Canmetcon
Identification
Name:Tryptophanase
Synonyms:
  • L-tryptophan indole-lyase
  • TNase
Gene Name:tnaA
Enzyme Class:
Biological Properties
General Function:Involved in lyase activity
Specific Function:L-tryptophan + H(2)O = indole + pyruvate + NH(3)
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+ThumbThumb+Thumb+Thumb
Thumb+Thumb+Thumb+ThumbThumb+Thumb+Thumb
SMPDB Reactions:
ThumbThumb+Thumb+Thumb
ThumbThumb+Thumb+Thumb
ThumbThumb+Thumb+Thumb
EcoCyc Reactions:
Thumb+ThumbThumb+Thumb+Thumb
Complex Reactions:
Thumb+ThumbThumb+Thumb+Thumb
ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb+Thumb
Thumb+ThumbThumb+Thumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB036092-Aminoacrylic acidMetaboCard
ECMDB241982-aminoprop-2-enoateMetaboCard
ECMDB00051AmmoniaMetaboCard
ECMDB21186AmmoniumMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB03276Hydrogen sulfideMetaboCard
ECMDB00738IndoleMetaboCard
ECMDB00574L-CysteineMetaboCard
ECMDB00187L-SerineMetaboCard
ECMDB00929L-TryptophanMetaboCard
ECMDB00243Pyruvic acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
carbon-carbon lyase activity
catalytic activity
cofactor binding
lyase activity
pyridoxal phosphate binding
tryptophanase activity
Process
aromatic amino acid family metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid derivative metabolic process
cellular amino acid metabolic process
cellular biogenic amine metabolic process
cellular metabolic process
indolalkylamine metabolic process
metabolic process
tryptophan metabolic process
Gene Properties
Blattner:b3708
Gene OrientationClockwise
Centisome Percentage:83.77
Left Sequence End3886753
Right Sequence End3888168
Gene Sequence:
>1416 bp
GTGAAACAAAGCACTATTGCACTGGCACTCTTACCGTTACTGTTTACCCCTGTGACAAAA
GCCCGGACACCAGAAATGCCTGTTCTGGAAAACCGGGCTGCTCAGGGCGATATTACTGCA
CCCGGCGGTGCTCGCCGTTTAACGGGTGATCAGACTGCCGCTCTGCGTGATTCTCTTAGC
GATAAACCTGCAAAAAATATTATTTTGCTGATTGGCGATGGGATGGGGGACTCGGAAATT
ACTGCCGCACGTAATTATGCCGAAGGTGCGGGCGGCTTTTTTAAAGGTATAGATGCCTTA
CCGCTTACCGGGCAATACACTCACTATGCGCTGAATAAAAAAACCGGCAAACCGGACTAC
GTCACCGACTCGGCTGCATCAGCAACCGCCTGGTCAACCGGTGTCAAAACCTATAACGGC
GCGCTGGGCGTCGATATTCACGAAAAAGATCACCCAACGATTCTGGAAATGGCAAAAGCC
GCAGGTCTGGCGACCGGTAACGTTTCTACCGCAGAGTTGCAGGATGCCACGCCCGCTGCG
CTGGTGGCACATGTGACCTCGCGCAAATGCTACGGTCCGAGCGCGACCAGTGAAAAATGT
CCGGGTAACGCTCTGGAAAAAGGCGGAAAAGGATCGATTACCGAACAGCTGCTTAACGCT
CGTGCCGACGTTACGCTTGGCGGCGGCGCAAAAACCTTTGCTGAAACGGCAACCGCTGGT
GAATGGCAGGGAAAAACGCTGCGTGAACAGGCACAGGCGCGTGGTTATCAGTTGGTGAGC
GATGCTGCCTCACTGAATTCGGTGACGGAAGCGAATCAGCAAAAACCCCTGCTTGGCCTG
TTTGCTGACGGCAATATGCCAGTGCGCTGGCTAGGACCGAAAGCAACGTACCATGGCAAT
ATCGATAAGCCCGCAGTCACCTGTACGCCAAATCCGCAACGTAATGACAGTGTACCAACC
CTGGCGCAGATGACCGACAAAGCCATTGAATTGTTGAGTAAAAATGAGAAAGGCTTTTTC
CTGCAAGTTGAAGGTGCGTCAATCGATAAACAGGATCATGCTGCGAATCCTTGTGGGCAA
ATTGGCGAGACGGTCGATCTCGATGAAGCCGTACAACGGGCGCTGGAATTCGCTAAAAAG
GAGGGTAACACGCTGGTCATAGTCACCGCTGATCACGCCCACGCCAGCCAGATTGTTGCG
