Q65HJ2 (DXS_BACLD) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 54.
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 | Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 279010 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 633 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 MF_00315 |
| Catalytic activity | Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO2. HAMAP MF_00315 |
| Cofactor | 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 MF_00315 |
| Subunit structure | Homodimer By similarity. HAMAP MF_00315 |
| Sequence similarities | Belongs to the transketolase family. DXPS subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Isoprene biosynthesis Thiamine biosynthesis |
| Ligand | Thiamine pyrophosphate |
| Molecular function | Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | terpenoid biosynthetic process Inferred from electronic annotation. Source: InterPro thiamine biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 1-deoxy-D-xylulose-5-phosphate synthase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 633 | 633 | 1-deoxy-D-xylulose-5-phosphate synthase HAMAP MF_00315 | PRO_0000256378 | |||
Sequences
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References
| [1] | "The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580. |
| [2] | "Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. Berka R.M.Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017333 Genomic DNA. Translation: AAU41472.1. CP000002 Genomic DNA. Translation: AAU24113.2. |
| RefSeq | YP_079751.2. NC_006270.3. YP_092165.1. NC_006322.1. |
3D structure databases | |
| ProteinModelPortal | Q65HJ2. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q65HJ2. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000055534; EBBACP00000054065; EBBACG00000055525. EBBACT00000058504; EBBACP00000056937; EBBACG00000058495. |
| GeneID | 3029280. 3099865. |
| GenomeReviews | Gene locus BLi02598 in contig AE017333_GR. Gene locus BL01523 in contig CP000002_GR. |
| KEGG | bld:BLi02598. bli:BL01523. |
| NMPDR | fig|279010.5.peg.441. |
| PATRIC | 18950870. VBIBacLic203714_2637. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1154. |
| GeneTree | EBGT00070000031844. |
| HOGENOM | HBG571647. |
| ProtClustDB | PRK05444. |
Enzyme and pathway databases | |
| BioCyc | BLIC279010-1:BLI02598-MONOMER. BLIC279010:BL01523-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00315. DXP_synth. [Tree] |
| 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. [Graphical view] |
| Gene3D | G3DSA:3.40.50.920. Transketo_C_like. 1 hit. |
| KO | K01662. |
| Pfam | 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. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DXS_BACLD | ||||||||
| Accession | Primary (citable) accession number: Q65HJ2 Secondary accession number(s): Q62SZ6 | ||||||||
| 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 |

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