Threonine synthase (P00934)

Identification
Name:Threonine synthase
Synonyms:
  • TS
Gene Name:thrC
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. To a lesser extent, is able to slowly catalyze the deamination of L-threonine into alpha-ketobutyrate and that of L- serine and 3-chloroalanine into pyruvate. Is also able to rapidly convert vinylglycine to threonine, which proves that the pyridoxal p-quinonoid of vinylglycine is an intermediate in the TS reaction
Cellular Location:Not Available
SMPDB Pathways:
  • Secondary Metabolites: threonine biosynthesis from aspartate PW000976
  • threonine biosynthesis PW000817
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Water + 1.0O-Phosphohomoserine ↔ 1.0Phosphate + 1.0L-Threonine
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Water + 1.0O-Phospho-4-hydroxy-L-threonine → 1.04-Hydroxy-L-threonine + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0O-Phospho-4-hydroxy-L-threonine + 1.0Water ↔ 1.04-Hydroxy-L-threonine + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0O-Phosphohomoserine + 1.0Water → 1.0Phosphate + 1.0L-Threonine
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0L-Threonine+1.0Thumb
1.0O-Phosphohomoserine + 1.0Water → 1.0Phosphate + 1.0L-Threonine + 1.0L-Threonine
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Water + 1.0O-Phosphohomoserine ↔ 1.0Phosphate + 1.0L-Threonine
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0O-Phosphohomoserine + 1.0Water → 1.0Phosphate + 1.0L-Threonine
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0O-Phosphohomoserine + 1.0Water → 1.0L-Threonine + 1.0Inorganic phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB200924-Hydroxy-L-threonineMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB00167L-ThreonineMetaboCard
ECMDB06802O-Phospho-4-hydroxy-L-threonineMetaboCard
ECMDB03484O-PhosphohomoserineMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
carbon-oxygen lyase activity
carbon-oxygen lyase activity, acting on phosphates
catalytic activity
cofactor binding
lyase activity
pyridoxal phosphate binding
threonine synthase activity
Process
aspartate family amino acid metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
metabolic process
threonine biosynthetic process
threonine metabolic process
Gene Properties
Blattner:b0004
Gene OrientationClockwise
Centisome Percentage:0.08
Left Sequence End3734
Right Sequence End5020
Gene Sequence:
>1287 bp
ATGAAACTCTACAATCTGAAAGATCACAACGAGCAGGTCAGCTTTGCGCAAGCCGTAACC
CAGGGGTTGGGCAAAAATCAGGGGCTGTTTTTTCCGCACGACCTGCCGGAATTCAGCCTG
ACTGAAATTGATGAGATGCTGAAGCTGGATTTTGTCACCCGCAGTGCGAAGATCCTCTCG
GCGTTTATTGGTGATGAAATCCCACAGGAAATCCTGGAAGAGCGCGTGCGCGCGGCGTTT
GCCTTCCCGGCTCCGGTCGCCAATGTTGAAAGCGATGTCGGTTGTCTGGAATTGTTCCAC
GGGCCAACGCTGGCATTTAAAGATTTCGGCGGTCGCTTTATGGCACAAATGCTGACCCAT
ATTGCGGGTGATAAGCCAGTGACCATTCTGACCGCGACCTCCGGTGATACCGGAGCGGCA
GTGGCTCATGCTTTCTACGGTTTACCGAATGTGAAAGTGGTTATCCTCTATCCACGAGGC
