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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
cell part
intracellular part
cytoplasm
Function
nucleotide binding
tRNA binding
phenylalanine-tRNA ligase activity
ligase activity
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
aminoacyl-tRNA ligase activity
RNA binding
catalytic activity
Process
tRNA processing
metabolic process
cellular macromolecule metabolic process
macromolecule metabolic process
RNA metabolic process
ncRNA metabolic process
phenylalanyl-tRNA aminoacylation
tRNA metabolic process
biosynthetic process
tRNA aminoacylation
tRNA aminoacylation for protein translation
macromolecule biosynthetic process
cellular macromolecule biosynthetic process
translation
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