P27735 (THRC_SERMA) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 64.
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 | Serratia marcescens | ||
| Taxonomic identifier | 615 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Serratia![]() |
Protein attributes
| Sequence length | 429 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 |
| 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)
Sequences
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References
| [1] | "Nucleotide sequence of the Serratia marcescens threonine operon and analysis of the threonine operon mutations which alter feedback inhibition of both aspartokinase I and homoserine dehydrogenase I." Omori K., Suzuki S., Komatsubara S. J. Bacteriol. 175:785-794(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Sr41. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D10387 Genomic DNA. Translation: BAA01222.1. X60821 Genomic DNA. Translation: CAA43214.1. |
| PIR | S16043. D47057. |
3D structure databases | |
| ProteinModelPortal | P27735. |
| SMR | P27735. Positions 1-425. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P27735. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| UniPathway | UPA00050; UER00065. |
Family and domain databases | |
| InterPro | IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS. IPR004450. Thr_synthase_like. IPR001926. Trp_syn_b_sub_like_PLP_eny_SF. [Graphical view] |
| Pfam | PF00291. PALP. 1 hit. [Graphical view] |
| 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_SERMA | ||||||||
| Accession | Primary (citable) accession number: P27735 | ||||||||
| 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
