Tryptophan synthase beta chain (P0A879)

Identification
Name:Tryptophan synthase beta chain
Synonyms:Not Available
Gene Name:trpB
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
  • Glycine, serine and threonine metabolism ec00260
  • Metabolic pathways eco01100
  • Phenylalanine, tyrosine and tryptophan biosynthesis ec00400
  • Tryptophan metabolism ec00380
KEGG Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Indole + 1.0L-Serine → 1.0Water + 1.0L-Tryptophan
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Indoleglycerol phosphate + 1.0L-Serine → 1.0D-Glyceraldehyde 3-phosphate + 1.0Water + 1.0L-Tryptophan
ReactionCard
1.0Thumb → 1.0Thumb+1.0Thumb
1.0Indoleglycerol phosphate → 1.0D-Glyceraldehyde 3-phosphate + 1.0Indole
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Serine + 1.0Indole ↔ 1.0L-Tryptophan + 1.0Water
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Indoleglycerol phosphate ↔ 1.0Indole + 1.0D-Glyceraldehyde 3-phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Serine + 1.0Indoleglycerol phosphate ↔ 1.0L-Tryptophan + 1.0D-Glyceraldehyde 3-phosphate + 1.0Water
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Serine + 1.0Indoleglycerol phosphate + 1.0Indole ↔ 1.0L-Tryptophan + 1.0D-Glyceraldehyde 3-phosphate + 1.0Water
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0L-Serine+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Indole + 1.0L-Serine + 1.0L-Serine → 1.0Water + 1.0L-Tryptophan
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Indole + 1.0L-Serine → 1.0Water + 1.0L-Tryptophan
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Indoleglycerol phosphate + 1.0L-Serine → 1.0D-Glyceraldehyde 3-phosphate + 1.0Water + 1.0L-Tryptophan
ReactionCard
1.0Thumb → 1.0Thumb+1.0Thumb
1.0Indoleglycerol phosphate → 1.0D-Glyceraldehyde 3-phosphate + 1.0Indole
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01112D-Glyceraldehyde 3-phosphateMetaboCard
ECMDB00738IndoleMetaboCard
ECMDB20160Indoleglycerol phosphateMetaboCard
ECMDB00187L-SerineMetaboCard
ECMDB00929L-TryptophanMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
carbon-oxygen lyase activity
catalytic activity
cofactor binding
hydro-lyase activity
lyase activity
pyridoxal phosphate binding
tryptophan synthase activity
Process
cellular amino acid and derivative metabolic process
cellular amino acid derivative metabolic process
cellular biogenic amine metabolic process
cellular metabolic process
indolalkylamine metabolic process
metabolic process
tryptophan metabolic process
Gene Properties
Blattner:b1261
Gene OrientationCounterclockwise
Centisome Percentage:28.35
Left Sequence End1315246
Right Sequence End1316439
Gene Sequence:
>1194 bp
ATGACAACATTACTTAACCCCTATTTTGGTGAGTTTGGCGGCATGTACGTGCCACAAATC
CTGATGCCTGCTCTGCGCCAGCTGGAAGAAGCTTTTGTCAGTGCGCAAAAAGATCCTGAA
TTTCAGGCTCAGTTCAACGACCTGCTGAAAAACTATGCCGGGCGTCCAACCGCGCTGACC
AAATGCCAGAACATTACAGCCGGGACGAACACCACGCTGTATCTCAAGCGTGAAGATTTG
CTGCACGGCGGCGCGCATAAAACTAACCAGGTGCTGGGGCAGGCGTTGCTGGCGAAGCGG
ATGGGTAAAACCGAAATCATCGCCGAAACCGGTGCCGGTCAGCATGGCGTGGCGTCGGCC
CTTGCCAGCGCCCTGCTCGGCCTGAAATGCCGTATTTATATGGGTGCCAAAGACGTTGAA
CGCCAGTCGCCTAACGTTTTTCGTATGCGCTTAATGGGTGCGGAAGTGATCCCGGTGCAT
AGCGGTTCCGCGACGCTGAAAGATGCCTGTAACGAGGCGCTGCGCGACTGGTCCGGTAGT
TACGAAACCGCGCACTATATGCTGGGCACCGCAGCTGGCCCGCATCCTTATCCGACCATT
