Q8G292 (DXS_BRUSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 59.
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 | Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 204722 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella |
Protein attributes
| Sequence length | 643 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 oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptorInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 643 | 643 | 1-deoxy-D-xylulose-5-phosphate synthase HAMAP MF_00315 | PRO_0000189093 | |||
Sequences
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References
| [1] | "The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. Fraser C.M.Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed: 12271122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330. |
| [2] | "Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed: 22038969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014291 Genomic DNA. Translation: AAN29379.1. CP002997 Genomic DNA. Translation: AEM17792.1. |
| RefSeq | NP_697464.1. NC_004310.3. |
3D structure databases | |
| ProteinModelPortal | Q8G292. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1166097. |
| GenomeReviews | Gene locus BR0436 in contig AE014291_GR. |
| KEGG | bms:BR0436. |
| NMPDR | fig|204722.1.peg.421. |
| PATRIC | 17789166. VBIBruSui107850_0451. |
| TIGR | BR0436. |
Phylogenomic databases | |
| HOGENOM | HBG571647. |
| OMA | DPILYHG. |
| PhylomeDB | Q8G292. |
| ProtClustDB | PRK05444. |
Enzyme and pathway databases | |
| BioCyc | BSUI204722:BR_0436-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00315. DXP_synth. [Tree] |
| InterPro | IPR001017. DH_E1. 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 | PF00676. E1_dh. 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. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DXS_BRUSU | ||||||||
| Accession | Primary (citable) accession number: Q8G292 Secondary accession number(s): G0K6Q5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Brucella suis Brucella suis (strain 1330): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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