Threonine dehydratase biosynthetic (P04968)

Identification
Name:Threonine dehydratase biosynthetic
Synonyms:
  • Threonine deaminase
Gene Name:ilvA
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Catalyzes the formation of alpha-ketobutyrate from threonine in a two-step reaction. The first step is a dehydration of threonine, followed by rehydration and liberation of ammonia. Deaminates L-threonine, but also L-serine to a lesser extent
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Serine ↔ 1.0Pyruvic acid + 1.0Ammonia
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1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Threonine ↔ 1.02-Ketobutyric acid + 1.0Ammonia
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1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Threonine → 1.0Hydrogen ion + 1.02-Ketobutyric acid + 1.0Ammonia
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1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Threonine → 1.02-Ketobutyric acid + 1.0Ammonia
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1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Serine → 1.0Pyruvic acid + 1.0Ammonia
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1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Threonine + 1.02-Aminobut-2-enoate + 1.02-Iminobutanoate + 1.0Water ↔ 1.02-Ketobutyric acid + 1.0Ammonia
ReactionCard
SMPDB Reactions:
1.0L-Threonine+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Threonine + 1.0L-Threonine → 1.0Hydrogen ion + 1.0Water + 1.0 (2Z)-2-aminobut-2-enoate
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EcoCyc Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Serine ↔ 1.0Pyruvic acid + 1.0Ammonia
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1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Threonine → 1.0Hydrogen ion + 1.02-Ketobutyric acid + 1.0Ammonia
ReactionCard
1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Threonine → 1.02-Ketobutyric acid + 1.0Ammonia
ReactionCard
1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Serine → 1.0Pyruvic acid + 1.0Ammonia
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Complex Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Threonine → 1.02-Ketobutyric acid + 1.0Ammonium
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB24204 (2Z)-2-aminobut-2-enoateMetaboCard
ECMDB237402-Aminobut-2-enoateMetaboCard
ECMDB000052-Ketobutyric acidMetaboCard
ECMDB00051AmmoniaMetaboCard
ECMDB21186AmmoniumMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00187L-SerineMetaboCard
ECMDB00167L-ThreonineMetaboCard
ECMDB00243Pyruvic acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
ammonia-lyase activity
binding
carbon-nitrogen lyase activity
catalytic activity
cofactor binding
L-threonine ammonia-lyase activity
lyase activity
pyridoxal phosphate binding
Process
branched chain family amino acid metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
isoleucine biosynthetic process
isoleucine metabolic process
metabolic process
Gene Properties
Blattner:b3772
Gene OrientationClockwise
Centisome Percentage:85.21
Left Sequence End3953354
Right Sequence End3954898
Gene Sequence:
>1545 bp
ATGTGGGATGTCATTGATTTATCGCGCTGGCAGTTTGCTCTGACCGCGCTGTATCACTTT
TTATTTGTACCCCTTACCCTGGGGCTGATTTTTTTGCTGGCTATTATGGAAACCATTTAC
GTGGTCACCGGCAAAACAATCTACCGCGATATGACGCGCTTCTGGGGTAAGCTCTTCGGT
ATCAATTTTGCTCTTGGCGTGGCTACCGGCCTGACCATGGAGTTTCAGTTTGGTACTAAC
TGGTCATTCTATTCCAACTATGTGGGCGATATTTTTGGCGCACCGCTGGCGATGGAAGCA
TTAATGGCCTTCTTCCTCGAATCCACCTTTGTCGGGCTGTTCTTCTTCGGCTGGCAACGG
