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D7BG48 (D7BG48_MEISD) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | 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 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
Ordered Locus Names:Mesil_0021
OrganismMeiothermus silvanus (strain ATCC 700542 / DSM 9946 / VI-R2) (Thermus silvanus) [Complete proteome] [HAMAP]
Taxonomic identifier526227 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Meiothermus ›

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 SAAS005476

Catalytic activity

Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO2. HAMAP-Rule MF_00315 SAAS SAAS005476

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_00315 SAAS SAAS005476

Binds 1 thiamine pyrophosphate per subunit By similarity. HAMAP-Rule MF_00315 SAAS SAAS005476

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 SAAS005476

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00315 SAAS SAAS005476

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region113 – 1153Thiamine pyrophosphate binding By similarity HAMAP-Rule MF_00315
Region145 – 1462Thiamine pyrophosphate binding By similarity HAMAP-Rule MF_00315

Sites

Metal binding1441Magnesium By similarity HAMAP-Rule MF_00315
Metal binding1731Magnesium By similarity HAMAP-Rule MF_00315
Binding site721Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315
Binding site1731Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315
Binding site2811Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315
Binding site3601Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315

Sequences

Sequence LengthMass (Da)Tools
D7BG48 [UniParc].

Last modified August 10, 2010. Version 1.
Checksum: BCFA8F3509E6BF91

FASTA62168,326
        10         20         30         40         50         60 
MVLDKVNSPR DLKTLSEEEL LTLAQELRSE IIRVCGQNGG HLASSLGAVE LIVALHRVFD 

        70         80         90        100        110        120 
SPKDRLLFDV GHQAYAHKIL TGRKDVFHTI RQEGGISGFT KVSESPHDAI TAGHASTSLA 

       130        140        150        160        170        180 
NALGMAIARD ALREDYQIVS VIGDGALTGG MALAALNVIG EQRRKLLIIL NDNEMSISEN 

       190        200        210        220        230        240 
VGALNRYFKE FQIKKWVQDT QKWGRDVLEH ISPRLFNLVD RAKEAAKLML HQENPFYAWG 

       250        260        270        280        290        300 
VRYVGPVDGH DLKGLIHLFQ ELKELDGPTI LHVVTQKGKG YSVAEADPIY WHGPPGFNPE 

       310        320        330        340        350        360 
KPEKVSKGYS WSAAFGDAVT ELAYQEPRLF VITPAMREGS GLVRYSQTHP TRYLDTGICE 

       370        380        390        400        410        420 
DVAATAAAGM ALRGLKPVLA IYSTFMQRAY DQIIHDIAIE NLDVIFAVDR AGIVGGDGAT 

       430        440        450        460        470        480 
HNGVFDIAYL RTIPNVQIAA PKDALELRAM LKKALERGGP VAIRYPRDNV EKAPEGAWPE 

       490        500        510        520        530        540 
IEWGRWEVLK EGSTAYILSF GKTLRYALEA AGENPEIGVI NARFIKPLDR EMLERLALEG 

       550        560        570        580        590        600 
YKLVTAEDHQ RMGGFGSAVL EALSELGLKP DIRVLGLPDR FFDHGSIARM HKEAGIDAEA 

       610        620 
ILKALAEMGV VSKPPALDSK R

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002042 Genomic DNA. Translation: ADH61969.1.
RefSeqYP_003683477.1. NC_014212.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADH61969; ADH61969; Mesil_0021.
GeneID9249497.
KEGGmsv:Mesil_0021.
PATRIC38188696. VBIMeiSil18825_0021.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000012988.
KOK01662.
OMAPHDLVEN.

Enzyme and pathway databases

BioCycMSIL526227:GJ9Q-22-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.
IPR015941. Transketolase-like_C.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR005476. Transketolase_C.
[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.
PROSITEPS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD7BG48_MEISD
AccessionPrimary (citable) accession number: D7BG48
Entry history
Integrated into UniProtKB/TrEMBL: August 10, 2010
Last sequence update: August 10, 2010
Last modified: May 1, 2013
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info