Alanyl-tRNA synthetase (P00957)

Identification
Name:Alanyl-tRNA synthetase
Synonyms:
  • Alanine--tRNA ligase
  • AlaRS
Gene Name:alaS
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:Edits incorrectly charged Ser-tRNA(Ala) and Gly- tRNA(Ala) but not incorrectly charged Ser-tRNA(Thr)
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Ala)+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0L-Alanyl-tRNA+1.0Thumb
1.0Adenosine triphosphate + 1.0L-Alanine + 1.0tRNA(Ala) + 1.0tRNA(Ala) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Alanyl-tRNA + 1.0L-Alanyl-tRNA
ReactionCard
SMPDB Reactions:
1.0L-Alanine+1.0Thumb+1.0Thumb+1.0tRNA(Ala)+1.0Thumb → 1.0Pyrophosphate+1.0Thumb+1.0L-alanyl-tRNA(Ala)
1.0L-Alanine + 1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0tRNA(Ala) + 1.0L-Alanine → 1.0Pyrophosphate + 1.0Adenosine monophosphate + 1.0L-alanyl-tRNA(Ala)
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Ala) → 1.0L-Alanyl-tRNA(Ala)+1.0Thumb+1.0Thumb
1.0L-Alanine + 1.0Adenosine triphosphate + 1.0tRNA(Ala) → 1.0L-Alanyl-tRNA(Ala) + 1.0Adenosine monophosphate + 1.0Pyrophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00161L-AlanineMetaboCard
ECMDB23790L-Alanyl-tRNAMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB23878tRNA(Ala)MetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
alanine-tRNA ligase activity
aminoacyl-tRNA ligase activity
ATP binding
binding
catalytic activity
ligase activity
ligase activity, forming aminoacyl-tRNA and related compounds
ligase activity, forming carbon-oxygen bonds
nucleic acid binding
nucleoside binding
nucleotide binding
purine nucleoside binding
Process
alanyl-tRNA aminoacylation
biosynthetic process
cellular macromolecule biosynthetic process
cellular macromolecule metabolic process
macromolecule biosynthetic process
macromolecule metabolic process
metabolic process
ncRNA metabolic process
RNA metabolic process
translation
tRNA aminoacylation
tRNA aminoacylation for protein translation
tRNA metabolic process
Gene Properties
Blattner:b2697
Gene OrientationCounterclockwise
Centisome Percentage:60.72
Left Sequence End2817403
Right Sequence End2820033
Gene Sequence:
>2631 bp
ATGAGCAAGAGCACCGCTGAGATCCGTCAGGCGTTTCTCGACTTTTTCCATAGTAAGGGA
CATCAGGTAGTTGCCAGCAGCTCCCTGGTACCCCATAACGACCCAACTTTGTTGTTTACC
AACGCCGGGATGAACCAGTTCAAGGATGTGTTCCTTGGGCTCGACAAGCGTAATTATTCC
CGCGCTACCACTTCCCAACGCTGCGTGCGTGCGGGTGGTAAACACAACGACCTGGAAAAC
GTCGGTTACACCGCGCGTCACCATACCTTCTTCGAAATGCTGGGCAACTTCAGCTTCGGC
GACTATTTCAAACACGATGCCATTCAGTTTGCATGGGAACTGCTGACCAGCGAAAAATGG
TTTGCCCTGCCGAAAGAGCGTCTGTGGGTTACCGTCTATGAAAGCGACGACGAAGCCTAC
GAAATCTGGGAAAAAGAAGTAGGGATCCCGCGCGAACGTATTATTCGCATCGGCGATAAC
AAAGGTGCGCCATACGCATCTGACAACTTCTGGCAGATGGGTGACACTGGTCCGTGCGGC
CCGTGCACCGAAATCTTCTACGATCACGGCGACCACATTTGGGGGGGCCCTCCGGGAAGC
CCGGAAGAAGACGGCGACCGCTACATTGAGATCTGGAACATCGTCTTCATGCAGTTCAAC
CGCCAGGCCGATGGCACGATGGAACCGCTGCCGAAGCCGTCTGTAGATACCGGTATGGGT
CTGGAGCGTATTGCTGCGGTGCTGCAACACGTTAACTCTAACTATGACATCGACCTGTTC
CGCACGCTGATCCAGGCGGTAGCGAAAGTCACTGGCGCAACCGATCTGAGCAATAAATCG
CTGCGCGTAATCGCTGACCACATTCGTTCTTGTGCGTTCCTGATCGCGGATGGCGTAATG
