P0A8L1 · SYS_ECOLI

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)

Catalytic activity

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
64 μMserine
0.068 μMATP

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.

TypeIDPosition(s)Description
Binding site237-239L-serine (UniProtKB | ChEBI)
Binding site268-270ATP (UniProtKB | ChEBI)
Binding site291L-serine (UniProtKB | ChEBI)
Binding site355-358ATP (UniProtKB | ChEBI)
Binding site391L-serine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular Functionidentical protein binding
Molecular Functionmagnesium ion binding
Molecular Functionserine-tRNA ligase activity
Biological Processselenocysteine biosynthetic process
Biological Processseryl-tRNA aminoacylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Serine--tRNA ligase
  • EC number
  • Alternative names
    • Seryl-tRNA synthetase (SerRS)
    • Seryl-tRNA(Ser/Sec) synthetase

Gene names

    • Name
      serS
    • Ordered locus names
      b0893, JW0876

Organism names

  • Taxonomic identifier
  • Strains
    • K12
    • K12 / W3110 / ATCC 27325 / DSM 5911
    • K12 / MG1655 / ATCC 47076
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P0A8L1
  • Secondary accessions
    • P09156

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis355Loss of serine activation activity.

Chemistry

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001220441-430Serine--tRNA ligase

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).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P0A8L1serS P0A8L13EBI-548422, EBI-548422

Protein-protein interaction databases

Chemistry

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 status
    Complete
  • Length
    430
  • Mass (Da)
    48,414
  • Last updated
    2005-06-07 v1
  • Checksum
    87675745A512A626
MLDPNLLRNEPDAVAEKLARRGFKLDVDKLGALEERRKVLQVKTENLQAERNSRSKSIGQAKARGEDIEPLRLEVNKLGEELDAAKAELDALQAEIRDIALTIPNLPADEVPVGKDENDNVEVSRWGTPREFDFEVRDHVTLGEMHSGLDFAAAVKLTGSRFVVMKGQIARMHRALSQFMLDLHTEQHGYSENYVPYLVNQDTLYGTGQLPKFAGDLFHTRPLEEEADTSNYALIPTAEVPLTNLVRGEIIDEDDLPIKMTAHTPCFRSEAGSYGRDTRGLIRMHQFDKVEMVQIVRPEDSMAALEEMTGHAEKVLQLLGLPYRKIILCTGDMGFGACKTYDLEVWIPAQNTYREISSCSNVWDFQARRMQARCRSKSDKKTRLVHTLNGSGLAVGRTLVAVMENYQQADGRIEVPEVLRPYMNGLEYIG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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