CCGGATACCAAAGCTCCGGGCCTCACCCAGGCGCTAAATACCAAAGATGGCGCAGTGATG
GTGATGAGTTACGGGAACTCCGAAGAGGATTCACAAGAACATACCGGCAGTCAGTTGCGT
ATTGCGGCGTATGGCCCGCATGCCGCCAATGTTGTTGGACTGACCGACCAGACCGATCTC
TTCTACACCATGAAAGCCGCTCTGGGGCTGAAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:471
Protein Molecular Weight:52773
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Tryptophanase
MENFKHLPEPFRIRVIEPVKRTTRAYREEAIIKSGMNPFLLDSEDVFIDLLTDSGTGAVT
QSMQAAMMRGDEAYSGSRSYYALAESVKNIFGYQYTIPTHQGRGAEQIYIPVLIKKREQE
KGLDRSKMVAFSNYFFDTTQGHSQINGCTVRNVYIKEAFDTGVRYDFKGNFDLEGLERGI
EEVGPNNVPYIVATITSNSAGGQPVSLANLKAMYSIAKKYDIPVVMDSARFAENAYFIKQ
REAEYKDWTIEQITRETYKYADMLAMSAKKDAMVPMGGLLCMKDDSFFDVYTECRTLCVV
QEGFPTYGGLEGGAMERLAVGLYDGMNLDWLAYRIAQVQYLVDGLEEIGVVCQQAGGHAA
FVDAGKLLPHIPADQFPAQALACELYKVAGIRAVEIGSFLLGRDPKTGKQLPCPAELLRL
TIPRATYTQTHMDFIIEAFKHVKENAANIKGLTFTYEPKVLRHFTAKLKEV
References
External Links:
ResourceLink
Uniprot ID:P0A853
Uniprot Name:TNAA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674524
Ecogene ID:EG11005
Ecocyc:EG11005
ColiBase:b3708
Kegg Gene:b3708
EchoBASE ID:EB0998
CCDB:TNAA_ECOLI
BacMap:90111643
General Reference:
  • 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
  • Burland, V., Plunkett, G. 3rd, Daniels, D. L., Blattner, F. R. (1993). "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Genomics 16:551-561. Pubmed: 7686882
  • Deeley, M. C., Yanofsky, C. (1981). "Nucleotide sequence of the structural gene for tryptophanase of Escherichia coli K-12." J Bacteriol 147:787-796. Pubmed: 6268608
  • 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
  • Kagamiyama, H., Matsubara, H., Snell, E. E. (1972). "The chemical structure of tryptophanase from Escherichia coli. 3. Isolation and amino acid sequence of the tryptic peptides." J Biol Chem 247:1576-1586. Pubmed: 4551944
  • Ku, S. Y., Yip, P., Howell, P. L. (2006). "Structure of Escherichia coli tryptophanase." Acta Crystallogr D Biol Crystallogr 62:814-823. Pubmed: 16790938
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Phillips, R. S., Gollnick, P. D. (1989). "Evidence that cysteine 298 is in the active site of tryptophan indole-lyase." J Biol Chem 264:10627-10632. Pubmed: 2659590
  • Sarsero, J. P., Wookey, P. J., Gollnick, P., Yanofsky, C., Pittard, A. J. (1991). "A new family of integral membrane proteins involved in transport of aromatic amino acids in Escherichia coli." J Bacteriol 173:3231-3234. Pubmed: 2022620
  • Stewart, V., Yanofsky, C. (1985). "Evidence for transcription antitermination control of tryptophanase operon expression in Escherichia coli K-12." J Bacteriol 164:731-740. Pubmed: 3902796
  • Tokushige, M., Tsujimoto, N., Oda, T., Honda, T., Yumoto, N., Ito, S., Yamamoto, M., Kim, E. H., Hiragi, Y. (1989). "Role of cysteine residues in tryptophanase for monovalent cation-induced activation." Biochimie 71:711-720. Pubmed: 2502187
  • 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