CCGTCCAATGAAAACCGTGGTTATGTACTGCGTCGTATCATTCGTCGCGCAGTGCGTCAC
GGTAATATGCTCGGCGCGAAAGAAACCTTCTTCTACAAACTGGTTGGTCCGCTGATCGAC
GTTATGGGCTCTGCGGGTGAAGACCTGAAACGCCAGCAGGCGCAGGTTGAGCAGGTGCTG
AAGACTGAAGAAGAGCAGTTTGCTCGTACTCTGGAGCGCGGTCTGGCGTTGCTGGATGAA
GAGCTGGCAAAACTTTCTGGTGATACGCTGGATGGTGAAACTGCTTTCCGTCTGTACGAC
ACCTATGGCTTCCCGGTTGACCTGACGGCTGATGTTTGTCGTGAGCGCAACATCAAAGTT
GACGAAGCTGGTTTTGAAGCTGCAATGGAAGAGCAGCGTCGTCGCGCGCGCGAAGCCAGC
GGCTTTGGTGCCGATTACAACGCAATGATCCGTGTTGACAGTGCATCTGAATTTAAAGGC
TATGACCATCTGGAACTGAACGGCAAAGTGACTGCGCTGTTTGTTGATGGTAAAGCGGTT
GATGCCATCAATGCAGGCCAGGAAGCTGTGGTCGTGCTGGATCAAACGCCATTCTATGCG
GAATCCGGCGGTCAGGTTGGCGATAAAGGCGAACTGAAAGGCGCTAACTTCTCCTTTGCG
GTGGAAGATACGCAGAAATACGGCCAGGCGATTGGTCACATCGGTAAACTTGCTGCGGGT
TCTCTGAAAGTGGGCGACGCGGTGCAGGCTGATGTTGATGAGGCTCGTCGCGCCCGTATT
CGTCTGAATCACTCCGCAACGCACCTGATGCACGCTGCGCTGCGCCAGGTTCTGGGTACT
CATGTATCGCAGAAAGGTTCACTGGTTAACGACAAGGTGCTGCGCTTCGACTTCTCACAC
AACGAAGCGATGAAACCAGAAGAGATTCGTGCGGTCGAAGACCTGGTGAACACACAGATT
CGTCGCAATTTGCCGATCGAAACCAACATCATGGATCTCGAAGCGGCGAAAGCGAAAGGT
GCGATGGCGCTGTTCGGCGAGAAGTATGATGAGCGCGTACGCGTGCTGAGCATGGGCGAT
TTCTCTACCGAGTTGTGTGGCGGTACTCACGCCAGCCGCACTGGTGATATTGGTCTGTTC
CGCATCATCTCTGAATCGGGTACTGCTGCAGGCGTTCGTCGTATCGAAGCGGTAACCGGA
GAAGGTGCTATCGCCACCGTTCATGCAGACAGCGATCGCTTAAGCGAAGTCGCGCATCTG
CTGAAAGGCGATAGCAATAATCTGGCTGATAAAGTGCGCTCAGTACTGGAACGTACGCGT
CAGCTGGAAAAAGAGTTACAACAGCTTAAAGAACAAGCTGCCGCACAGGAGAGCGCAAAT
CTTTCCAGTAAGGCAATTGATGTTAATGGTGTTAAGCTGTTGGTTAGCGAGCTTAGCGGT
GTTGAGCCGAAAATGTTGCGTACCATGGTTGACGATTTAAAAAATCAGCTGGGGTCGACA
ATTATCGTGCTGGCAACGGTAGTCGAAGGTAAGGTTTCTCTGATTGCAGGCGTATCTAAG
GACGTCACAGATCGTGTGAAAGCAGGGGAACTGATTGGTATGGTCGCTCAGCAGGTGGGC
GGCAAGGGTGGTGGACGTCCTGACATGGCGCAAGCCGGTGGTACGGATGCTGCGGCCTTA
CCTGCAGCGTTAGCCAGTGTGAAAGGCTGGGTCAGCGCGAAATTGCAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:876
Protein Molecular Weight:96032
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Alanyl-tRNA synthetase
MSKSTAEIRQAFLDFFHSKGHQVVASSSLVPHNDPTLLFTNAGMNQFKDVFLGLDKRNYS
RATTSQRCVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKHDAIQFAWELLTSEKW
FALPKERLWVTVYESDDEAYEIWEKEVGIPRERIIRIGDNKGAPYASDNFWQMGDTGPCG
PCTEIFYDHGDHIWGGPPGSPEEDGDRYIEIWNIVFMQFNRQADGTMEPLPKPSVDTGMG
LERIAAVLQHVNSNYDIDLFRTLIQAVAKVTGATDLSNKSLRVIADHIRSCAFLIADGVM
PSNENRGYVLRRIIRRAVRHGNMLGAKETFFYKLVGPLIDVMGSAGEDLKRQQAQVEQVL
KTEEEQFARTLERGLALLDEELAKLSGDTLDGETAFRLYDTYGFPVDLTADVCRERNIKV
DEAGFEAAMEEQRRRAREASGFGADYNAMIRVDSASEFKGYDHLELNGKVTALFVDGKAV
DAINAGQEAVVVLDQTPFYAESGGQVGDKGELKGANFSFAVEDTQKYGQAIGHIGKLAAG
SLKVGDAVQADVDEARRARIRLNHSATHLMHAALRQVLGTHVSQKGSLVNDKVLRFDFSH
NEAMKPEEIRAVEDLVNTQIRRNLPIETNIMDLEAAKAKGAMALFGEKYDERVRVLSMGD
FSTELCGGTHASRTGDIGLFRIISESGTAAGVRRIEAVTGEGAIATVHADSDRLSEVAHL
LKGDSNNLADKVRSVLERTRQLEKELQQLKEQAAAQESANLSSKAIDVNGVKLLVSELSG
VEPKMLRTMVDDLKNQLGSTIIVLATVVEGKVSLIAGVSKDVTDRVKAGELIGMVAQQVG
GKGGGRPDMAQAGGTDAAALPAALASVKGWVSAKLQ
References
External Links:
ResourceLink
Uniprot ID:P00957
Uniprot Name:SYA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1800083
Ecogene ID:EG10034
Ecocyc:EG10034
ColiBase:b2697
Kegg Gene:b2697
EchoBASE ID:EB0033
CCDB:SYA_ECOLI
BacMap:16130604
