Q3ZXC2 (DXS_DEHSC) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 57.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended 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 |
| ||||
| Organism | Dehalococcoides sp. (strain CBDB1) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 255470 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Chloroflexi › Dehalococcoidetes › Dehalococcoidales › Dehalococcoidaceae › Dehalococcoides › ![]() |
Protein attributes
| Sequence length | 647 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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. 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. |
| Sequence similarities | Belongs to the transketolase family. DXPS subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Isoprene biosynthesis Thiamine biosynthesis |
| Ligand | Magnesium Metal-binding Thiamine pyrophosphate |
| Molecular function | Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | 1-deoxy-D-xylulose 5-phosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway terpenoid biosynthetic processInferred from electronic annotation. Source: HAMAP thiamine biosynthetic processInferred from electronic annotation. Source: HAMAP |
| Molecular_function | 1-deoxy-D-xylulose-5-phosphate synthase activity Inferred from electronic annotation. Source: HAMAP magnesium ion bindingInferred from electronic annotation. Source: HAMAP thiamine pyrophosphate bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 647 | 647 | 1-deoxy-D-xylulose-5-phosphate synthase HAMAP-Rule MF_00315 | PRO_0000256409 | |||||
Regions | |||||||||
| Region | 129 – 131 | 3 | Thiamine pyrophosphate binding By similarity | ||||||
| Region | 161 – 162 | 2 | Thiamine pyrophosphate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 160 | 1 | Magnesium By similarity | ||||||
| Metal binding | 189 | 1 | Magnesium By similarity | ||||||
| Binding site | 88 | 1 | Thiamine pyrophosphate By similarity | ||||||
| Binding site | 189 | 1 | Thiamine pyrophosphate By similarity | ||||||
| Binding site | 300 | 1 | Thiamine pyrophosphate By similarity | ||||||
| Binding site | 377 | 1 | Thiamine pyrophosphate By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of the chlorinated compound-respiring bacterium Dehalococcoides species strain CBDB1." Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L. Nat. Biotechnol. 23:1269-1273(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CBDB1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ965256 Genomic DNA. Translation: CAI82881.1. |
| RefSeq | YP_307797.1. NC_007356.1. |
3D structure databases | |
| ProteinModelPortal | Q3ZXC2. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 255470.cbdb_A720. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAI82881; CAI82881; cbdbA720. |
| GeneID | 3623188. |
| KEGG | deh:cbdb_A720. |
| PATRIC | 21611541. VBIDehSp125902_0609. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1154. |
| KO | K01662. |
| OMA | PVAYHGP. |
| ProtClustDB | PRK05444. |
Enzyme and pathway databases | |
| BioCyc | DSP255470:GJXW-617-MONOMER. |
| UniPathway | UPA00064; UER00091. |
Family and domain databases | |
| Gene3D | 3.40.50.920. 1 hit. |
| HAMAP | MF_00315. DXP_synth. |
| InterPro | IPR005477. Dxylulose-5-P_synthase. IPR009014. Transketo_C/Pyr-ferredox_oxred. IPR015941. Transketolase-like_C. IPR005475. Transketolase-like_Pyr-bd. IPR005476. Transketolase_C. IPR005474. Transketolase_N. [Graphical view] |
| Pfam | PF13292. DXP_synthase_N. 1 hit. PF02779. Transket_pyr. 1 hit. PF02780. Transketolase_C. 1 hit. [Graphical view] |
| SMART | SM00861. Transket_pyr. 1 hit. [Graphical view] |
| SUPFAM | SSF52922. Transketo_C_like. 1 hit. |
| TIGRFAMs | TIGR00204. dxs. 1 hit. |
| PROSITE | PS00801. TRANSKETOLASE_1. 1 hit. PS00802. TRANSKETOLASE_2. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DXS_DEHSC | ||||||||
| Accession | Primary (citable) accession number: Q3ZXC2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
