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C9XNT4 (C9XNT4_CLODC) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 31. Feed History...

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

Names and origin

Protein namesRecommended name:
1-deoxy-D-xylulose-5-phosphate synthase HAMAP-Rule MF_00315

EC=2.2.1.7 HAMAP-Rule MF_00315
Alternative name(s):
1-deoxyxylulose-5-phosphate synthase HAMAP-Rule MF_00315
Gene names
Name:dxs HAMAP-Rule MF_00315 EMBL CBA62029.1
Ordered Locus Names:CD196_1067 EMBL CBA62029.1
OrganismClostridium difficile (strain CD196) [Complete proteome] [HAMAP] EMBL CBA62029.1
Taxonomic identifier645462 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptostreptococcaceae

Protein attributes

Sequence length621 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 SAAS SAAS005477

Catalytic activity

Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO2. HAMAP-Rule MF_00315 SAAS SAAS005477

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_00315 SAAS SAAS005477

Binds 1 thiamine pyrophosphate per subunit By similarity. HAMAP-Rule MF_00315 SAAS SAAS005477

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 SAAS SAAS005477

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00315 SAAS SAAS005477

Sequence similarities

Belongs to the transketolase family. DXPS subfamily. HAMAP-Rule MF_00315

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region115 – 1173Thiamine pyrophosphate binding By similarity HAMAP-Rule MF_00315
Region147 – 1482Thiamine pyrophosphate binding By similarity HAMAP-Rule MF_00315

Sites

Metal binding1461Magnesium By similarity HAMAP-Rule MF_00315
Metal binding1751Magnesium By similarity HAMAP-Rule MF_00315
Binding site741Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315
Binding site1751Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315
Binding site2871Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315
Binding site3661Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315

Sequences

Sequence LengthMass (Da)Tools
C9XNT4 [UniParc].

Last modified November 24, 2009. Version 1.
Checksum: B99CF096BFC9762F

FASTA62168,970
        10         20         30         40         50         60 
MYKYLDKVNS PKDIKNMSIE EMDLLAKDIR KFLVKSVSKT GGHLASNLGV VELTLALHKV 

        70         80         90        100        110        120 
FDSPKDKIVW DVGHQSYVHK IVTGRKDCFV SLRQFNGLSG FPKENESPHD IFDTGHSSTS 

       130        140        150        160        170        180 
ISIATGIACA RDIKKENYSV ISVIGDGSIT GGMALEALNQ LGYIDTNMIV ILNDNEMSID 

       190        200        210        220        230        240 
KNVGGMSKYL SSIIRNSTVE KMTDEVDKIL NVTQTGEILS KTAHRFKDKL MYSFSPQDCS 

       250        260        270        280        290        300 
FFDSLGIRYY GPIDGHNTKE LIDILRKAKH KKGPVLLHVI TKKGKGYRFA EEQPDKYHGV 

       310        320        330        340        350        360 
SKFDIKTGVT SAKVKSMSIS VGEKLVDMAN NNEDIVAITA AMPSGTGLNL FESAYPKRYY 

       370        380        390        400        410        420 
DVGIAEQHAT GFAAGLAKNG MKPYFAVYSS FLQRAYDQVI HDVCITKKPV TFLIDRAGLV 

       430        440        450        460        470        480 
GNDGETHHGM FDLSYLNSIP NIVVMAPKDT REMELMMDLS LKLDCPLAIR YPRGSSYYLD 

       490        500        510        520        530        540 
KGEYGEIVLG KYEVLDDGQD TVILCIGSMV KHALEAKEIL SREGINPTIV NARFLKPIDE 

       550        560        570        580        590        600 
GMLKALLKNH KNVVTIEDNI VTGGFGSRIN KFIIDNEYNV NILNIAIPEE FVKHGNIDEL 

       610        620 
YDFVGLSPKS IADKIRKLVI E 

« Hide

References

[1]"Comparative genome and phenotypic analysis of Clostridium difficile 027 strains provides insight into the evolution of a hypervirulent bacterium."
Stabler R.A., He M., Dawson L., Martin M., Valiente E., Corton C., Lawley T.D., Sebaihia M., Quail M.A., Rose G., Gerding D.N., Gibert M., Popoff M.R., Parkhill J., Dougan G., Wren B.W.
Genome Biol. 10:R102.1-R102.15(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CD196 EMBL CBA62029.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FN538970 Genomic DNA. Translation: CBA62029.1.
RefSeqYP_003214098.1. NC_013315.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING645462.CD196_1067.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCBA62029; CBA62029; CD196_1067.
GeneID8463984.
KEGGcdc:CD196_1067.
PATRIC19448384. VBICloDif125228_1108.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1154.
HOGENOMHOG000012987.
KOK01662.
OMAAINHAGH.
OrthoDBEOG6BKJ6P.

Enzyme and pathway databases

BioCycCDIF645462:GJED-1153-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 nameC9XNT4_CLODC
AccessionPrimary (citable) accession number: C9XNT4
Entry history
Integrated into UniProtKB/TrEMBL: November 24, 2009
Last sequence update: November 24, 2009
Last modified: February 19, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)