General Reference:
  • Beebe, K., Mock, M., Merriman, E., Schimmel, P. (2008). "Distinct domains of tRNA synthetase recognize the same base pair." Nature 451:90-93. Pubmed: 18172502
  • Beebe, K., Ribas De Pouplana, L., Schimmel, P. (2003). "Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability." EMBO J 22:668-675. Pubmed: 12554667
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Chong, Y. E., Yang, X. L., Schimmel, P. (2008). "Natural homolog of tRNA synthetase editing domain rescues conditional lethality caused by mistranslation." J Biol Chem 283:30073-30078. Pubmed: 18723508
  • Guo, M., Chong, Y. E., Beebe, K., Shapiro, R., Yang, X. L., Schimmel, P. (2009). "The C-Ala domain brings together editing and aminoacylation functions on one tRNA." Science 325:744-747. Pubmed: 19661429
  • Guo, M., Chong, Y. E., Shapiro, R., Beebe, K., Yang, X. L., Schimmel, P. (2009). "Paradox of mistranslation of serine for alanine caused by AlaRS recognition dilemma." Nature 462:808-812. Pubmed: 20010690
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Herlihy, W. C., Royal, N. J., Biemann, K., Putney, S. D., Schimmel, P. R. (1980). "Mass spectra of partial protein hydrolysates as a multiple phase check for long polypeptides deduced from DNA sequences: NH2-terminal segment of alanine tRNA synthetase." Proc Natl Acad Sci U S A 77:6531-6535. Pubmed: 7005898
  • Miller, W. T., Hill, K. A., Schimmel, P. (1991). "Evidence for a "cysteine-histidine box" metal-binding site in an Escherichia coli aminoacyl-tRNA synthetase." Biochemistry 30:6970-6976. Pubmed: 1712632
  • Murayama, N., Shimizu, H., Takiguchi, S., Baba, Y., Amino, H., Horiuchi, T., Sekimizu, K., Miki, T. (1996). "Evidence for involvement of Escherichia coli genes pmbA, csrA and a previously unrecognized gene tldD, in the control of DNA gyrase by letD (ccdB) of sex factor F." J Mol Biol 256:483-502. Pubmed: 8604133
  • Musier-Forsyth, K., Schimmel, P. (1994). "Acceptor helix interactions in a class II tRNA synthetase: photoaffinity cross-linking of an RNA miniduplex substrate." Biochemistry 33:773-779. Pubmed: 8292605
  • Putney, S. D., Melendez, D. L., Schimmel, P. R. (1981). "Cloning, partial sequencing, and in vitro transcription of the gene for alanine tRNA synthetase." J Biol Chem 256:205-211. Pubmed: 6256345
  • Putney, S. D., Royal, N. J., Neuman de Vegvar, H., Herlihy, W. C., Biemann, K., Schimmel, P. (1981). "Primary structure of a large aminoacyl-tRNA synthetase." Science 213:1497-1501. Pubmed: 7025207
  • Putney, S. D., Sauer, R. T., Schimmel, P. R. (1981). "Purification and properties of alanine tRNA synthetase from Escherichia coli A tetramer of identical subunits." J Biol Chem 256:198-204. Pubmed: 7005211
  • Romeo, T., Gong, M., Liu, M. Y., Brun-Zinkernagel, A. M. (1993). "Identification and molecular characterization of csrA, a pleiotropic gene from Escherichia coli that affects glycogen biosynthesis, gluconeogenesis, cell size, and surface properties." J Bacteriol 175:4744-4755. Pubmed: 8393005
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842