P0A8L1 · SYS_ECOLI
- ProteinSerine--tRNA ligase
- GeneserS
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids430 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the attachment of serine to tRNA(Ser) (PubMed:7537870).
Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec)
Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec)
Catalytic activity
- tRNA(Ser) + L-serine + ATP = L-seryl-tRNA(Ser) + AMP + diphosphate + H+
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
64 μM | serine | |||||
0.068 μM | ATP |
Pathway
Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 237-239 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: TAE | ||||||
Binding site | 268-270 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RSE | ||||||
Binding site | 291 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 355-358 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EISS | ||||||
Binding site | 391 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | identical protein binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | serine-tRNA ligase activity | |
Biological Process | selenocysteine biosynthetic process | |
Biological Process | seryl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine--tRNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0A8L1
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 355 | Loss of serine activation activity. | ||||
Sequence: E → Q |
Chemistry
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000122044 | 1-430 | Serine--tRNA ligase | |||
Sequence: MLDPNLLRNEPDAVAEKLARRGFKLDVDKLGALEERRKVLQVKTENLQAERNSRSKSIGQAKARGEDIEPLRLEVNKLGEELDAAKAELDALQAEIRDIALTIPNLPADEVPVGKDENDNVEVSRWGTPREFDFEVRDHVTLGEMHSGLDFAAAVKLTGSRFVVMKGQIARMHRALSQFMLDLHTEQHGYSENYVPYLVNQDTLYGTGQLPKFAGDLFHTRPLEEEADTSNYALIPTAEVPLTNLVRGEIIDEDDLPIKMTAHTPCFRSEAGSYGRDTRGLIRMHQFDKVEMVQIVRPEDSMAALEEMTGHAEKVLQLLGLPYRKIILCTGDMGFGACKTYDLEVWIPAQNTYREISSCSNVWDFQARRMQARCRSKSDKKTRLVHTLNGSGLAVGRTLVAVMENYQQADGRIEVPEVLRPYMNGLEYIG |
Proteomic databases
Interaction
Subunit
Homodimer (PubMed:7537870).
The tRNA molecule binds across the dimer, one part binds the N-terminus of the first SerRS subunit and the other part to the active site of the second subunit (PubMed:7537870).
The tRNA molecule binds across the dimer, one part binds the N-terminus of the first SerRS subunit and the other part to the active site of the second subunit (PubMed:7537870).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P0A8L1 | serS P0A8L1 | 3 | EBI-548422, EBI-548422 |
Protein-protein interaction databases
Chemistry
Structure
Family & Domains
Domain
Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length430
- Mass (Da)48,414
- Last updated2005-06-07 v1
- Checksum87675745A512A626
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X05017 EMBL· GenBank· DDBJ | CAA28673.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC73979.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAA35625.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
J03412 EMBL· GenBank· DDBJ | AAA83842.1 EMBL· GenBank· DDBJ | Genomic DNA |