437.
GeneID1166097.
12136756.
KEGGbms:BR0436.
bsi:BS1330_I0437.
PATRIC17789166. VBIBruSui107850_0451.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1154.
HOGENOMHOG000012988.
KOK01662.
OMAGDIKPDM.
ProtClustDBPRK05444.

Enzyme and pathway databases

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.
IPR015941. Transketolase-like_C.
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. 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_BRUSU
AccessionPrimary (citable) accession number: Q8G292
Secondary accession number(s): G0K6Q5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: March 1, 2003
Last modified: May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Brucella suis

Brucella suis (strain 1330): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents