Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial (Q03557)

Identification
NameGlutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial
Synonyms
  • Glu-ADT subunit A
  • HMG2-induced ER-remodeling protein 2
  • Loss of respiratory capacity protein 6
Gene NameHER2
Enzyme Class
Biological Properties
General FunctionInvolved in carbon-nitrogen ligase activity, with glutamine as amido-N-donor
Specific FunctionFurnishes a means for formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu- tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho- Glu-tRNA(Gln). Required for HMG2-induced ER-remodeling
Cellular LocationMitochondrion
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG Reactions
water + 4-guanidinobutanamide → 4-guanidinobutanoic acid + Ammonium
Metabolites
YMDB IDNameView
YMDB00002L-GlutamineShow
YMDB00109Adenosine triphosphateShow
YMDB00271L-Glutamic acidShow
YMDB00423AmmoniumShow
YMDB005854-guanidinobutanoic acidShow
YMDB005864-guanidinobutanamideShow
YMDB00890waterShow
YMDB00907phosphateShow
YMDB00914ADPShow
GO Classification
Component
Not Available
Function
catalytic activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
carbon-nitrogen ligase activity, with glutamine as amido-N-donor
Process
biosynthetic process
macromolecule biosynthetic process
cellular macromolecule biosynthetic process
translation
metabolic process
Gene Properties
Chromosome Locationchromosome 13
LocusYMR293C
Gene Sequence>1395 bp ATGCCACTGAAACGCTCCTTAAAAGAATCAATCGAAAGATTATCTAGTTTTCAATCAAAA TATAATATTTTCACTAGTATCAATCCATCTCCTTATTCAATCACAAATAAAAAAGGTACA AAAGAAACATTGACAGGTTGCGTTGCCAGTATCAAGGATAATATAGTTACAAAAGATTTT CCAACCACATGTGCCTCACATATACTTGAGAATTTCAAGTCTCCCTTCGATGCAACAGTA GTGAAACTATTAAAACAGGCAGGAGTGCATATCTTAGGCAAGACAAATTTAGATGAATTT GGAATGGGTTCTGGGGGAGTACATTCAATAAGAGGGCCCGTAATTAACCCTTTATATCCT CATGAGGACAAGAAGATCATGGGAGGTTCATCGTCTGGAGCCGCTGCAAGCGTTGCTTGC GATCTAGTCGATTTTGCCTTGGGAACAGATACTGGTGGCTCCGTTAGGCTCCCCGCATGC TATGGATCTGTTTTAGGATTCAAGCCGTCCTATGGACGGTTGTCAAGATTTGGCGTAATA GCGTATTCTCAATCTTTAGACACTGTTGGCATACTTAGCAAAAAGATAAACGTCTTGCGA AAAGTATTTCATACGCTCGATAAATATGACATGAAAGATCCCACTTCCTTAAGTGTGGAA TTGCGTGAATTGATAGAAGGGAATAAAAAGGTTAGGAGACCTTTAAAGGTAGGAATTGTA AAGGAATTTAGCCATGAAAGTATGCCCATTGGGTTCCACAGATTATATTTATCCTTACTA GAAAAGCTGATAAATTTAGGGCTTGAAATATACCCTGTATCCATTCCATCTGTAAAAAAC TGTTTACCGATTTATTATACGCTATCACCCGCTGAAGCGGCTTCCAATTTATCAAGGTAT GATGGTATCAGATATGGATACAGAGATTCAGAACTCGATATAAAAGACGGTATTTTATTC GCACCTACTAGGTCCAAATTCGGAACAGAAGTTAAGAATAGAATCATTCTAGGTAATTAT AATCTTTGTTCAGATGCATTTAAGAACAATTTTATTAAGGCAGAAAAGCTACGAGTTAAT TTGATCGATGAATTTGACGGGATCTTCAGATTTCCAAATGTTTTAACTAATTCTAAGGGA AATCCAGACGGCCTAGATCTACTGATAGTTCCCACATCGTCCAAGCTTCCTGGATCCATA AGGGACTTCGAAGAAGAGGAAGCCAAATCTCCGGCTAACTCGTATATAAACGATGTCTTT ACTGTCCCAATGTCATTGGCTGGACTACCAAGTTTATCAATGCCTTTAAAAGAGAAGACC CCGATTGGCTTACAGGTAGTAGGTCAATATGGTGATGATTCCACTGTGTTAGATTTTGTC GAGTCAATATCATAA
Protein Properties
Pfam Domain Function
Protein Residues464
Protein Molecular Weight50918.0
Protein Theoretical pI8.84
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial MPLKRSLKESIERLSSFQSKYNIFTSINPSPYSITNKKGTKETLTGCVASIKDNIVTKDF PTTCASHILENFKSPFDATVVKLLKQAGVHILGKTNLDEFGMGSGGVHSIRGPVINPLYP HEDKKIMGGSSSGAAASVACDLVDFALGTDTGGSVRLPACYGSVLGFKPSYGRLSRFGVI AYSQSLDTVGILSKKINVLRKVFHTLDKYDMKDPTSLSVELRELIEGNKKVRRPLKVGIV KEFSHESMPIGFHRLYLSLLEKLINLGLEIYPVSIPSVKNCLPIYYTLSPAEAASNLSRY DGIRYGYRDSELDIKDGILFAPTRSKFGTEVKNRIILGNYNLCSDAFKNNFIKAEKLRVN LIDEFDGIFRFPNVLTNSKGNPDGLDLLIVPTSSKLPGSIRDFEEEEAKSPANSYINDVF TVPMSLAGLPSLSMPLKEKTPIGLQVVGQYGDDSTVLDFVESIS
References
External Links
ResourceLink
Saccharomyces Genome Database HER2
Uniprot IDQ03557
Uniprot NameGATH_YEAST
GenBank Gene IDX80836
Genebank Protein ID530350
General Reference
  • Bowman, S., Churcher, C., Badcock, K., Brown, D., Chillingworth, T., Connor, R., Dedman, K., Devlin, K., Gentles, S., Hamlin, N., Hunt, S., Jagels, K., Lye, G., Moule, S., Odell, C., Pearson, D., Rajandream, M., Rice, P., Skelton, J., Walsh, S., Whitehead, S., Barrell, B. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Nature 387:90-93.9169872
  • Kumar, A., Agarwal, S., Heyman, J. A., Matson, S., Heidtman, M., Piccirillo, S., Umansky, L., Drawid, A., Jansen, R., Liu, Y., Cheung, K. H., Miller, P., Gerstein, M., Roeder, G. S., Snyder, M. (2002). "Subcellular localization of the yeast proteome." Genes Dev 16:707-719.11914276
  • 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
  • Frechin, M., Senger, B., Braye, M., Kern, D., Martin, R. P., Becker, H. D. (2009). "Yeast mitochondrial Gln-tRNA(Gln) is generated by a GatFAB-mediated transamidation pathway involving Arc1p-controlled subcellular sorting of cytosolic GluRS." Genes Dev 23:1119-1130.19417106
  • 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
  • Federovitch, C. M., Jones, Y. Z., Tong, A. H., Boone, C., Prinz, W. A., Hampton, R. Y. (2008). "Genetic and structural analysis of Hmg2p-induced endoplasmic reticulum remodeling in Saccharomyces cerevisiae." Mol Biol Cell 19:4506-4520.18667535