CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010326
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 1-deoxy-D-xylulose-5-phosphate synthase 
Protein Synonyms/Alias
 1-deoxyxylulose-5-phosphate synthase; DXP synthase; DXPS 
Gene Name
 dxs 
Gene Synonyms/Alias
 yajP; b0420; JW0410 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
25QELRLLPKESLPKLCacetylation[1]
30LPKESLPKLCDELRRacetylation[1]
223FSGVPPIKELLKRTEacetylation[1]
283QFLHIMTKKGRGYEPacetylation[1]
293RGYEPAEKDPITFHAacetylation[1]
335WLCETAAKDNKLMAIacetylation[1]
338ETAAKDNKLMAITPAacetylation[1]
411LHDVAIQKLPVLFAIacetylation[1]
491VELTPLEKLPIGKGIacetylation[1, 2]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 
Functional Description
 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). 
Sequence Annotation
 REGION 121 123 Thiamine pyrophosphate binding.
 REGION 153 154 Thiamine pyrophosphate binding.
 METAL 152 152 Magnesium.
 METAL 181 181 Magnesium.
 BINDING 80 80 Thiamine pyrophosphate.
 BINDING 181 181 Thiamine pyrophosphate.
 BINDING 288 288 Thiamine pyrophosphate.
 BINDING 370 370 Thiamine pyrophosphate.  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; Isoprene biosynthesis; Magnesium; Metal-binding; Reference proteome; Thiamine biosynthesis; Thiamine pyrophosphate; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 620 AA 
Protein Sequence
MSFDIAKYPT LALVDSTQEL RLLPKESLPK LCDELRRYLL DSVSRSSGHF ASGLGTVELT 60
VALHYVYNTP FDQLIWDVGH QAYPHKILTG RRDKIGTIRQ KGGLHPFPWR GESEYDVLSV 120
GHSSTSISAG IGIAVAAEKE GKNRRTVCVI GDGAITAGMA FEAMNHAGDI RPDMLVILND 180
NEMSISENVG ALNNHLAQLL SGKLYSSLRE GGKKVFSGVP PIKELLKRTE EHIKGMVVPG 240
TLFEELGFNY IGPVDGHDVL GLITTLKNMR DLKGPQFLHI MTKKGRGYEP AEKDPITFHA 300
VPKFDPSSGC LPKSSGGLPS YSKIFGDWLC ETAAKDNKLM AITPAMREGS GMVEFSRKFP 360
DRYFDVAIAE QHAVTFAAGL AIGGYKPIVA IYSTFLQRAY DQVLHDVAIQ KLPVLFAIDR 420
AGIVGADGQT HQGAFDLSYL RCIPEMVIMT PSDENECRQM LYTGYHYNDG PSAVRYPRGN 480
AVGVELTPLE KLPIGKGIVK RRGEKLAILN FGTLMPEAAK VAESLNATLV DMRFVKPLDE 540
ALILEMAASH EALVTVEENA IMGGAGSGVN EVLMAHRKPV PVLNIGLPDF FIPQGTQEEM 600
RAELGLDAAG MEAKIKAWLA 620 
Gene Ontology
 GO:0005829; C:cytosol; IDA:EcoCyc.
 GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IDA:EcoCyc.
 GO:0000287; F:magnesium ion binding; IEA:HAMAP.
 GO:0030976; F:thiamine pyrophosphate binding; IDA:EcoCyc.
 GO:0052865; P:1-deoxy-D-xylulose 5-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0008615; P:pyridoxine biosynthetic process; IDA:EcoCyc.
 GO:0016114; P:terpenoid biosynthetic process; IEA:HAMAP.
 GO:0009228; P:thiamine biosynthetic process; IMP:EcoCyc.
 GO:0006744; P:ubiquinone biosynthetic process; IDA:EcoCyc. 
Interpro
 IPR005477; 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. 
Pfam
 PF13292; DXP_synthase_N
 PF02779; Transket_pyr
 PF02780; Transketolase_C 
SMART
 SM00861; Transket_pyr 
PROSITE
 PS00801; TRANSKETOLASE_1
 PS00802; TRANSKETOLASE_2 
PRINTS