P04990 (THRC_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 101.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Threonine synthase Short name=TS EC=4.2.3.1 | ||||
| Gene names |
| ||||
| Organism | Bacillus subtilis (strain 168) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 224308 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›  |
Protein attributes
| Sequence length | 352 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine By similarity. |
| Catalytic activity | O-phospho-L-homoserine + H2O = L-threonine + phosphate. |
| Cofactor | Pyridoxal phosphate By similarity. |
| Pathway | Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 5/5. |
| Sequence similarities | Belongs to the threonine synthase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Threonine biosynthesis |
| Ligand | Pyridoxal phosphate |
| Molecular function | Lyase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | threonine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Molecular_function | pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro threonine synthase activityInferred 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 – 352 | 352 | Threonine synthase | PRO_0000185626 | |||||
Regions | |||||||||
| Region | 185 – 189 | 5 | Pyridoxal phosphate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 85 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 314 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 59 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase." Parsot C. EMBO J. 5:3013-3019(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.  Danchin A.Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [3] | "Cloning and nucleotide sequence of the Bacillus subtilis hom gene coding for homoserine dehydrogenase. Structural and evolutionary relationships with Escherichia coli aspartokinases-homoserine dehydrogenases I and II." Parsot C., Cohen G.N. J. Biol. Chem. 263:14654-14660(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35. Strain: 168. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X04603 Genomic DNA. Translation: CAA28270.1. AL009126 Genomic DNA. Translation: CAB15215.1. M23217 Genomic DNA. Translation: AAA50610.1. |
| PIR | A25364. |
| RefSeq | NP_391105.1. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | P04990. |
| SMR | P04990. Positions 2-325. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 224308.BSU32250. |
Proteomic databases | |
| PaxDb | P04990. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB15215; CAB15215; BSU32250. |
| GeneID | 936660. |
| KEGG | bsu:BSU32250. |
| PATRIC | 18978422. VBIBacSub10457_3374. |
Organism-specific databases | |
| GenoList | BSU32250. [Micado] |
Phylogenomic databases | |
| eggNOG | COG0498. |
| HOGENOM | HOG000076503. |
| KO | K01733. |
| OMA | WALRTED. |
| ProtClustDB | PRK07409. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU32250-MONOMER. |
| UniPathway | UPA00050; UER00065. |
Family and domain databases | |
| InterPro | IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS. IPR026260. Thr_Synthase. IPR004450. Thr_synthase_like. IPR001926. Trp_syn_b_sub_like_PLP_eny_SF. [Graphical view] |
| Pfam | PF00291. PALP. 1 hit. [Graphical view] |
| PIRSF | PIRSF038945. Thr_synthase. 1 hit. |
| SUPFAM | SSF53686. PyrdxlP-dep_enz_bsu. 1 hit. |
| TIGRFAMs | TIGR00260. thrC. 1 hit. |
| PROSITE | PS00165. DEHYDRATASE_SER_THR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | THRC_BACSU | ||||||||
| Accession | Primary (citable) accession number: P04990 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |