Q81M54 (DXS_BACAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 66.
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 anthracis | ||||
| Taxonomic identifier | 1392 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 630 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 Reference 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 thiamine pyrophosphate bindingInferred 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 – 630 | 630 | 1-deoxy-D-xylulose-5-phosphate synthase HAMAP MF_00315 | PRO_0000189083 | |||
Sequences
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References
| [1] | "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. Fraser C.M.Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton. |
| [2] | "Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor. |
| [3] | "Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016879 Genomic DNA. Translation: AAP28115.1. AE017334 Genomic DNA. Translation: AAT33519.1. AE017225 Genomic DNA. Translation: AAT56382.1. |
| RefSeq | NP_846629.1. NC_003997.3. YP_021044.1. NC_007530.2. YP_030331.1. NC_005945.1. |
3D structure databases | |
| ProteinModelPortal | Q81M54. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000011092; EBBACP00000010848; EBBACG00000011084. EBBACT00000016687; EBBACP00000016308; EBBACG00000016678. EBBACT00000023815; EBBACP00000023300; EBBACG00000023806. |
| GeneID | 1087729. 2819989. 2852469. |
| GenomeReviews | Gene locus BA_4400 in contig AE016879_GR. Gene locus BAS4081 in contig AE017225_GR. Gene locus GBAA_4400 in contig AE017334_GR. |
| KEGG | ban:BA_4400. bar:GBAA_4400. bat:BAS4081. |
| TIGR | BA_4400. GBAA_4400. |
Phylogenomic databases | |
| GeneTree | EBGT00070000031844. |
| HOGENOM | HBG571647. |
| OMA | RFANEHD. |
| ProtClustDB | PRK05444. |
Enzyme and pathway databases | |
| BioCyc | BANT260799:BAS4081-MONOMER. BANT261594:GBAA4400-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00315. DXP_synth. [Tree] |
| InterPro | IPR005477. Dxylulose-5-P_synthase. IPR011766. TPP_enzyme-bd_C. 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 | PF02775. TPP_enzyme_C. 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_BACAN | ||||||||
| Accession | Primary (citable) accession number: Q81M54 Secondary accession number(s): Q6HTK7, Q6KMU7 | ||||||||
| 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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