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UniProtKB - P77488 (DXS_ECOLI)
Protein
1-deoxy-D-xylulose-5-phosphate synthase
Gene
dxs
Organism
Escherichia coli (strain K12)
Status
Functioni
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).
3 PublicationsCatalytic activityi
Cofactori
Protein has several cofactor binding sites:- Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication
- thiamine diphosphate2 PublicationsNote: Binds 1 thiamine pyrophosphate per subunit.1 Publication
pH dependencei
Optimum pH is 7.5-8.0.
Temperature dependencei
Optimum temperature is 42-44 degrees Celsius.
: 1-deoxy-D-xylulose 5-phosphate biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate. This subpathway is part of the pathway 1-deoxy-D-xylulose 5-phosphate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.View all proteins of this organism that are known to be involved in the subpathway that synthesizes 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate, the pathway 1-deoxy-D-xylulose 5-phosphate biosynthesis and in Metabolic intermediate biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 80 | Thiamine pyrophosphate1 Publication | 1 | |
Metal bindingi | 152 | Magnesium1 Publication | 1 | |
Metal bindingi | 181 | Magnesium1 Publication | 1 | |
Binding sitei | 181 | Thiamine pyrophosphate1 Publication | 1 | |
Binding sitei | 288 | Thiamine pyrophosphate1 Publication | 1 | |
Binding sitei | 370 | Thiamine pyrophosphate1 Publication | 1 |
GO - Molecular functioni
- 1-deoxy-D-xylulose-5-phosphate synthase activity Source: EcoCyc
- magnesium ion binding Source: UniProtKB-UniRule
- thiamine pyrophosphate binding Source: EcoCyc
- transketolase or transaldolase activity Source: GO_Central
GO - Biological processi
- 1-deoxy-D-xylulose 5-phosphate biosynthetic process Source: UniProtKB-UniPathway
- isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway Source: EcoCyc
- isoprenoid biosynthetic process Source: EcoCyc
- pyridoxine biosynthetic process Source: EcoCyc
- terpenoid biosynthetic process Source: UniProtKB-UniRule
- thiamine biosynthetic process Source: EcoCyc
- ubiquinone biosynthetic process Source: EcoCyc
Keywordsi
Molecular function | Transferase |
Biological process | Isoprene biosynthesis, Thiamine biosynthesis |
Ligand | Magnesium, Metal-binding, Thiamine pyrophosphate |
Enzyme and pathway databases
BioCyci | EcoCyc:DXS-MONOMER |
BRENDAi | 2.2.1.7, 2026 |
SABIO-RKi | P77488 |
UniPathwayi | UPA00064;UER00091 |
Names & Taxonomyi
Protein namesi | Recommended name: 1-deoxy-D-xylulose-5-phosphate synthase1 Publication1 Publication (EC:2.2.1.72 Publications)Alternative name(s): 1-deoxyxylulose-5-phosphate synthase1 Publication Short name: DXP synthase1 Publication Short name: DXPS |
Gene namesi | Name:dxs1 Publication Synonyms:yajP Ordered Locus Names:b0420, JW0410 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 370 | E → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 392 | Y → A: Slightly increases activity. 1 Publication | 1 | |
Mutagenesisi | 392 | Y → F: Increases activity 3-fold. 1 Publication | 1 | |
Mutagenesisi | 398 | R → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 431 | H → A: No effect on activity. 1 Publication | 1 | |
Mutagenesisi | 478 | R → A: Loss of activity. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL3217381 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000189111 | 2 – 620 | 1-deoxy-D-xylulose-5-phosphate synthaseAdd BLAST | 619 |
Proteomic databases
jPOSTi | P77488 |
PaxDbi | P77488 |
PRIDEi | P77488 |
Interactioni
Subunit structurei
Homodimer.
1 PublicationProtein-protein interaction databases
BioGRIDi | 4259592, 367 interactors |
DIPi | DIP-9485N |
IntActi | P77488, 19 interactors |
MINTi | P77488 |
STRINGi | 511145.b0420 |
Chemistry databases
BindingDBi | P77488 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P77488 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P77488 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 121 – 123 | Thiamine pyrophosphate binding | 3 | |
Regioni | 153 – 154 | Thiamine pyrophosphate binding | 2 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG1154, Bacteria |
HOGENOMi | CLU_009227_1_4_6 |
InParanoidi | P77488 |
PhylomeDBi | P77488 |
Family and domain databases
CDDi | cd02007, TPP_DXS, 1 hit |
Gene3Di | 3.40.50.920, 1 hit |
HAMAPi | MF_00315, DXP_synth, 1 hit |
