P45837 (THRC_MYCLE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 87.
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: Threonine synthase Short name=TS EC=4.2.3.1 | ||||
| Gene names |
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| Organism | Mycobacterium leprae (strain TN) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 272631 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › ![]() |
Protein attributes
| Sequence length | 360 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. |
| Subunit structure | Homodimer By similarity. |
| 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 |
| 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 – 360 | 360 | Threonine synthase | PRO_0000185636 | |||||
Regions | |||||||||
| Region | 196 – 200 | 5 | Pyridoxal phosphate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 95 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 326 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 69 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Smith D.R., Robison K. Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. Barrell B.G.Nature 409:1007-1011(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U15186 Genomic DNA. Translation: AAA63090.1. AL583920 Genomic DNA. Translation: CAC31511.1. |
| PIR | T09991. |
| RefSeq | NP_301824.1. NC_002677.1. |
3D structure databases | |
| ProteinModelPortal | P45837. |
| SMR | P45837. Positions 10-358. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 272631.ML1130. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAC31511; CAC31511; CAC31511. |
| GeneID | 910224. |
| KEGG | mle:ML1130. |
| PATRIC | 18054215. VBIMycLep78757_2052. |
Organism-specific databases | |
| Leproma | ML1130. |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0498. |
| HOGENOM | HOG000076503. |
| KO | K01733. |
| OMA | AMGKLSQ. |
| ProtClustDB | PRK07409. |
Enzyme and pathway databases | |
| 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_MYCLE | ||||||||
| Accession | Primary (citable) accession number: P45837 | ||||||||
| 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