AAAATCAGTCCACTGCAAGAAAAACTGTTCTGTACATTGGGCGGCAATATCGAAACTGTT
GCCATCGACGGCGATTTCGATGCCTGTCAGGCGCTGGTGAAGCAGGCGTTTGATGATGAA
GAACTGAAAGTGGCGCTAGGGTTAAACTCGGCTAACTCGATTAACATCAGCCGTTTGCTG
GCGCAGATTTGCTACTACTTTGAAGCTGTTGCGCAGCTGCCGCAGGAGACGCGCAACCAG
CTGGTTGTCTCGGTGCCAAGCGGAAACTTCGGCGATTTGACGGCGGGTCTGCTGGCGAAG
TCACTCGGTCTGCCGGTGAAACGTTTTATTGCTGCGACCAACGTGAACGATACCGTGCCA
CGTTTCCTGCACGACGGTCAGTGGTCACCCAAAGCGACTCAGGCGACGTTATCCAACGCG
ATGGACGTGAGTCAGCCGAACAACTGGCCGCGTGTGGAAGAGTTGTTCCGCCGCAAAATC
TGGCAACTGAAAGAGCTGGGTTATGCAGCCGTGGATGATGAAACCACGCAACAGACAATG
CGTGAGTTAAAAGAACTGGGCTACACTTCGGAGCCGCACGCTGCCGTAGCTTATCGTGCG
CTGCGTGATCAGTTGAATCCAGGCGAATATGGCTTGTTCCTCGGCACCGCGCATCCGGCG
AAATTTAAAGAGAGCGTGGAAGCGATTCTCGGTGAAACGTTGGATCTGCCAAAAGAGCTG
GCAGAACGTGCTGATTTACCCTTGCTTTCACATAATCTGCCCGCCGATTTTGCTGCGTTG
CGTAAATTGATGATGAATCATCAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:428
Protein Molecular Weight:47113
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Threonine synthase
MKLYNLKDHNEQVSFAQAVTQGLGKNQGLFFPHDLPEFSLTEIDEMLKLDFVTRSAKILS
AFIGDEIPQEILEERVRAAFAFPAPVANVESDVGCLELFHGPTLAFKDFGGRFMAQMLTH
IAGDKPVTILTATSGDTGAAVAHAFYGLPNVKVVILYPRGKISPLQEKLFCTLGGNIETV
AIDGDFDACQALVKQAFDDEELKVALGLNSANSINISRLLAQICYYFEAVAQLPQETRNQ
LVVSVPSGNFGDLTAGLLAKSLGLPVKRFIAATNVNDTVPRFLHDGQWSPKATQATLSNA
MDVSQPNNWPRVEELFRRKIWQLKELGYAAVDDETTQQTMRELKELGYTSEPHAAVAYRA
LRDQLNPGEYGLFLGTAHPAKFKESVEAILGETLDLPKELAERADLPLLSHNLPADFAAL
RKLMMNHQ
References
External Links:
ResourceLink
Uniprot ID:P00934
Uniprot Name:THRC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321894
Ecogene ID:EG11000
Ecocyc:EG11000
ColiBase:b0004
Kegg Gene:b0004
EchoBASE ID:EB0993
CCDB:THRC_ECOLI
BacMap:16127998
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, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • 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
  • Laber, B., Gerbling, K. P., Harde, C., Neff, K. H., Nordhoff, E., Pohlenz, H. D. (1994). "Mechanisms of interaction of Escherichia coli threonine synthase with substrates and inhibitors." Biochemistry 33:3413-3423. Pubmed: 7907888
  • 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
  • Parsot, C., Cossart, P., Saint-Girons, I., Cohen, G. N. (1983). "Nucleotide sequence of thrC and of the transcription termination region of the threonine operon in Escherichia coli K12." Nucleic Acids Res 11:7331-7345. Pubmed: 6316258
  • Wilkins, M. R., Gasteiger, E., Tonella, L., Ou, K., Tyler, M., Sanchez, J. C., Gooley, A. A., Walsh, B. J., Bairoch, A., Appel, R. D., Williams, K. L., Hochstrasser, D. F. (1998). "Protein identification with N and C-terminal sequence tags in proteome projects." J Mol Biol 278:599-608. Pubmed: 9600841
  • Yura, T., Mori, H., Nagai, H., Nagata, T., Ishihama, A., Fujita, N., Isono, K., Mizobuchi, K., Nakata, A. (1992). "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Nucleic Acids Res 20:3305-3308. Pubmed: 1630901