InterProi | View protein in InterPro IPR005477, Dxylulose-5-P_synthase IPR029061, THDP-binding IPR009014, Transketo_C/PFOR_II IPR005475, Transketolase-like_Pyr-bd IPR020826, Transketolase_BS IPR033248, Transketolase_C IPR005474, Transketolase_N |
PANTHERi | PTHR43322, PTHR43322, 1 hit |
Pfami | View protein in Pfam PF13292, DXP_synthase_N, 1 hit PF02779, Transket_pyr, 1 hit PF02780, Transketolase_C, 1 hit |
SMARTi | View protein in SMART SM00861, Transket_pyr, 1 hit |
SUPFAMi | SSF52518, SSF52518, 2 hits SSF52922, SSF52922, 1 hit |
TIGRFAMsi | TIGR00204, dxs, 1 hit |
PROSITEi | View protein in PROSITE PS00801, TRANSKETOLASE_1, 1 hit PS00802, TRANSKETOLASE_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P77488-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSFDIAKYPT LALVDSTQEL RLLPKESLPK LCDELRRYLL DSVSRSSGHF
60 70 80 90 100
ASGLGTVELT VALHYVYNTP FDQLIWDVGH QAYPHKILTG RRDKIGTIRQ
110 120 130 140 150
KGGLHPFPWR GESEYDVLSV GHSSTSISAG IGIAVAAEKE GKNRRTVCVI
160 170 180 190 200
GDGAITAGMA FEAMNHAGDI RPDMLVILND NEMSISENVG ALNNHLAQLL
210 220 230 240 250
SGKLYSSLRE GGKKVFSGVP PIKELLKRTE EHIKGMVVPG TLFEELGFNY
260 270 280 290 300
IGPVDGHDVL GLITTLKNMR DLKGPQFLHI MTKKGRGYEP AEKDPITFHA
310 320 330 340 350
VPKFDPSSGC LPKSSGGLPS YSKIFGDWLC ETAAKDNKLM AITPAMREGS
360 370 380 390 400
GMVEFSRKFP DRYFDVAIAE QHAVTFAAGL AIGGYKPIVA IYSTFLQRAY
410 420 430 440 450
DQVLHDVAIQ KLPVLFAIDR AGIVGADGQT HQGAFDLSYL RCIPEMVIMT
460 470 480 490 500
PSDENECRQM LYTGYHYNDG PSAVRYPRGN AVGVELTPLE KLPIGKGIVK
510 520 530 540 550
RRGEKLAILN FGTLMPEAAK VAESLNATLV DMRFVKPLDE ALILEMAASH
560 570 580 590 600
EALVTVEENA IMGGAGSGVN EVLMAHRKPV PVLNIGLPDF FIPQGTQEEM
610 620
RAELGLDAAG MEAKIKAWLA
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF035440 Genomic DNA Translation: AAC46162.1 U82664 Genomic DNA Translation: AAB40176.1 U00096 Genomic DNA Translation: AAC73523.1 AP009048 Genomic DNA Translation: BAE76200.1 |
PIRi | D64771 |
RefSeqi | NP_414954.1, NC_000913.3 WP_000006797.1, NZ_SSZK01000009.1 |
Genome annotation databases
EnsemblBacteriai | AAC73523; AAC73523; b0420 BAE76200; BAE76200; BAE76200 |
GeneIDi | 945060 |
KEGGi | ecj:JW0410 eco:b0420 |
PATRICi | fig|1411691.4.peg.1857 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF035440 Genomic DNA Translation: AAC46162.1 U82664 Genomic DNA Translation: AAB40176.1 U00096 Genomic DNA Translation: AAC73523.1 AP009048 Genomic DNA Translation: BAE76200.1 |
PIRi | D64771 |
RefSeqi | NP_414954.1, NC_000913.3 WP_000006797.1, NZ_SSZK01000009.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2O1S | X-ray | 2.40 | A/B/C/D | 1-620 | [»] | |
SMRi | P77488 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4259592, 367 interactors |
DIPi | DIP-9485N |
IntActi | P77488, 19 interactors |
MINTi | P77488 |
STRINGi | 511145.b0420 |
Chemistry databases
BindingDBi | P77488 |
ChEMBLi | CHEMBL3217381 |
Proteomic databases
jPOSTi | P77488 |
PaxDbi | P77488 |
PRIDEi | P77488 |
Genome annotation databases
EnsemblBacteriai | AAC73523; AAC73523; b0420 BAE76200; BAE76200; BAE76200 |
GeneIDi | 945060 |
KEGGi | ecj:JW0410 eco:b0420 |
PATRICi | fig|1411691.4.peg.1857 |
Organism-specific databases
EchoBASEi | EB3378 |
Phylogenomic databases
eggNOGi | COG1154, Bacteria |
HOGENOMi | CLU_009227_1_4_6 |
InParanoidi | P77488 |
PhylomeDBi | P77488 |
Enzyme and pathway databases
UniPathwayi | UPA00064;UER00091 |
BioCyci | EcoCyc:DXS-MONOMER |
BRENDAi | 2.2.1.7, 2026 |
SABIO-RKi | P77488 |
Miscellaneous databases
EvolutionaryTracei | P77488 |
PROi | PR:P77488 |
Family and domain databases
CDDi | cd02007, TPP_DXS, 1 hit |
Gene3Di | 3.40.50.920, 1 hit |
HAMAPi | MF_00315, DXP_synth, 1 hit |
InterProi | View protein in InterPro IPR005477, Dxylulose-5-P_synthase IPR029061, THDP-binding IPR009014, Transketo_C/PFOR_II IPR005475, Transketolase-like_Pyr-bd IPR020826, Transketolase_BS IPR033248, Transketolase_C IPR005474, Transketolase_N |
PANTHERi | PTHR43322, PTHR43322, 1 hit |
Pfami | View protein in Pfam PF13292, DXP_synthase_N, 1 hit PF02779, Transket_pyr, 1 hit PF02780, Transketolase_C, 1 hit |
SMARTi | View protein in SMART SM00861, Transket_pyr, 1 hit |
SUPFAMi | SSF52518, SSF52518, 2 hits SSF52922, SSF52922, 1 hit |
TIGRFAMsi | TIGR00204, dxs, 1 hit |
PROSITEi | View protein in PROSITE PS00801, TRANSKETOLASE_1, 1 hit PS00802, TRANSKETOLASE_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | DXS_ECOLI | |
Accessioni | P77488Primary (citable) accession number: P77488 Secondary accession number(s): Q2MC06 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 181 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families