Transaminated amino acid decarboxylase (Q06408)

Identification
NameTransaminated amino acid decarboxylase
Synonyms
  • Transaminated branched-chain amino acid decarboxylase
Gene NameARO10
Enzyme Class
Biological Properties
General FunctionInvolved in magnesium ion binding
Specific FunctionOne of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) involved in amino acid catabolism. The enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids (alpha-keto-acids). In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids, phenylalanine, tryptophan, (and probably tyrosine), but also isoleucine, whereas leucine is a low efficiency and valine and pyruvate are no substrates. In analogy to the pyruvate decarboxylases the enzyme may in a side-reaction catalyze condensation (or carboligation) reactions leading to the formation of 2-hydroxy ketone, collectively called acyloins
Cellular LocationCytoplasm
SMPDB Pathways
Leucine DegradationPW002490 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG PathwaysNot Available
SMPDB Reactions
Ketoleucine + hydron → 3-methylbutanal + Carbon dioxide
KEGG Reactions
hydron + (S)-3-methyl-2-oxovaleric acid → 2-Methylbutanal + Carbon dioxide
Ketoleucine + hydron → Carbon dioxide + 3-methylbutanal
hydron + 3-(indol-3-yl)pyruvic acid ↔ Indoleacetaldehyde + Carbon dioxide
hydron + keto-phenylpyruvic acid → Phenylacetaldehyde + Carbon dioxide
Metabolites
YMDB IDNameView
YMDB00116PhenylacetaldehydeShow
YMDB00168(S)-3-methyl-2-oxovaleric acidShow
YMDB001693-(indol-3-yl)pyruvic acidShow
YMDB00354IndoleacetaldehydeShow
YMDB00388KetoleucineShow
YMDB004852-MethylbutanalShow
YMDB004993-methylbutanalShow
YMDB00786keto-phenylpyruvic acidShow
YMDB00862hydronShow
YMDB00912Carbon dioxideShow
GO Classification
Component
Not Available
Function
catalytic activity
lyase activity
carbon-carbon lyase activity
carboxy-lyase activity
binding
ion binding
cation binding
metal ion binding
vitamin binding
magnesium ion binding
thiamin pyrophosphate binding
Process
Not Available
Gene Properties
Chromosome Locationchromosome 4
LocusYDR380W
Gene Sequence>1908 bp ATGGCACCTGTTACAATTGAAAAGTTCGTAAATCAAGAAGAACGACACCTTGTTTCCAAC CGATCAGCAACAATTCCGTTTGGTGAATACATATTTAAAAGATTGTTGTCCATCGATACG AAATCAGTTTTCGGTGTTCCTGGTGACTTCAACTTATCTCTATTAGAATATCTCTATTCA CCTAGTGTTGAATCAGCTGGCCTAAGATGGGTCGGCACGTGTAATGAACTGAACGCCGCT TATGCGGCCGACGGATATTCCCGTTACTCTAATAAGATTGGCTGTTTAATAACCACGTAT GGCGTTGGTGAATTAAGCGCCTTGAACGGTATAGCCGGTTCGTTCGCTGAAAATGTCAAA GTTTTGCACATTGTTGGTGTGGCCAAGTCCATAGATTCGCGTTCAAGTAACTTTAGTGAT CGGAACCTACATCATTTGGTCCCACAGCTACATGATTCAAATTTTAAAGGGCCAAATCAT AAAGTATATCATGATATGGTAAAAGATAGAGTCGCTTGCTCGGTAGCCTACTTGGAGGAT ATTGAAACTGCATGTGACCAAGTCGATAATGTTATCCGCGATATTTACAAGTATTCTAAA CCTGGTTATATTTTTGTTCCTGCAGATTTTGCGGATATGTCTGTTACATGTGATAATTTG GTTAATGTTCCACGTATATCTCAACAAGATTGTATAGTATACCCTTCTGAAAACCAATTG TCTGACATAATCAACAAGATTACTAGTTGGATATATTCCAGTAAAACACCTGCGATCCTT GGAGACGTACTGACTGATAGGTATGGTGTGAGTAACTTTTTGAACAAGCTTATCTGCAAA ACTGGGATTTGGAATTTTTCCACTGTTATGGGAAAATCTGTAATTGATGAGTCAAACCCA ACTTATATGGGTCAATATAATGGTAAAGAAGGTTTAAAACAAGTCTATGAACATTTTGAA CTGTGCGACTTGGTCTTGCATTTTGGAGTCGACATCAATGAAATTAATAATGGGCATTAT ACTTTTACTTATAAACCAAATGCTAAAATCATTCAATTTCATCCGAATTATATTCGCCTT GTGGACACTAGGCAGGGCAATGAGCAAATGTTCAAAGGAATCAATTTTGCCCCTATTTTA AAAGAACTATACAAGCGCATTGACGTTTCTAAACTTTCTTTGCAATATGATTCAAATGTA