Phenylalanyl-tRNA synthetase, mitochondrial (P08425)

Identification
NamePhenylalanyl-tRNA synthetase, mitochondrial
Synonyms
  • Phenylalanine--tRNA ligase
  • PheRS
Gene NameMSF1
Enzyme Class
Biological Properties
General FunctionInvolved in nucleotide binding
Specific FunctionCatalyzes direct attachment of p-Tyr (Tyr) to tRNAPhe. Permits also, with a lower efficiency, the attachment of m-Tyr to tRNAPhe, thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins
Cellular LocationMitochondrion matrix
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG Reactions
tRNA(Phe) + Adenosine triphosphate + L-Phenylalanine → Adenosine monophosphate + Pyrophosphate + Phe-tRNA(Phe)
Metabolites
YMDB IDNameView
YMDB00097Adenosine monophosphateShow
YMDB00109Adenosine triphosphateShow
YMDB00219PyrophosphateShow
YMDB00304L-PhenylalanineShow
GO Classification
Component
intracellular part
cytoplasm
cell part
Function
binding
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
ion binding
adenyl ribonucleotide binding
cation binding
ATP binding
metal ion binding
ligase activity, forming carbon-oxygen bonds
magnesium ion binding
ligase activity, forming aminoacyl-tRNA and related compounds
nucleic acid binding
catalytic activity
aminoacyl-tRNA ligase activity
RNA binding
nucleotide binding
tRNA binding
phenylalanine-tRNA ligase activity
ligase activity
Process
biosynthetic process
tRNA metabolic process
tRNA aminoacylation
tRNA aminoacylation for protein translation
macromolecule biosynthetic process
cellular macromolecule biosynthetic process
translation
metabolic process
tRNA processing
macromolecule metabolic process
cellular macromolecule metabolic process
RNA metabolic process
ncRNA metabolic process
phenylalanyl-tRNA aminoacylation
Gene Properties
Chromosome Locationchromosome 16
LocusYPR047W
Gene Sequence>1425 bp ATGGAGGTAACTTCAATGTTTCTCAATAGAATGATGAAGACCAGGACTGGTCTTTATCGC TTATATTCAACCCTTAAAGTTCCACATGTAGAAATCAATGGCATAAAATACAAGACCGAC CCACAGACTACCAATGTTACAGATTCAATAATAAAGCTTACCGACAGATCATTACATTTG AAAGAATCACATCCAGTAGGCATTCTTCGCGATCTAATTGAAAAGAAATTAAACTCAGTC GACAACACATTTAAGATCTTTAATAATTTCAAGCCCGTGGTAACCACAATGGAAAACTTC GATTCTTTAGGGTTTCCTAAGGATCATCCTGGAAGATCAAAATCTGACACATATTATATA AATGAGACGCACCTACTGAGAACACATACTTCAGCCCACGAATTAGAGTGCTTTCAAAAA ATAAGAAACGATTCAGATAATATTAAAAGTGGATTTTTAATATCTGCAGATGTGTACAGA AGAGATGAAATTGACAAAACTCACTATCCGGTATTCCACCAAATGGAAGGAGCCACAATT TGGAAACGAACGAAGGCTGATGTGGGCGTAAAGGAGCCAATGTATATCGAGAAAATCCGT GAAGATATCAGACAGGTAGAGAACCTTTTAAATAAAGAAAATGTAAAGATTACGGTTGAC GATGATACTATACCTTTGAAAGAAAATAATCCTAAACAAGAGTATATGTCCGATCTGGAG GTTGATTTGTGCTCTCAACATTTGAAGAGGTCCATTGAACTGATAGTTTCTGAAGTTTTT AACAAAAAAATATCTAGCATGATCAAGAACAAAGCGAATAATACACCCAAAGAGCTAAAA GTCCGTTGGATTAACGCTTACTTCCCCTGGACCGCGCCCTCATGGGAAATAGAGGTTTGG TGGCAGGGCGAATGGCTCGAACTCTGCGGATGCGGATTGATTCGTCAAGATGTGCTACTA