DB code: S00373
| CATH domain | 3.40.50.1470 : Rossmann fold | Catalytic domain |
|---|---|---|
| E.C. | 3.1.1.29 | |
| CSA | 2pth | |
| M-CSA | 2pth | |
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| P0A7D1 |
Peptidyl-tRNA hydrolase
|
PTH
EC 3.1.1.29 |
NP_415722.1
(Protein)
NC_000913.2 (DNA/RNA sequence) YP_489471.1 (Protein) NC_007779.1 (DNA/RNA sequence) |
PF01195
(Pept_tRNA_hydro)
[Graphical View] |
| KEGG enzyme name |
|---|
|
aminoacyl-tRNA hydrolase
aminoacyl-transfer ribonucleate hydrolase N-substituted aminoacyl transfer RNA hydrolase peptidyl-tRNA hydrolase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P0A7D1 | PTH_ECOLI | N-substituted aminoacyl-tRNA + H(2)O = N- substituted amino acid + tRNA. | Monomer. | Cytoplasm. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|
| Compound table | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Substrates | Products | Intermediates | ||||||||
| KEGG-id | C03880 | C00001 | C03523 | C00066 | ||||||
| E.C. | ||||||||||
| Compound | N-Substituted aminoacyl-tRNA | H2O | N-Substituted amino acid | tRNA | ||||||
| Type | amino acids,amide group,nucleic acids | H2O | amino acids,amide group | nucleic acids | ||||||
| ChEBI |
15377 15377 |
|||||||||
| PubChem |
22247451 962 22247451 962 |
|||||||||
| 2pthA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| literature [2],[3] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 2pthA |
|
|
|
|
|
ASN 10;HIS 20;ASN 21;ASN 68;ASP 93;ASN 114 | ||||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 9144799 |
| Journal | Proteins |
| Year | 1997 |
| Volume | 28 |
| Pages | 135-6 |
| Authors | Schmitt E, Fromant M, Plateau P, Mechulam Y, Blanquet S |
| Title | Crystallization and preliminary X-ray analysis of Escherichia coli peptidyl-tRNA hydrolase. |
| Related PDB | |
| Related UniProtKB | P0A7D1 |
| [2] | |
| Resource | |
| Comments | X-ray crystallography (1.2 Angstroms) |
| Medline ID | |
| PubMed ID | 9303320 |
| Journal | EMBO J |
| Year | 1997 |
| Volume | 16 |
| Pages | 4760-9 |
| Authors | Schmitt E, Mechulam Y, Fromant M, Plateau P, Blanquet S |
| Title | Crystal structure at 1.2 A resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase. |
| Related PDB | 2pth |
| Related UniProtKB | P0A7D1 |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10213600 |
| Journal | Biochemistry |
| Year | 1999 |
| Volume | 38 |
| Pages | 4982-7 |
| Authors | Fromant M, Plateau P, Schmitt E, Mechulam Y, Blanquet S |
| Title | Receptor site for the 5'-phosphate of elongator tRNAs governs substrate selection by peptidyl-tRNA hydrolase. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
| Created | Updated |
|---|---|
| 2002-09-05 | 2009-02-26 |