ACTCAATATACGAACGAAACAATGCGGTTAGAAGATCCTACCAATGGACAATCAAGCATT ATTACACAAGTTCACTTACAAAAGACGATGCCTAAATTTTTGAACCCTGGTGATGTTGTC GTTTGTGAAACAGGCTCTTTTCAATTCTCTGTTCGTGATTTCGCGTTTCCTTCGCAATTA AAATATATATCGCAAGGATTTTTCCTTTCCATTGGCATGGCCCTTCCTGCCGCCCTAGGT GTTGGAATTGCCATGCAAGACCACTCAAACGCTCACATCAATGGTGGCAACGTAAAAGAG GACTATAAGCCAAGATTAATTTTGTTTGAAGGTGACGGTGCAGCACAGATGACAATCCAA GAACTGAGCACCATTCTGAAGTGCAATATTCCACTAGAAGTTATCATTTGGAACAATAAC GGCTACACTATTGAAAGAGCCATCATGGGCCCTACCAGGTCGTATAACGACGTTATGTCT TGGAAATGGACCAAACTATTTGAAGCATTCGGAGACTTCGACGGAAAGTATACTAATAGC ACTCTCATTCAATGTCCCTCTAAATTAGCACTGAAATTGGAGGAGCTTAAGAATTCAAAC AAAAGAAGCGGGATAGAACTTTTAGAAGTCAAATTAGGCGAATTGGATTTCCCCGAACAG CTAAAGTGCATGGTTGAAGCAGCGGCACTTAAAAGAAATAAAAAATAG
Protein Properties
Pfam Domain Function
Protein Residues635
Protein Molecular Weight71383.79688
Protein Theoretical pI6.51
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Transaminated amino acid decarboxylase MAPVTIEKFVNQEERHLVSNRSATIPFGEYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYS PSVESAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSALNGIAGSFAENVK VLHIVGVAKSIDSRSSNFSDRNLHHLVPQLHDSNFKGPNHKVYHDMVKDRVACSVAYLED IETACDQVDNVIRDIYKYSKPGYIFVPADFADMSVTCDNLVNVPRISQQDCIVYPSENQL SDIINKITSWIYSSKTPAILGDVLTDRYGVSNFLNKLICKTGIWNFSTVMGKSVIDESNP TYMGQYNGKEGLKQVYEHFELCDLVLHFGVDINEINNGHYTFTYKPNAKIIQFHPNYIRL VDTRQGNEQMFKGINFAPILKELYKRIDVSKLSLQYDSNVTQYTNETMRLEDPTNGQSSI ITQVHLQKTMPKFLNPGDVVVCETGSFQFSVRDFAFPSQLKYISQGFFLSIGMALPAALG VGIAMQDHSNAHINGGNVKEDYKPRLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNN GYTIERAIMGPTRSYNDVMSWKWTKLFEAFGDFDGKYTNSTLIQCPSKLALKLEELKNSN KRSGIELLEVKLGELDFPEQLKCMVEAAALKRNKK
References
External Links
ResourceLink
Saccharomyces Genome Database ARO10
Uniprot IDQ06408
Uniprot NameARO10_YEAST
GenBank Gene IDU28373
Genebank Protein ID849201
General Reference
  • Vuralhan, Z., Morais, M. A., Tai, S. L., Piper, M. D., Pronk, J. T. (2003). "Identification and characterization of phenylpyruvate decarboxylase genes in Saccharomyces cerevisiae." Appl Environ Microbiol 69:4534-4541.12902239
  • 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
  • Iraqui, I., Vissers, S., Andre, B., Urrestarazu, A. (1999). "Transcriptional induction by aromatic amino acids in Saccharomyces cerevisiae." Mol Cell Biol 19:3360-3371.10207060
  • Dickinson, J. R., Salgado, L. E., Hewlins, M. J. (2003). "The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae." J Biol Chem 278:8028-8034.12499363
  • Dickinson, J. R., Harrison, S. J., Dickinson, J. A., Hewlins, M. J. (2000). "An investigation of the metabolism of isoleucine to active Amyl alcohol in Saccharomyces cerevisiae." J Biol Chem 275:10937-10942.10753893
  • Peng, J., Schwartz, D., Elias, J. E., Thoreen, C. C., Cheng, D., Marsischky, G., Roelofs, J., Finley, D., Gygi, S. P. (2003). "A proteomics approach to understanding protein ubiquitination." Nat Biotechnol 21:921-926.12872131
  • Jacq, C., Alt-Morbe, J., Andre, B., Arnold, W., Bahr, A., Ballesta, J. P., Bargues, M., Baron, L., Becker, A., Biteau, N., Blocker, H., Blugeon, C., Boskovic, J., Brandt, P., Bruckner, M., Buitrago, M. J., Coster, F., Delaveau, T., del Rey, F., Dujon, B., Eide, L. G., Garcia-Cantalejo, J. M., Goffeau, A., Gomez-Peris, A., Zaccaria, P., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Nature 387:75-78.9169867