AGAGCCGGATATAAACCTTCTGAAACAATTGGGTGGGCTTTTGGCTTGGGTTTGGACCGC ATTGCTATGCTTCTTTTTGAAATTCCAGATATTAGACTGCTTTGGAGTCGTGATGAAAGA TTTTCAAGACAATTCTCCAAGGGATTAATTACTTCCTTCAAACCTTATTCAAAACACCCG GGATCATTTAGGGATGTTGCGTTTTGGTTACCAGAAGATAAACCAGATATTCATCAAGTT CATGAAAATGATTTGATGGAAATTATCAGAAATATAGCTGGCGATTTGGTAGAGAGTGTC AAGCTAGTCGATAGCTTTACGCATCCGAAAACTGGGAGAAAATCTATGTGCTACAGGATC AACTATCAATCAATGGACAGAAATTTGACAAACGCCGAAGTTAACACTTTGCAAGACATG GTGTGTTCTAAATTGGTAAAAGAATACAGCGTAGAACTCAGATAG
Protein Properties
Pfam Domain Function
Protein Residues469
Protein Molecular Weight54828.39844
Protein Theoretical pI8.14
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Phenylalanyl-tRNA synthetase, mitochondrial MFLNRMMKTRTGLYRLYSTLKVPHVEINGIKYKTDPQTTNVTDSIIKLTDRSLHLKESHP VGILRDLIEKKLNSVDNTFKIFNNFKPVVTTMENFDSLGFPKDHPGRSKSDTYYINETHL LRTHTSAHELECFQKIRNDSDNIKSGFLISADVYRRDEIDKTHYPVFHQMEGATIWKRTK ADVGVKEPMYIEKIREDIRQVENLLNKENVKITVDDDTIPLKENNPKQEYMSDLEVDLCS QHLKRSIELIVSEVFNKKISSMIKNKANNTPKELKVRWINAYFPWTAPSWEIEVWWQGEW LELCGCGLIRQDVLLRAGYKPSETIGWAFGLGLDRIAMLLFEIPDIRLLWSRDERFSRQF SKGLITSFKPYSKHPGSFRDVAFWLPEDKPDIHQVHENDLMEIIRNIAGDLVESVKLVDS FTHPKTGRKSMCYRINYQSMDRNLTNAEVNTLQDMVCSKLVKEYSVELR
References
External Links
ResourceLink
Saccharomyces Genome Database MSF1
Uniprot IDP08425
Uniprot NameSYFM_YEAST
GenBank Gene IDZ49219
Genebank Protein ID805030
General Reference
  • Koerner, T. J., Myers, A. M., Lee, S., Tzagoloff, A. (1987). "Isolation and characterization of the yeast gene coding for the alpha subunit of mitochondrial phenylalanyl-tRNA synthetase." J Biol Chem 262:3690-3696.3029120
  • Bussey, H., Storms, R. K., Ahmed, A., Albermann, K., Allen, E., Ansorge, W., Araujo, R., Aparicio, A., Barrell, B., Badcock, K., Benes, V., Botstein, D., Bowman, S., Bruckner, M., Carpenter, J., Cherry, J. M., Chung, E., Churcher, C., Coster, F., Davis, K., Davis, R. W., Dietrich, F. S., Delius, H., DiPaolo, T., Hani, J., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Nature 387:103-105.9169875
  • Sanni, A., Walter, P., Boulanger, Y., Ebel, J. P., Fasiolo, F. (1991). "Evolution of aminoacyl-tRNA synthetase quaternary structure and activity: Saccharomyces cerevisiae mitochondrial phenylalanyl-tRNA synthetase." Proc Natl Acad Sci U S A 88:8387-8391.1924298
  • Kellis, M., Patterson, N., Endrizzi, M., Birren, B., Lander, E. S. (2003). "Sequencing and comparison of yeast species to identify genes and regulatory elements." Nature 423:241-254.12748633
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Sickmann, A., Reinders, J., Wagner, Y., Joppich, C., Zahedi, R., Meyer, H. E., Schonfisch, B., Perschil, I., Chacinska, A., Guiard, B., Rehling, P., Pfanner, N., Meisinger, C. (2003). "The proteome of Saccharomyces cerevisiae mitochondria." Proc Natl Acad Sci U S A 100:13207-13212.14576278