CTGAATAAATACCAGCACCTGCTGGTGACGTGGCTGGTGGCGTTCGGTTCAAATCTCTCT
GCGTTGTGGATATTGAATGCCAACGGTTGGATGCAATACCCGACCGGTGCGCATTTTGAT
ATCGACACCCTGCGTATGGAGATGACCAGCTTCAGCGAGCTGGTCTTTAATCCGGTCAGC
CAGGTGAAATTTGTGCACACCGTAATGGCGGGCTACGTGACCGGGGCCATGTTTATTATG
GCGATCAGCGCCTGGTATTTACTGCGCGGACGGGAGCGCAATGTCGCATTACGCTCGTTT
GCCATCGGTTCCGTCTTCGGTACTCTGGCGATTATCGGTACCCTGCAACTCGGAGACAGT
TCTGCGTATGAAGTCGCGCAAGTACAACCGGTAAAACTGGCGGCGATGGAAGGGGAGTGG
CAAACGGAACCTGCACCTGCACCGTTCCATGTGGTTGCCTGGCCGGAACAGGATCAAGAG
CGTAACGCCTTTGCCCTCAAAATTCCCGCGCTGCTAGGGATCCTCGCCACTCACTCATTA
GATAAACCCGTGCCGGGTCTGAAGAATTTGATGGCTGAAACCTACCCACGCTTGCAACGC
GGACGTATGGCCTGGCTGTTAATGCAGGAAATATCGCAAGGCAATCGTGAGCCGCATGTG
TTGCAGGCATTCCGGGGACTGGAAGGTGACCTGGGCTACGGCATGTTGCTCTCCCGCTAT
GCGCCGGATATGAATCATGTCACAGCCGCACAGTACCAGGCGGCGATGCGTGGCGCGATA
CCTCAGGTTGCGCCGGTATTCTGGAGTTTCCGCATCATGGTGGGCTGTGGTTCCCTGCTG
CTACTGGTGATGCTGATTGCGCTTGTCCAGACGCTGCGTGGCAAAATCGACCAGCATCGC
TGGGTGCTGAAAATGGCGCTCTGGAGTTTGCCGTTGCCGTGGATTGCGATTGAAGCCGGG
TGGTTTATGACCGAGTTTGGTCGTCAGCCGTGGGCGATACAGGACATCTTACCGACATAC
TCCGCGCACTCCGCTTTAACCACAGGACAACTGGCTTTCTCACTGATCATGATCGTAGGG
CTTTACACCCTGTTCTTAATCGCCGAAGTCTACCTGATGCAGAAATATGCCCGTCTGGGG
CCGAGCGCGATGCAGAGTGAACAACCGACGCAGCAACAGGGGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:514
Protein Molecular Weight:56195
Protein Theoretical pI:6
PDB File:1TDJ
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Threonine dehydratase biosynthetic
MADSQPLSGAPEGAEYLRAVLRAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHS
FKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKALIVMPTATADIKVDA
VRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELLQQDAHL
DRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAE
GVAVKRIGDETFRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYI
ALHNIRGERLAHILSGANVNFHGLRYVSERCELGEQREALLAVTIPEEKGSFLKFCQLLG
GRSVTEFNYRFADAKNACIFVGVRLSRGLEERKEILQMLNDGGYSVVDLSDDEMAKLHVR
YMVGGRPSHPLQERLYSFEFPESPGALLRFLNTLGTYWNISLFHYRSHGTDYGRVLAAFE
LGDHEPDFETRLNELGYDCHDETNNPAFRFFLAG
References
External Links:
ResourceLink
Uniprot ID:P04968
Uniprot Name:THD1_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651479
PDB ID:1TDJ
Ecogene ID:EG10493
Ecocyc:EG10493
ColiBase:b3772
Kegg Gene:b3772
EchoBASE ID:EB0488
CCDB:THD1_ECOLI
BacMap:16131630
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
  • Cox, J. L., Cox, B. J., Fidanza, V., Calhoun, D. H. (1987). "The complete nucleotide sequence of the ilvGMEDA cluster of Escherichia coli K-12." Gene 56:185-198. Pubmed: 3315862
  • Daniels, D. L., Plunkett, G. 3rd, Burland, V., Blattner, F. R. (1992). "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Science 257:771-778. Pubmed: 1379743
  • Gallagher, D. T., Gilliland, G. L., Xiao, G., Zondlo, J., Fisher, K. E., Chinchilla, D., Eisenstein, E. (1998). "Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase." Structure 6:465-475. Pubmed: 9562556
  • 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
  • Lawther, R. P., Wek, R. C., Lopes, J. M., Pereira, R., Taillon, B. E., Hatfield, G. W. (1987). "The complete nucleotide sequence of the ilvGMEDA operon of Escherichia coli K-12." Nucleic Acids Res 15:2137-2155. Pubmed: 3550695
  • Lopes, J. M., Lawther, R. P. (1989). "Physical identification of an internal promoter, ilvAp, in the distal portion of the ilvGMEDA operon." Gene 76:255-269. Pubmed: 2473940
  • Wek, R. C., Hatfield, G. W. (1986). "Nucleotide sequence and in vivo expression of the ilvY and ilvC genes in Escherichia coli K12. Transcription from divergent overlapping promoters." J Biol Chem 261:2441-2450. Pubmed: 3003115