GTGCGTGAGTTTCAGCGGATGATTGGCGAAGAAACCAAAGCGCAGATTCTGGAAAGAGAA
GGTCGCCTGCCGGATGCCGTTATCGCCTGTGTTGGCGGCGGTTCGAATGCCATCGGCATG
TTTGCTGATTTCATCAATGAAACCAACGTCGGCCTGATTGGTGTGGAGCCAGGTGGTCAC
GGTATCGAAACTGGCGAGCACGGCGCACCGCTAAAACATGGTCGCGTGGGTATCTATTTC
GGTATGAAAGCGCCGATGATGCAAACCGAAGACGGGCAGATTGAAGAATCTTACTCCATC
TCCGCCGGACTGGATTTCCCGTCTGTCGGCCCACAACACGCGTATCTTAACAGCACTGGA
CGCGCTGATTACGTGTCTATTACCGATGATGAAGCCCTTGAAGCCTTCAAAACGCTGTGC
CTGCACGAAGGGATCATCCCGGCGCTGGAATCCTCCCACGCCCTGGCCCATGCGTTGAAA
ATGATGCGCGAAAACCCGGATAAAGAGCAGCTACTGGTGGTTAACCTTTCCGGTCGCGGC
GATAAAGACATCTTCACCGTTCACGATATTTTGAAAGCACGAGGGGAAATCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:397
Protein Molecular Weight:42983
Protein Theoretical pI:6
PDB File:1KFJ
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Tryptophan synthase beta chain
MTTLLNPYFGEFGGMYVPQILMPALRQLEEAFVSAQKDPEFQAQFNDLLKNYAGRPTALT
KCQNITAGTNTTLYLKREDLLHGGAHKTNQVLGQALLAKRMGKTEIIAETGAGQHGVASA
LASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSGSATLKDACNEALRDWSGS
YETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILEREGRLPDAVIACVGGGSNAIGM
FADFINETNVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTEDGQIEESYSI
SAGLDFPSVGPQHAYLNSTGRADYVSITDDEALEAFKTLCLHEGIIPALESSHALAHALK
MMRENPDKEQLLVVNLSGRGDKDIFTVHDILKARGEI
References
External Links:
ResourceLink
Uniprot ID:P0A879
Uniprot Name:TRPB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674888
PDB ID:1KFJ
Ecogene ID:EG11025
Ecocyc:EG11025
ColiBase:b1261
Kegg Gene:b1261
EchoBASE ID:EB1018
CCDB:TRPB_ECOLI
BacMap:16129222
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • 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
  • Cotton, R. G., Crawford, I. P. (1972). "Tryptophan synthetase B 2 subunit. Application of genetic analysis to the study of primary structure." J Biol Chem 247:1883-1891. Pubmed: 4552018
  • Crawford, I. P., Nichols, B. P., Yanofsky, C. (1980). "Nucleotide sequence of the trpB gene in Escherichia coli and Salmonella typhimurium." J Mol Biol 142:489-502. Pubmed: 7007651
  • Fluri, R., Jackson, L. E., Lee, W. E., Crawford, I. P. (1971). "Tryptophan synthetase 2 subunit. Primary structure of the pyridoxyl peptide from the Escherichia coli enzyme." J Biol Chem 246:6620-6624. Pubmed: 4943677
  • 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
  • Higgins, W., Miles, E. W., Fairwell, T. (1980). "Location of three active site residues in the NH2-terminal sequence of the beta 2 subunit tryptophan synthase from Escherichia coli." J Biol Chem 255:512-517. Pubmed: 6985892
  • 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
  • Milkman, R., Bridges, M. M. (1993). "Molecular evolution of the Escherichia coli chromosome. IV. Sequence comparisons." Genetics 133:455-468. Pubmed: 8095913
  • Yanofsky, C., Platt, T., Crawford, I. P., Nichols, B. P., Christie, G. E., Horowitz, H., VanCleemput, M., Wu, A. M. (1981). "The complete nucleotide sequence of the tryptophan operon of Escherichia coli." Nucleic Acids Res 9:6647-6668. Pubmed: 7038627
  • Zhao, G. P., Somerville, R. L. (1992). "Genetic and biochemical characterization of the trpB8 mutation of Escherichia coli tryptophan synthase. An amino acid switch at the sharp turn of the trypsin-sensitive "hinge" region diminishes substrate binding and alters solubility." J Biol Chem 267:526-541. Pubmed: 1309752